ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
|
|---|---|---|
K6WXD3 | MGEGMTGELAMTGGVSMGYGALVPEAFLMGGAILTLLVGSYLPLRRQPIVTVVAVAAAIGSAVAAVVAVVADPMARTVFDGTYALDAASTVIRVAAPLATTVVLLLARADLNGSPRESETVTLLLLATLGTVVLAGAHDVMIVITGYLLATVPLYALIGLRTGRLGAEASLKTYLLGALLGVTLMFGAAVLAAVGGGTAYAQLTAGLGDAPKAAVAIGFVAVLAGLLFKVGAVPGHFWVPDAAQGASVSVAAFLTTVPKLGALVAVARLVALVEPVLRADLAVAAFAAATMVLGTFAAFWQNDVRRLLGWSTVSQAGFLLLPAAAIGTAPKALAPLLVYAVFYAITNLALFSTVAALPDRREIPDWRSAGARHPVLVGVVIAGLLSIVGTPPTLVFVGKISAFTAAAAAGLVWLVVVAVVASVASLFYALRWIAPTVRRADADSTDDRAVPLPAVVALTLGVLVVAGGVAAIPILAADLTLAA | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
EC: 7.1.1.-
Subcellular Location: Cell membrane
Sequence Length: 483
Sequence Mass (Da): 48545
Location Topology: Multi-pass membrane protein
|
A0A6P4ZXP7 | MAASRGKLLEFMMLVGQLKRVPRTGWVLRGVQNVESVADHMYRMAIMAFLLDGEGDLNRDKCIKMALVHDMAESIVGDIAPADGISKEEKHRREKEAMVHLSGLVGGEVGKELYSLWEEYEQESTAEAKAVKDLDKFDMVLQAFEYETLQKRPGQLQDFFNSTRGKFHYPLVKSWMEELNRLRDNDDTDNPLTRIVNPSTKRDPSATSSDVQEENSST | Function: Catalyzes the dephosphorylation of the nucleoside 5'-monophosphates deoxyadenosine monophosphate (dAMP), deoxycytidine monophosphate (dCMP), deoxyguanosine monophosphate (dGMP) and deoxythymidine monophosphate (dTMP).
EC: 3.1.3.89
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + H2O = a 2'-deoxyribonucleoside + phosphate
Sequence Length: 218
Sequence Mass (Da): 24772
|
A0A1Y2FWC8 | GDIINLVGDFDIDSTPSLTVSRLSGLLILHPDILVSSTKVADSAHCARKALLQEITRIVGGSTPSLVYGNMLHELMQACMTEGRWEDEWRESKIDEIVAREVQTLWAMDVQVEKARESMREKSKAFGEFKEMFVGGKQPKPNAFCSDLHSSSSSDARLAITETLSVEEDIWSPKYGLKGKIDVSVSGTLVDGGDVTQQGIARHEGTLPFEIKTGRTSAGMDHRAQTMLYTLLMSDRYDEAISAGLLFYSQSNQVLRVKAARNEIRGLLIARNELATYLHRRMTLSDGTEALWEENGGEQAGEEEDEKQLLPAPIDDERSCKRCYVADACMLFRKAVEGDTEISTDEDAPLQLLYEDKTGFLTEEHTTFFKKWEKLISYEEQELVRFKKEIWTMGAEERMLVGRCLANMSIDTSYRPPESTGDRKMHRYTYRLHHSIPLATQATSSQRAARSLIGGSLTVKDPIVVSLEHPHVLSISRGFVLEITAHHIVLGVDHSLVDNPQAARQLPNSTQAGDLVFRIDKDELAAGMGRIRDNLIQLFVAKGDEKRRRLVVDLEAPEFDDSLVASGSTTRRKLIPSHLNEDQERAVEKVLSARDYALIMGFPGTGKTTTIAEILKALAKAGKSVLLTSYTHSAVDNLLLKVKDTDLSILRLGSRDKIMPALHHLTIDPDNKATSLAQLDHQLMMPQIVATTCLGINDSFLLWCVRNQAARKGGLDVSLFKLLADQHPTAVVELAHQYRMNEDIMYLSNKLVYEDKLKIGSADVATQKLQLPRNEALADEKPWLRGLLAPERAVIFVDTDQLPAREQKKGPLVENEMEACLVTETANALIRCGVAETEVGVIALYRQQIKLITRKLEHLPDVEILTADRSQGRDKSCIIMSLTRSNAEGQIGDLLKDWRRINVCLTRAKSKLIVFGSRSTLASAPLDHLRRFFAAVDEKGWTYTLPKEAGEGLSSPRVQVKREAKEEERVDSSSSPSAPKKIRRGGGALALGGPLSQDVVNSLL | Function: Key enzyme involved in DNA replication and DNA repair. Involved in Okazaki fragments processing by cleaving long flaps that escape FEN1: flaps that are longer than 27 nucleotides are coated by replication protein A complex (RPA), leading to recruit DNA2 which cleaves the flap until it is too short to bind RPA and becomes a substrate for FEN1. Also involved in 5'-end resection of DNA during double-strand break (DSB) repair by mediating the cleavage of 5'-ssDNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
EC: 3.1.-.-
Subcellular Location: Nucleus
Sequence Length: 1004
Sequence Mass (Da): 111565
|
A0A9D8ECL3 | MSESNVLTSIIEGVLEDVEKRARPIKQLQDQLQDAPVLRGAYQSLSKPGMRLIAEVKRASPSKGELAVIEDPQSLSAKYQEGGADLISVLTEERRFKGSIADLISVRSTIKLPVLRKDFIVTEFQIYESRILGADLILLIVAGLSKSQLEDFYQLSIELGMDALVEVHDLQEAEKALAINARIIGVNSRNLKTLEVSDQVFQRILPQLPKSVIKVAESGISSRAQVELVEQLGANAVLIGESLVRAGNPVHTIKELLSR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 259
Sequence Mass (Da): 28431
|
A0A128EAQ1 | MRRDRFKKDTTAKNYYEDRFYVAPQSPKFDVLGSKFEDDLKALDGLVLNSYVEFDQMVVFVDKNDNLKALEKLKEFGYEILSELSGVDFIHQRGGIEVFYQLLSIKHKRRARVKCFVKNGEFLQSATSLYKSANWAERELYDMMGVWIENHPNLKRILMPDDWYGHPLLKSYPLHGDEAAKWYEVDKIFGREYRDIVGEENRDSAFIDSKDTFNFSRIYHETEYGGVEPSEAYLQEYQEKGGVPFIKHATRDKFKILKKRR | Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 261
Sequence Mass (Da): 30880
|
A0A7V1CK51 | MMKVAIIGASSLTGNKLIEILAKHPKADVAFAFSKNYAGQNVSSLYPENESDITYVSFDEDKIAQCDVIFSCLPHGKSMLILPTLTSPEKLIIDLGADFRIPADVFKKWYDEEHKAKKQTPATYGLSEIFAGEIKESKFIANPGCYPTTVLLALAPLLKQNIELKNIGVYSLSGRSGAGRDNAKQYATEGENVFSYKDPYNHQHIGEMEYVGSMIGAGPLKLYYFSPHVVTNIYQGMHTTLTASCELESAQSLLSIYESFYSEQPFVSVKKVSGQKLNLNSVVNKNDCLIGLDYDKVTKRLYIISIIDNLVKGASGQAIQNMNLALGFEQTLGLKED | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.38
Subcellular Location: Cytoplasm
Sequence Length: 337
Sequence Mass (Da): 37156
|
A0A7V5C227 | MSRYVEVVDAEALRERAAQLGEAIAADYGARRPLVVAVLKGAVPFLIDLTRHLPPDIEIDFLSLTRFGTQGRVGIALDVSVPVAGRDVLVVEDIVDTGLTLATLRRIFTARGARSVRTVALLDKRPRRIVDVPVEYRGFEVGDEFLLGYGLDWQGRYRNLPSIWAVMDFPAFRDDPKTFDALVFPTAARSQRSRP | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 195
Sequence Mass (Da): 21708
|
A0A965KHP1 | LGTNLRTFVHVTGGGLAENTARVIPVGLCATYDRSTWALPVEMLFMAKAGDVAQSALERTWNAGVGMVAVVAPEVADLTLRSLAARGMKAWIAGEVRSNEASARSTLEGTYQAR | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 114
Sequence Mass (Da): 12050
|
A0A966BGN3 | MTSTNEDKAKQLPPASGAWHIGLPAGDRNFFELSPDRPYIFEGGGVVHRPVVAYETWGTLDATASNAILLCHALTGDAHAYGTEGPGQPTPGWWNDFIGPGKPLDTDRHFIVCANVLGGCQGSSGPSSIDPVSGKRYGIDFPTLTVRDVVRSQRALGLSLGISKWLSVVGGSMGGMQALEWTTSFPSSVRSLVVIASTAAASAQQIAWSSAGRHAIIDDPGWQLGQYYDSEPGEGPAVGLANARRIAFIHYRSDEEFNRRFDRFSNESLEPFRLDHRFDIESYLDYQALKMPWRFDANTYLLLNKMMDLHDVGRGRGGVEKALTRIESPALIMSVRTDCLYPRDQQMRIVDALKNQVHVEHVDIDSDNGHDGFLTEPEQTGEPMKEFITRVEKDSLT | Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1.
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine.
Catalytic Activity: acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine
EC: 2.3.1.31
Subcellular Location: Cytoplasm
Sequence Length: 397
Sequence Mass (Da): 43726
|
A0A966YJ15 | SVAGAYWRGDVTRPMLQRIYGTAWADKKALKTHLQMLAEAEKRDHRRLAAELDLVSWPDELGPGLAVWHPKGALIRKIMEDYSRDRHENGGYDFVFSPHIAKSVLWETSGHLDFYADGMYPPMEMDGATYYPKPMNCPFHVMIYKSNQRSYRELPVRLFELGAVYRYELSGAVHGLMRSRGFTQDDSHIFTTREDIQSELMSLLDFVLSVLRAFGFEDFQAKLSTRPPEKSVGEDELWDEATEGLRAALDRSGLDYITDEGGGAFYGPKIDVDVKDAIGRAWQLSTIQLDFNLPERFDLEYIASDGERKRPVMIHRALMGSVERFFGVLIEHYAGAFPAWLAPTQVRILPVAEVHADHAHDVAARLRSSGFRVDVVGAVEQLGKRVRNGKIEKLPYILVVGDDDVANDTVGVNKRGHDTPERDVTVDDFIARLGDDVENKV | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-threonyl-tRNA(Thr)
EC: 6.1.1.3
Subcellular Location: Cytoplasm
Sequence Length: 441
Sequence Mass (Da): 49845
|
A0A938EHW6 | MVLALYRRYRPDTLLTVIGQEHVTEPLARAIDSGKVHHAYLFNGPRGCGKTSTARIMARSLNCEKGPTSNPCGKCESCIALAPGGAGTVDVVEIDAATHGGVDDARELREQVGYVPIKDKYKIYIIDEAHQLSTSANNAMLKMIEEPPSHLRFIFATTEPEKMLGTIRSRTHNYAFRLVNREVLAKHLAEICKRENIKCDDAALKAIATASGGSVRDALSLLGQFSAGMDEKGLSTEYVEWQLGLTPLGILDELGNSVLENDLAKALEVIRNACTQGIEPHRLLSDFLNYLGIRIREADTNDRDAMSILVTAATSVSVSLSQLKSSSNPELSLDLAIARLFVQPATQIQTNAPKQSEPVTKTEVKPVEKKLEKPQPVKAVVKKDITDVADLEVRWKDIMGELSRVSRVAWLAYMDSKPLELNQTVLVVGLKDASKLMIASEMKHIENLKNVLVSAVSLNVSIEFKHMELTNTEEFDQPNTNDESVEYKDGLSVAMEALGAVKIHEFENGGN | Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity.
EC: 2.7.7.7
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Length: 511
Sequence Mass (Da): 56089
|
A0A9C8C3U0 | MFESGDKVLVAVSGGQDSVLLLHFLIQLKDVFDLSLHIFHLNHMLRGDDSYKDAVFVRDLAEKENLSSTILSYNVPDYIAKKNLSTEEGARKVRYMLLEKVAKDINADKVALGHTADDQVETFLMRILRGSGLKGLSAIPPVRGVFVRPLIEITRKEIESYCKSEGIDFRVDISNFDSTYLRNRVRRDLIPVLEQYNPDLRDTIFQTIRVVSDDNQYLDEIASKEFYSVSAIKNDLISFSLKKLKALPVAVKRRVLRKGIEILKGNLEGIEFKHLKDLLLDAEKMPKFRRDIPGNLAIIREYDNLILIRRNLLEKKKRVEVTLDGLGRIEIPELKVELKASIMKLEGDNFAGERFLKNKFLPSSKINLVAYFDADKIDFPISICNRSRGGRFYPLGLEGEKKLQDFFVDVKLPERLRDSVPIVTSFDGEIIWVVGYRIDDRFKVDCKTQRVLEIKAKFKNNM | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 462
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 53077
|
A0A938J0K7 | MSDLPSEPPRRRVRPRTPAGRARTVDRLLSEEYPDAVCELDHRNAFELLAATILSAQCTDARVNLVTPALFERYPDAAALAVADPEQVEEMIHSTGFYRSKAKNLIGMAAGLIDRFDGEVPTRVEDLTSLPGVGRKTANVVRSVALGLPGLPVDTHVLRLSRLLHLTSSEDPVRVEHELNPMVPAMGRGDFSLRLILHGRRVCVARRPDCGRCVLAWMCPSAGP | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
EC: 4.2.99.18
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Length: 224
Sequence Mass (Da): 24575
|
A0A960GE96 | MTDTLTSLSDIGVSIWLDDLDRGRLAGGGLADLIADSHVVGVTTNPSIFDHSITTGSAAYAEQIRDLAVRGVDVGEAVRALTAYDVRWACDLFTPTFEATSGSDGRVSIEVDPRLASDTAATIAEAKALWWLVDRPNLLVKIPATEEGLPAI | Pathway: Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3.
Function: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
Catalytic Activity: D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-phosphate
EC: 2.2.1.2
Subcellular Location: Cytoplasm
Sequence Length: 152
Sequence Mass (Da): 16096
|
A0A2G9ZDG2 | MKKISEIRKSFFGDKYVIFAPKRGLRPHKISEEDAKRKEQFKENCFFCPGPDEDKAVYKIDVGGKWLVKVVENKFPALSLTNKKAYGKQEIVIDTPNHGEDFCDLSPEHIRTVVDVYAARIKAINELENINYVQVFKNDGGKAGASIPHAHSQIIGLEYIPHHMMADTMAMDKYCCENGSCAYCDIIKKELKEKERIVFDDDNVVALCPWASSSPYALWVLPKAHKNKLEDLTPEERLSIAKALKIATSRLDTEEIPYNFFIHDSLPHNDHHFRLKIASRMNVWGGFEIGSGVIINPVFPEDAADFYKK | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 309
Sequence Mass (Da): 35206
|
A0A945SWS3 | MSPTLYFLTGPTASGKTALSLRLAMELDAEIISCDSLQIYEGMDIGTAKPTSDELSAVVHHGIGVFPVNRGVSVHDFSLLASAAVEDIHNRGKSVLVTGGSGFYLKSFLEPIIDDIVISRETRSVVNSLYENSGLASVVARLQELNPNGVGGLDIQNPRRVIRALERCLQSGDSVLQLRANLATLPEPYAGIEKRLCVIQREDNTLRKRIEQRTREMLNAGLVEEVRELITLGLLDNKSASASIGYRETIAFINGTLESELDETINLHTWQLVRKQRKWFRKELSNSRAVNLDFFAEPSLKHVFG | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 305
Sequence Mass (Da): 33719
|
A0A972HCG3 | GIPDELPLTEESKLSAINPYGRTKLMLEEIFEDVAASEPGWNIILLRYFNPIGAHSSGLIGEDPAGIPNNLLPFVAQVAVGRLDKLKVFGNDWPTRDGTPIRDYIHVADLATGHVAALAKLAENPGVVVYNLGTGDGVTVLEVVAAFEEATGVEIPYEFVGRRDGDAAEAWADASKAERELGWKATRTLVQGCADSWNWQSNNPHGFRDPE | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.2
Catalytic Activity: UDP-alpha-D-glucose = UDP-alpha-D-galactose
Sequence Length: 211
Sequence Mass (Da): 22850
|
A0A424RSS6 | MIQKIMFMNGYGVFVWFSFAITFVSCAIIYIKTLRTLKKYENEFAKELNKLSVSERKIVLKKSKVASQVFASYNKSF | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 77
Sequence Mass (Da): 9004
Location Topology: Single-pass membrane protein
|
A0A962NED3 | MESLLLLWRESGLALMTPGQAVMLLVGLVLLYLAISKKFEPLLLLPISVGTLLANMPGAGFEAAPVYDAAGHLLSPGG | Function: Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
Catalytic Activity: H(+) + 2 Na(+)(in) + oxaloacetate = CO2 + 2 Na(+)(out) + pyruvate
EC: 7.2.4.2
Subcellular Location: Cell membrane
Sequence Length: 78
Sequence Mass (Da): 8132
Location Topology: Multi-pass membrane protein
|
A0A1F2TP85 | MSYQNHDQSSADPHNSFFRKIFPVGLQDALFIFLASYLFVVFFLWVGGELVANKDAETVDLAVPSLATTMQRLIRSDTGWYLTIINDGYERKPFSVEKQANWAFFPAYPLIVKYAAKIFSADIIFVGCILSTLSYFFSLYMLWQLFALDFDRETTVRSLLLIVFYPFAFGLVAFGPDSLFLLTICLSLYCARKERWLLAGLIAGITSATRPQGVLIGVPLLYMYLRRCGFSWKRIDIRCLALALVPSGLLLFMFHLRQITGNPLAFMEIQFTWNNSVTYPFYFLERYMEAPQLIGHYGWDPEFLSVLFVLSLIPVILWSWLPGRMPTEYRLFLILQFLVLVSRETTMGNLRYMMAIFPYFLALGVLGGNPAFFRLILLFFAGLAGLMVALFANNYHIATF | Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 400
Sequence Mass (Da): 45899
Location Topology: Multi-pass membrane protein
|
A0A835BU99 | MSSRDVNDDDYYTSDDDYEYDYDDDGDVSDDDDPQPMETNDDDDDAELSTKEKGYDFETEDDVRRTSGSPTRGGAVGLLTTSPAGRHAITVPTALNDMPLTCAICFDAYAPGEMRSAGCSHYYCHGCWRGYVHVAVTDAGSGCLLLRCPDPPCRVPVVRELVDAVATGADRARYATFVVRSFVEEGTSRYVRWCPGPGCTLAVRSRPGSGAYEVTCRCNHVFCFRCGDEAHRPSSCDTTRAWVVKSTSEGETAKWVLANTKHCPKCKRAIEKNLGCNHMTCGAPCKHEFCWICLGSWKGHAGGYYRCNVYMANPSEFDEETTRREQAKASLERYLHYYERWCAHGASMKKARQDLDGLQGGGLDRVAEEMGRQPTEMDFLLEAYAQIVEARRVLRWTYAYVYYLDPERDEVKRRFCEYLQGVAE | Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
EC: 2.3.2.31
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Length: 424
Sequence Mass (Da): 47683
|
A0A960EJN2 | MSTPSVVLNEVAEQLHGDVPNLPLRMLNEFVYCPRLFYLEWVLGEWDANLDTDQGSFVHRNIVEAASHRKGPAQPDERPEVTRSIHLESNELALVGVADIVEISRSTAIPVEYKKGTAKRGQDGYELWPSDKVQLGGQMLLLEAAGFDVPEGFVWFDAIKRRVALPMTDDLREWVTGQIAAARRTAAGELPAPLVDSPKCPRCSLVTICLPGEHEVLADQSDARPWPRRLVPRVDETKPLLVTQPGSRVGVSGGRLVVHPKGEPDVSFRLIDISYVGLFTGVEISQAAITRLSSRGVPVVWMTRTGKLRAFTQNEWSKNIVLRQSQFGTSDAKRLGIARKMVAGKIRNSRVMIRRNSDVKPAATLRRLAALAEKAERAASFAELLGLEGAAARTYFSSFADMLRPDWAAESFRSVGRKRRPPPEPVNAALSFAYGLLAKELVLAATVVGLDPYLGVYHRPRFGRPALALDLCEEFRPLVADSVVVRAFNTGELTADDFVGGLGRSGFTQAGMRRFLNSYERRVNETVTHPVFGYKATYRRIFETQARVLGAVLMGEFDEYAPMVTR | Function: CRISPR (clustered regularly interspaced short palindromic repeat), is an adaptive immune system that provides protection against mobile genetic elements (viruses, transposable elements and conjugative plasmids). CRISPR clusters contain spacers, sequences complementary to antecedent mobile elements, and target invading nucleic acids. CRISPR clusters are transcribed and processed into CRISPR RNA (crRNA). Acts as a dsDNA endonuclease. Involved in the integration of spacer DNA into the CRISPR cassette.
EC: 3.1.-.-
Catalytic Activity: exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 3'-phosphates.
Sequence Length: 566
Sequence Mass (Da): 62680
|
A0A0R2D1B5 | MNNIEQALTDLKAGKLIVVADDPDREGEGDLLGVAEYATPETVNTMITLARGLVCVPMTEEWAERQGLDRMTDVNNDAFGTPFLVSADARTTSTGISAFDRADTIKQMADPKSTFADFYHPGHVFPLHAAVGGLKERDGHTEAGVALAELTSDSPVAYICEIIKPDGHMAKGQELVDFSDEHGFTMITIDDLIAYLNQQN | Cofactor: Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
Function: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate.
EC: 4.1.99.12
Catalytic Activity: D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)
Sequence Length: 200
Sequence Mass (Da): 21672
|
A0A2M6ZZQ2 | MKILCLDVGEKRIGLAASDALGITVNAIGTITRTTKQKDFSEILRYLSENNAEKLVIGLPLNEEGEIGVSAKKILKFVKELKGFLHNKKHDMPVETWDERYSTAEAEAYLIGFDVSRKKRKKVIDKMAAVMILRSYMEANS | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 141
Sequence Mass (Da): 15848
|
A0A2K9LV96 | MFGSEEVNEGAIRESLGKQAELCRMKHEAAQKTIELKTPNVERFVAVDMALSALSQFRRDNNQIFLAIVFFVCALTAALTHHHIGLRPMQTVMDYRFGITAQLIAHVSLTYSSYSYLNNGWASGTLIQNEHVRWFYLFGFGALALVSLFQLFTIPKTAKPGGSIGKALLSVPLFAYMAISSARFFIFETGNPQGMVLFVDKIMDQASLFLNIGLYIWVGMLLKQTYLGEYIFRIFKPWKLPPELLAFVAVVIMAVPTAYTGASGIIIIAMGAVVYAELRRVGARRNLALAATAMSGSLGVVLRPCLLVLLIAMLNKEVTTDMMYGWGVKVFMLTSFLFFLVSLVAKQGPMKIAPISEALSPSLRAFQPLVPYVLIFVVTAAAYAFLLDAHLDEHTAPVVLPMIILLLLVYEFVVKNTKKLLPWLLLLVIPTATFMYQQDGLMTAAILPLLLLLVLVLESKVKHSPDEDKHETYEGEERATSLENSVRRATTDTTVHIGALLSIMALSLTVGGVIEDSGIFEEVAAQSDFFGNIWTAMIALVIVLVIIGMIMDPFGAIVLVSGTVAQAAYSQGIDPLHFWMITLVAFELGYLSPPVAVNHLLTRQVVGEEEIEKAKEDTRGKSFWIRHERYVLPLTVMGIALVLVAFGPLVYQQYF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 655
Sequence Mass (Da): 72425
Location Topology: Multi-pass membrane protein
|
A0A962NDT8 | AATMSKVAIPQMRQRGYSDSLASGSVAAAGVLGMLIPPSVPLMIYGLIADQDIRKLFIAVMIPGVLVALSFIGAIILFAIFRPADLPAGGANKSLREKLASLKGVIWTLVMFAVVIGGMYGGIFTVTEAAGIGCTSAFFIALIRRGMGFKDIVSCAVDAGKTTGMLFMIVFGAMVFANFVNLSGFAYLLGEWVRSLGLGPMGILLAIALIYILLGCVLETLGLILLTVPIFLPIVTDFGVHPIWFGIFLIMMVEFGQLTPPVGLNVLTVKSVVNDIPTGKIFIGVTPFLIANLLIVALIILFPEIVLAPTNWF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 313
Sequence Mass (Da): 33199
Location Topology: Multi-pass membrane protein
|
A0A662ZJM7 | MSTVDNVNGSDLTARIHSIETGGAVDGPGIRYIVFFQGCQFKCIYCHNRDTWDFKGGEEVTVKKLMDEIVTYAPFFRASGGGVTASGGEASMQAKFVAELFRQVHAAGFNTCLDTNGGIRNYNKDVENLINETDTFLLDLKCMDDDLHREITGRSNSDTLAFARYLAAHNKKMWIRLVVVPTYTDSEDNARRMGEFVKELGDAVERVELLPYHEMGKHKWAFFNDPYKLNDIHPPKAEDMKRLKDILKEYHKEVY | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
EC: 1.97.1.4
Catalytic Activity: glycyl-[formate C-acetyltransferase] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[formate C-acetyltransferase] + H(+) + L-methionine + semiquinone [flavodoxin]
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 28993
|
A0A938G3A6 | MTTQPSAVRPLQPWKLTTAQRFSRFATVIAVVAVAALLVLVSPLAGLAGIALVAIPLQVAVSVARSGRHGSVAARNDVATSLIGSAFLILMAPWLSILYTVVRRGYEAISWNFLTDDMRVTAPDAELGTGGIAHAIVGTGVMVLVATAVSVPLGILSGVYITEIRGRFTKLVRFIVQAMSGVPSIVAGLFIYSTLVIYNKSYSGFAGALALAVLMIPTVARTAEEVLKLVPEELRFAGYALGSTQASNVFRIVLPTVRSGLVTSAILGVARVAGETAPLLMTAQIFLATKGNPFDGPLASLPIVTFSFFQNGADNAVTRAWGTSMVLLVLISLLFALARAVSADRRRSRR | Function: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane.
Subcellular Location: Cell membrane
Sequence Length: 350
Sequence Mass (Da): 36882
Location Topology: Multi-pass membrane protein
|
A0A2E9RTD5 | MGRTIIIGAGLCGLVAARTCSSEGGVLVLEAGSCPGGMIRSERRDGYLLEHGPNTLALRAGHATDYLEQIGLLEDTIEANPEANKRFIVRGGQPVAVPTSASSFVTSSLFSPLGKLRILVEPLLPRGSARKKESVADFFMRRLGREVRDYAANPFIAGVYAARPETLVLRHAFPAIYEIESKHRSLMLGGIKTAKKRKREGLPKTRLVSFKEGLVGLPNRLAEELGDDLRLNALVRKISRDGDNWKVVFEEAGELKEERANRITCSVPAHALESIEWQGLSEGDSLKTLASASHYPVAVVHLGFLRKDVLHPLDGFGFLVPEKENLRILGTLFSSTLFPERAPKGHVLLTTFVGGERQPDVTEKSDEELYELVRKELQGLLELRATPTFRNLVRWPKAIPLPDSGKDDRLAAAKRLINANPGLILNGSHLTGVSLPACLEGTESLLSKNG | Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
EC: 1.3.3.15
Subcellular Location: Cytoplasm
Sequence Length: 450
Sequence Mass (Da): 49124
|
A0A2M6ZYQ5 | MAGSIPTLSAKIGAADLENGMRKWKIKVSVIYMNKKFQQLPSVSEVLKHTSIHGFIETKGHSLVVYAIRKSIQFARSNIDFHAQTRGTKKQTDLINLIVSKTIELIHAISGNNLKPVINATGIILHTNLGRAPLGEKAIHDALEVMSGYSNLEFDLKTGKRGKRSDHITDILKYLTGAEDAIVVNNNAAAIILALNTLAKDKEVIISRGELIEIGDSFRIPDIIKAADVKMVEVGTTNKTNLSDYEKAISNKTGLIIKVHQSNYIIKGFTKEVSIADLAKLAHSKKLPLIYDIGSGLLRRHEKTSSQSEPDVKSAIASGADLVMFSCDKLLGGPQAGIIVGKTKFIGKLAKAPLMRALRVGKLTLITLINACRYYLEENSLIDNNPVFLMLEKDSNYLLKSAEELAGLLKKEKINCSVEETKGACGGGSLPEMKLKSYSVVFGNSHSSPKNKETLTEHVFHNLLNMDRPIIPVLKKGKLYFDMLTIGKKDISYIASSIVHHCKSYSQHSNDNRLTTNDEL | Pathway: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1.
Function: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Catalytic Activity: H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate
EC: 2.9.1.1
Subcellular Location: Cytoplasm
Sequence Length: 520
Sequence Mass (Da): 57125
|
A0A2M7DT34 | MKLDTNEIKTLVRDAIEEDVGSGDITSRNLIPPTEEATARIIARSNGIVSGLAVARQVFKTLDRKCIWRAKLSDGDSVRKGRSIAIVKGLARAILAGERTALNFLQHMSGIATLTHRFVRKARYTETRIYDTRKTLPGLRVIEKYAVKCGGGYSFRKALYDMVLIKNNHLKICKQLGLPLDHVVRNLRIKVPRGIDIEIEARTIREVELGIRADMDIIMLDNMDYNTIKKAISIIRKSGKPIEVEVSGGINLKNVEKIAKFKIDRISVGALTHSAPVLDVALEIISVD | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from quinolinate: step 1/1.
Function: Involved in the catabolism of quinolinic acid (QA).
EC: 2.4.2.19
Sequence Length: 288
Sequence Mass (Da): 32079
|
A0A3D2HJB8 | MMLKIDVLTLFPKMLDGFVTESIVGRALREQLFSLQVRNLRDWAEGPHYQVDDRPFGGGAGMVLQFDVLSKAIKSLRKEKTHVVYLCPDGMPLTMKKVRELTQKEHVVLVSGHYESVDERFREQYVDEEISIGDYVLTNGTLPAAVVIDAMVRCLPGALGDEQSLEQDSFRDGLLSFPQYTRPKEHEGKGVPSILFSGDHAAIAKWRLEQQIKRTIRRRPDLIFN | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 225
Sequence Mass (Da): 25601
|
A0A3D2KPB1 | MAIFPKQPTIEVDLERILLTNEQIQTRLKELGATITAYYRQRDVNTITLVCITNGSIVFVADLMRYFDMHVRLDSMRISSYLEGTSASRKPQLAADISLDIRNEHVLVLDDILDTGHTLTKVLDVLGGKAPASVEVCVLLDKKERREVPIQANFVGFEIPNAFVVGYGLDFDQKYRNLACIGVLKH | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 186
Sequence Mass (Da): 20923
|
A0A931FKK4 | MFGDIGGSEVILIMVVILIFFGANKIPELARGLGKGIREFKDASTEIRREFEQAGQPAQPNNYAQQNNNYPPQQQYGAQNQYPAPLPVADAEPASGFDPWATPAYVAPTTAAAATAAADEAFTHKTEEPAPPVASQLPPNLAPEGTQPRQPYIPANASPSADA | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 163
Sequence Mass (Da): 17272
Location Topology: Single-pass membrane protein
|
A0A077LZ31 | MLRWLTAGESHGPALLATIEGVPAGVEVTTSELAAALARRRLGFGRGARMKFEQDEVELLGGVRHGATMGSPIAIRIGNSEWPKWRTVMAADPVTEEAYAAANDVGAPQEVGRNRPLTRPRPGHADLVGMQKYGFDDARPVLERASARETAARVALGEVAARLLRQAYGIRLVSHTVAIGTAGVSDDAPLPTPDDVERLDADPVRTLDAQGSAAMVAEVEAARKDGDTLGGVVEVCAYGLPPGLGSHVHWDRRLDARLAGALMGIQAIKGVEVGDGFRTAARRGSAAHDEMERDATGAIQRRTGRSGGTEGGMSTGGVLRVRAAMKPISTVPRSLDTVDVASAEPAKAIHQRSDVCAVPAAGVVAEAMVALVLAEACLEKFGGDSVAETARNHAAYLAAIPEGMRTW | Cofactor: Reduced FMN (FMNH(2)).
Pathway: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 7/7.
Function: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
EC: 4.2.3.5
Catalytic Activity: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate + phosphate
Sequence Length: 407
Sequence Mass (Da): 42601
|
A0A963SDV5 | IEPTRIYVKSLLAPIRSGKIAALAHITGGGLLENIPRVLPKGAHAVVDAGAWEQPRLMAFLQAQGNIEPEEMARTFNCGVGMVLAVAETDVAEVTGMLEAAGEIVLRVGTIETGERGCTVRGAAGTWSAKGDWEATHLA | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.
EC: 6.3.3.1
Catalytic Activity: 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ATP = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + ADP + H(+) + phosphate
Sequence Length: 139
Sequence Mass (Da): 14573
|
A0A4V2DZR8 | MISLQQLSNKVVVIVGATASGKSQYAMGIAQQLNGVIINADSMQVYRNIPILTAQPSVQDTQLVSHMLYGIKQCDEYFSVGMWLELVKSSIIKVQASGKVPIIVGGSGLYIKALVYGFVYTPVISAGTKAYLSSVCAGLSLDCDRAAYNKSLHELLKDCDEESYQKLKVNDEQRILRALAVYHETGIPLSKWHTMNEKWLNRDQFYVVLIQKDRDELYRRCDARFVEMLNIGALEEAQYVLASFEKYPKVLGLFELMEYVSGKMSLADSTSQAQQKIRNYAKRQLTWFRHQIDYDEVIR | Function: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
EC: 2.5.1.75
Catalytic Activity: adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA
Sequence Length: 299
Sequence Mass (Da): 33908
|
A0A932AMT5 | MRIAVLVSGTGTILDALLGQGLPVVAVLADRPCAALDRAERAGVESVLVERTSFGPSFDRDAYSGRLAATLQERTVDLVVMAGFGTILGPSMHGVYGGRILNTHPALLPAFPGWHAVADALAYGVKVSGCTVHVAGLEVDTGPILAQEAVPVLPGDTVETLHERIKQVERRLYPRTIREIVERGSVLPEADAPARHYDGDDRNDRDDRDENHEEAHAT | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 218
Sequence Mass (Da): 23371
|
A0A350R0U7 | MQGCFLFPASLPSPLAFFPLNLLLLDKRFSSLFLAKDDPRTVHLLEVLKVQEGDEIDLAVRNGPKGKGIVSLPGEGAIKLEIRWLEPHPRDLHPVRLILGLARPQTCRKILEQASALGVERMAFFEAEKGEPSYAHSSLWQTHEWMERIDRGIEQSFSSFIPSCTVYSSLEETLVSEMTDRNPQKFALDNYESPEPLSAVGIERGSPVLLALGPERGWSAAERELLRSVNFEFRHLGERVLRLETAAVAALGIVLASYWREDSESW | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 266
Sequence Mass (Da): 29909
|
A0A9E2QAX7 | MVNRQLRRVQEKSRKSAKKKRAAAQKKKAADRKRGEKKRFWNTVIQFLKDVRIEMKKVIWPSKEEVVNYTIVVLITVTIVTTFILVLDLMLSKLLALIIT | Function: Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Location: Cell membrane
Sequence Length: 100
Sequence Mass (Da): 11738
Location Topology: Single-pass membrane protein
|
A0A432UUQ8 | CELPVIRKDFIIDPYQVYEARVIEADCILLIVAALNDDQLAELTQLAQELGMDVLMEVHDAPELERALETEVRLIGINNRDLRSFETRLETTLELLDKVPDDRLLVTESGLLTREDVEKMRTAHVHAFLVGEAFMRAANPGKALHELFYR | Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Length: 150
Sequence Mass (Da): 17144
|
A0A848SMB9 | MQSEDFRNECNRLTGAPITAGKQLGLAVSGGPDSLAMLLLAHGAFPGAIAAATVDHGLRPEAAGEAEYVASLCADLDVPHAILTPAAPIEGNLQSEARKARYALLENWRAGNDLAWVATAHHADDQLETQLMRLMRGSGIDGLSAIRPVNDHVIRPLLNVRKAELETYLAKRGIEAAHDAGNEDTQFDRVRIRQMLADLPGYDPSRIAQSAAALREASEALKWVVRREAGKVVEDRGDAVSLLEIAYPPELLRRLVQLCLEEIEPGIAPRGEALDRFIDTLRSGRKARIGAILGETQDEDGSSSWRFTLAPPRKTG | Function: Ligates lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine.
Catalytic Activity: ATP + cytidine(34) in tRNA(Ile2) + L-lysine = AMP + diphosphate + H(+) + lysidine(34) in tRNA(Ile2)
EC: 6.3.4.19
Subcellular Location: Cytoplasm
Sequence Length: 316
Domain: The N-terminal region contains the highly conserved SGGXDS motif, predicted to be a P-loop motif involved in ATP binding.
Sequence Mass (Da): 34226
|
A0A938VS93 | MTKVPESPVLDAMRGPYEPGPVEARWYPIWEACGYFQPSQDPARRPFVIAIPPPNITGVLHHGQAMFVAYQDFLIRWQRMRGRAALWIPGTDHAAIATQNVLERLLQQEGTSRLAIGREKFVERFWAWKAHVGATINQQFRRLGASLDWTREHFTLDPDLSRAVREAFVRLYERGRIYRGRYLVNWCPADRSAISDLEVEYAEVTGHLWSLRYPLKGGGHITVATTRPETMLGDTAIAVHPDDARYRRLIGATAVVPGIGREIAIVADAAVDQAFGTGAVKVTPGHDPNDWAIAQRHGLPAVNILNADGTLNEHAGRWAGLDRFVARKNYLEYLDAEGLVERVQEFRHNVGHCSRDGAVIEPLLSEQWFVDVKPMAQKAAAAVQDGRITFFPERFAAEFLRWMDGIQPWCISRQLWLGHRIPVWYCGVCSQQIVARTDPSTCPRCNATTLTQDPDVLDTWFSSGLWPFSILGWPDDTPDLCRFYPTDVLETGYDIIFFWVARMVMLGLELTDNTPFRTVYLHGLMRHADGSKISKSNYRPGDNPIDVIDAHGADALRFMVLTGGSPGSDMRLVLERVAEAGHFGNKLWNAAKFVIGAMERTRAAGVEPAASTTVDRWILGRLDEAIADTTRLVESYQIGEAGRALYDFLWREVFDWYIEAAKIRLYAEDAAAARRVAQTLETILDAALRLLHPFLPFITEEVWHHFRRAGGAPDGPEHLIVAPLPDAVGERSRADMARVAALIEIVQGIRNARHESGVEPGRYVEAHIVGAANDGGLQAESEFIARLGRVSPLHFHAAAPALVGPAVTVRAGGVEVFLPLAGMVDVVAELARLRKERDTAQADVTRAEALLDNASFAARAPAAVVDREREKAAEARARLAQLDARIGALSR | Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Catalytic Activity: ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
EC: 6.1.1.9
Subcellular Location: Cytoplasm
Sequence Length: 891
Domain: The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Sequence Mass (Da): 99030
|
A0A938EPJ4 | MRRSDDDTQPIPVTGAPEVDARTPGAGRHAAPRVRRSLGSWALVIAREAGIVAAIVVAAVILARLIVGPIAYVSDDAMEPSIAAGSRVLVTSWGETAAGDLVLVRSPDAWASPTGTSVARVIAVGGQQVVCCDDSGRITVDGVALEEPYRSGPTDQVTFDVSVPDGRVFVLADRRGTARDSRALLPVEGGSLPTSDIVGRVVVVLWPPRGFIG | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 213
Sequence Mass (Da): 22125
Location Topology: Single-pass type II membrane protein
|
A0A9D8FD92 | MISVHNPAEVSSALRGPRREARLIGFVPTMGALHLGHRALIERARQECDVVVVSIFVNPLQFENSEDLMRYPATLAADLEMCESTEVDIVYRPTTSTMYPNGFDCRVDVGRIGQVLEGRSRAGHYDGVATVVTKLLNVVCPDRVYFGQKDYQQTLVVRRLVRDLELDVELVVVPTVREGNGLALSSRNALLSAEARSRAVIISKAIELAESRYAAGETEAGELLSDAISSIEDAGLVVDYVTIADPETLVPQDIVRVGDIILVAATIDGIRLIDNAILGA | Pathway: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-pantothenate from (R)-pantoate and beta-alanine: step 1/1.
Function: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate.
Catalytic Activity: (R)-pantoate + ATP + beta-alanine = (R)-pantothenate + AMP + diphosphate + H(+)
EC: 6.3.2.1
Subcellular Location: Cytoplasm
Sequence Length: 280
Sequence Mass (Da): 30457
|
A0A2H9L7D2 | MKLKQLDVSKLDFKKLGGLIPAIAQNAETGEVLTLAFMDEPALRKTIETGYMNYYSRTRKKLWKKGEESGNVQKALEVYPDCDSDTLLFMVEQAHDIACHDGTRNCFRTDRFSLERLFQIIKERRDNPKKLSLSYTSKLLKDKTLMREKIMEEAGEVVKASVKEGMERIIYEAGDLLYHLLVLLAGEGIELREVIEELARRRK | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
Catalytic Activity: 1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide
Subcellular Location: Cytoplasm
Sequence Length: 203
Sequence Mass (Da): 23419
|
A0A0J5Q7H4 | MIVLLLIFAAAITIGVPIAIGMGLAGASWILFFEGLEGSILIRRMYGILSSFPLLAIPLFSMIGLLAERSGMLPEMVKWLQMILGRVRGGVAYINVAASVIMGGVSGTAVSDVAALGRMEIRMMTQAGYSRPYAAALTAATAVIAPIIPPSVAMVIFGLAAGGISIGGLFVAGVIPGLLMGAGLAFMVWSTARAAGEEVLASRPAPRDVILQTLRILPFLLLPVIVVGGIVTGVFTITESAAIGTVYTMVVGLVVTRTLRLRDVYDAMVYSAIISSVVGLLMGTGAIVSWILTRNRVTLYLAEMIGNFTDQATVFLALVAVVLLVLGTVMEATALIIAAAPILVPIARQYGIDDFQFGLVFVLSCMVGMITPPVGILLYMTATIAEIPLEQVFRATLRYALSAMALIGLLILVPQLTTWLPDQFGF | Function: Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Location: Cell inner membrane
Sequence Length: 426
Sequence Mass (Da): 44838
Location Topology: Multi-pass membrane protein
|
A0A432UVJ9 | MKIQKGAFVTDKRPVFLNLRKIKLPLPGLVSFLHRVSGVILFFAIPLCLFVLQQSLVSPSGFAAADEFLSNPLIVFMVFVLLLALSHHLLAGIRFLLMDLETGLTKAISIQSSRAVLIGAVVLALLLTIGLYQ | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Subcellular Location: Membrane
Sequence Length: 133
Sequence Mass (Da): 14529
Location Topology: Multi-pass membrane protein
|
A0A965FDI3 | MPESEKFTATYKPITNADGKERDFTLNVPNSRKFVQFRVAYKTFYGDKIVERVTKHQIAIEAAIIATASQFGEEEMTSVEGRAKLAEALRDAMNDVLIRNEDFGGIDEVMFTHFVFQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 117
Sequence Mass (Da): 13330
Location Topology: Single-pass membrane protein
|
A0A8T2B7E6 | MCLSLCVSIAVCDMVLIHVHQCSCSSHLIPKLYRWNVLSTLISLSHMPEYIQIYKKKSVEGVKPDRHLLMLIKCSLWVLYGLPVVHKDSILVTTSNGVGFVIEVIYVVVFCISCDDQSRTDVVYVKLYLEFCFVVVSYANTIWAIGSLVAKHTLIGIVCNLFNISIYVSFAKEKMVETKTFKSMPFRLSLLSFINAGLWTAYSLIYKIDIYVLICSGLETLFCVFQIIVHACSYKPHQVGVIG | Function: Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Location: Membrane
Sequence Length: 243
Sequence Mass (Da): 27440
Location Topology: Multi-pass membrane protein
|
G0V4I2 | MSKGELIEIKRRIKSIKNTQKITKAMGLVATARFKRLRGIVEFADEYFNEVSNTFRKLYCDEVYDSKYFSENNENKDLFIIITSNTGLCGSYNSNIINFANEKVAKEDYLILIGDRGYQFFKRREYNVLMNIPIQRFPSFDDAQMIFNLIDDYFTKGKVKNIYIVYTKFINSVRQEVEMLKILPFEKIQEKNKEILLEPNKLQVFDFSAKIYLQSFIYNSLANALASEFAMRMTAMDSATKNSGELLDKLQLKYNRIRQGTITQEVTEIVSGAEALNSN | Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
Subcellular Location: Cell membrane
Sequence Length: 279
Sequence Mass (Da): 32453
Location Topology: Peripheral membrane protein
|
A0A970QBZ7 | MSTDHDQAGAVPRSGPVSPGEPALRSESGLQGGSAPPGGSAPPVDDGLQGTLGSRREVDPRRAAGEARRRRAAAERKKRTPLGMVIEVVIIVAAAFAIAMLVQAFIVKPFTIHQVSMQPTLQERDRILLNRLSYHFRDPERGDVVVFHSPMVKGEDLVKRVIGVPNDRVAVKDGDLYINGAIQEEPYVLDSEMLDEDQEVLVPEGHVFVMGDNRNNSGDSRFFGPIETDSIIGCAFCVYWPIRHWRGL | Catalytic Activity: Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.
EC: 3.4.21.89
Subcellular Location: Membrane
Sequence Length: 248
Sequence Mass (Da): 27173
Location Topology: Single-pass type II membrane protein
|
A0A3D3B7B7 | MQRLXLVSDDIVNAIVSERIDQPDCAKGFILDGYPRTLVQADSVEAMLSAKNMKLDVVIELQVNDSVLVDRVSGRYTCAKCGTGYHDRLQKPKVEGVCDKCGSTEFKRRPDDNAETMTTRLQDYYKKTSPLIGYYYAKGKLKSVDGMAEIDAVTADIEAILAGL | Pathway: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1.
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
EC: 2.7.4.3
Subcellular Location: Cytoplasm
Sequence Length: 164
Domain: Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis. Some bacteria have evolved a zinc-coordinating structure that stabilizes the LID domain.
Sequence Mass (Da): 18145
|
A0A2P5MIN8 | MVREVETVDRDGEVTVRKPGSFKIGYRSVQGLGEAWFLSATLALTPGDTEAGLQQIKTLLDKRAQTQPVNQPSCGSVFKNPDGDFAARLIEQSGLKGYAIGGACVSEKHANFIVNTGQASAADIETLINHVRATVKESQGIELQTEVCMVGEPA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 154
Sequence Mass (Da): 16434
|
A0A3D4HF96 | MKPCRHFSSSPEDLSLVASDLASGAVVALPTETVYGLAADALNPAALKKIFKAKQRPSTDPLIIHIAHLVQADELAYTNKDFYILAQTFWPGPLSIILPKKDIVPSLATADRPTVALRMPKHPAFRTILEKAKCPLAAPSANPFGYISPTTAAHVIDSLGNVIDGVVDGGPCDHGIESTIVNLSNPKHIEILRPGPISAQAIEKVLNKAVLIHQKTYSLLSQESLEAPGLLSKHYSPKTPVTLVKAGDLSPSIAEQAAYVYLAYTPTENLNAPNVKYLSKNGSLEEASRNLYKVLRELDKENFKKIFIEKAPNEGLGIALNDRLNRAASKK | Function: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Catalytic Activity: ATP + hydrogencarbonate + L-threonine = diphosphate + H2O + L-threonylcarbamoyladenylate
EC: 2.7.7.87
Subcellular Location: Cytoplasm
Sequence Length: 331
Sequence Mass (Da): 35777
|
A0A1V4STV8 | MGFYDFEKNIFYQPNKSKLKKVEDFLKIQGLELDNNIDYTVTLENNGQIIGTGSFGGNVIKCMAIDKEFRGYGVSNIIASELINEEYRIGNSRLFVFTKPNNENLFNQLGFYTLERAEKAIILENDKHGIERYCNKLINESLYKDINSKNYKNIASIVMNCNPFTLGHKYLIEKASNENDLVHLFILDEDKSIFPSKVRYDLVEKGIGRLNNVILHKAKDYIISSATFPTYFLKNENDILKSQAELDAKIFAKYIAKSLNINKRYVGTEPICKVTSEYNKVLKEILPENDIELIEVERKTFNNEVISASKVREFIKEDKFDELRNFIPQSTYDFLNSEDGIEIVDKIKKI | Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
EC: 6.2.1.22
Catalytic Activity: acetate + ATP + holo-[citrate lyase ACP] = acetyl-[citrate lyase ACP] + AMP + diphosphate
Sequence Length: 350
Sequence Mass (Da): 40497
|
A0A1V4M9V2 | MKKETVSLALLSGLMLLFAFPRFGAGFLAWIALIPLLFAVRNESRGDAFRLGFLAGFIFNAGLLYWITYVVNHYGGLSRGFSAAVMLLLAAYLSLYTAFFALGVVFFSRRGIPVLLSAPCLWTVLEFLRGALFTGFPWEYLGYALHDRLHIIQIADITGVYGVSFLIVFVNCLLFELLLGGSRRTAVVKASVGVLVMVAVLSYGAWKTVLVDAELEKAEKLDVSLIQGNIDQSVKWDPAYQRKTIGIYRDLSRKASRSGVDFIVWPETAMPLFFQDMDDNHRTIRFVAQEANATLLFGSPAYSIENGVRSLMNTAWIVTPDGKVSGRYDKVRLVPFGEYVPLKSVLFFVDKLVTGFADFIPGDRVAPVNTDGLAAGVLICYEGIFPEISRTHVREGADFLVNITNDAWYGKTSAPYQHMSMIPFRAVENRRSLARAANTGISALVDPLGRVTAVSNLFEREIVSGSLKISTIDTFYTEWGDIFVLLCFVVTTVAFFCKRRKYDEH | Pathway: Protein modification; lipoprotein biosynthesis (N-acyl transfer).
Function: Catalyzes the phospholipid dependent N-acylation of the N-terminal cysteine of apolipoprotein, the last step in lipoprotein maturation.
Catalytic Activity: a glycerophospholipid + N-terminal S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein] = a 2-acyl-sn-glycero-3-phospholipid + H(+) + N-acyl-S-1,2-diacyl-sn-glyceryl-L-cysteinyl-[lipoprotein]
EC: 2.3.1.269
Subcellular Location: Cell membrane
Sequence Length: 505
Sequence Mass (Da): 56190
Location Topology: Multi-pass membrane protein
|
A0A7V5EWJ4 | MAEQERKRTARAPETTEAEAVETADAAQAKAEELTEKIDDLLDEIDTVLEENAEEFVKNYVQKGGE | Pathway: Protein degradation; proteasomal Pup-dependent pathway.
Function: Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.
Sequence Length: 66
Domain: The N-terminal unstructured half of Pup provides a signal required to initiate unfolding and degradation by the proteasome but is not needed for pupylation, while the C-terminal helical half of Pup interacts with ARC to target proteins to the proteasome.
Sequence Mass (Da): 7369
|
A0A2K9LFB9 | MLTDIIPEGVLWKVAEDWMWNTPVCDAEEALVTKAVDKRKREFRAGRHCAHALFDEAGISCSALLKGKQREPNWPDGWVGSISHSNGLCVVAIAPKAAYLSIGLDVEQATPLGEDIINLICSPAEQDQITRLQLTAGQKLASIPLSKVIFSAKESVHKTYFPLNYHTLDFLDARIDLLHDHFRFEATITKPEPNPRHPLQRLHGRFCMKESFVATFIALDAATAGTENQ | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 229
Sequence Mass (Da): 25486
|
Q0YP67 | MNYVPITLKVENKQLLILGGGKAALEKVQMLQRFGFTVTVIGEEIDEEILQSGCTCHLRPFRSEDFEDVLLVYACFADREVNRAIKEEANARGILVNTPDDPELCDFITPALFIDGPMMVAVSSGGTDVRKAVAWRNRIKTYFSSHDPIS | Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
EC: 1.3.1.76
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Length: 150
Sequence Mass (Da): 16738
|
I7LKT1 | MLILGIDPGIAIVGYGFIEYKNNRFKVIDYGAIFTTPKNTMPERLEIIYNKLEDLLNIFKPDAVAFEELFFNMNAKTAITVGQARGAAVLCAQRNKLNIFEYTPLQVKQAVVGYGRADKKQVQQMVKMLLNLSEIPKPDDVADALAIAICHAHSNQFGDMFRIK | Cofactor: Binds 2 Mg(2+) ion per subunit.
Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
EC: 3.1.21.10
Catalytic Activity: Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).
Subcellular Location: Cytoplasm
Sequence Length: 164
Sequence Mass (Da): 18414
|
A0A7V1CJK8 | MTTGLALVRKIALDIGSKRIGIAITDETNTLARPLTTIERSNVKTEAKMLTRIIKENEVDIIVAGMPVDLKGAKGVAAQNIEEYLEKLDKLTDTPIIRYDERFTTKIAEDFLRASGLKKGKRKKIIDEAAATIILQNYLEHAKKNQA | Function: Could be a nuclease involved in processing of the 5'-end of pre-16S rRNA.
EC: 3.1.-.-
Subcellular Location: Cytoplasm
Sequence Length: 147
Sequence Mass (Da): 16349
|
A0A2H0VP63 | MDNQLTYEKAFERLEKILTTLNEGKASLEESLKLFEEANQLINSCSSKLTMAEKKIETLIKARDGSLQLDDNGQPLKETFEPESKDLFSKKELTQ | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 95
Sequence Mass (Da): 10855
|
A0A1V4SXN2 | MKINVIGMPIFYGCDNPGVDQGPTVMRESGTIGLLHKPGNEVVDLGDIDMVYASQNEKYKDDEHAKFLSYVLDASEKLAKKVDSSISEGSFPLTIGGDHSLGLGSVAGASKACGDLDDFALIWFDAHADINTIQTSPSGNVHGMPIAGGIGIDDKLSHVYFDGIKVRPENVHIIAARDIDEGEVKIIADNNIDVYDMKKVREIGVQKTVKEVLEKIKAKGIKNIHLSYDIDGIDPEFIEGTGTRVPGGFNMEEAQYVIKEIIGSGLVKSMDLVEFNPRLEKGITLAHCLELTDTIAKSIAKLH | Cofactor: Binds 2 manganese ions per subunit.
Pathway: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.
EC: 3.5.3.1
Catalytic Activity: H2O + L-arginine = L-ornithine + urea
Sequence Length: 303
Sequence Mass (Da): 32835
|
A0A6P8Y8V8 | MPHALPHQFERLPTHVVPSHYVLHFKPDLVKCVFDGEVTVDLEVKEPTHRLLFNCVDLELLHIELHLQDGTLFLPSKVTLSCHCETAAVIFASKVPPGICKLSISFRGLLDDGLRGFYRSKYISHDTKEERYCAVTQFEACYAHRCFPCWDEPSIKATFDISLTVPKDRVALSNMPVTHEEELPDGNRLVRFETTPIMSTYLVAMVVGEFDFIEKMTSSGVCVRVYTPVGKQDQGQFALEVAVKVLPYFANCYKISYPLPKMDLVAIGSFSAGAMENWGLITYRETCLLVDPDNTSTQRKQGIALYVAHEMAHQWFGNLVTMGWWTHLWLNEGYATFAEFLCVAELYPEYDMWTQFVTETYSPALRLDALKSSHPIEVPVGHPLEVQEIFDDISYHKGASVIRMLYRYIGTEDFAKGMNLYLSNFQYGNATTDDLWEALEEASNKPISEVMPLWTRQMGYPVVSVRCEVVGNKRKFYLKQSPFRADGASVDPDEPKLWMVPIEFSTASVPNESVHVIVLSTRESTIFIDDVKPTDWIKLNPGSFGFYRVHYSSEMLQMLQPAVSDCSLPPIDRLTLLDDLFALVQAGQCSSDQVLRLLDAMRNESNYIVWSEIAIVLFKFQKLLEYAEDVLPSFMAFGRHMLGQLRQSISWDPIPDESHKDKLLRNVILELLHNFDDDIAREESSRRFEAHANGTATLWPDIRGTVYRAVLSKADTATYEIFLKMYREETLQEEKERISHAFASIENADLLKEVLMFALSDEVRSQSTLSILSAIAQSSKGREIVWTYAKENWNKLHAKYGASVILSHFITASFQHFATEEMADQLEDFFVTNDTRGTARAVQQTIERVRINAAWLKRDLTCIKSFLENFK | Cofactor: Binds 1 zinc ion per subunit.
EC: 3.4.11.-
Subcellular Location: Cell membrane
Sequence Length: 871
Sequence Mass (Da): 99466
Location Topology: Lipid-anchor
|
A0A2E4ZUD7 | MSKIVAAVEIGTSKVKIILGEITNENSLTIVGYDSVASLGVKKGEVVNFKEASEQVHLAIDSAEKSAGVKADEVYLAMTGRHLHGSFNPGSARVRSADNRVNQADVQRAIEEAKRKELPDDRIYVHFIQNPFLLDGRPVDNPMDLVGKELEVGYWSVDGDENVVRDFLDVINGYGLEVRHVIVSSLAAGEIATSRADRKAGALVIDLGAGTTDYVLYRDGCAGQAGVIPLGGDHLTNDISMGLRVDEDHAESLKKMHGRAFVGEDDKDERVWLLGNKVIGDRKVSRNAIRQVIAARVEEIFHILCKNLDGAIPEGSSVNVHLTGGGSLLPGITEVATDILGLPAKRAVLSGGIAEDLREHEFSTVVGLLHYALTGQPKETDFTKRSGGFMGTLVKLLGG | Function: Cell division protein that is involved in the assembly of the Z ring. May serve as a membrane anchor for the Z ring.
Subcellular Location: Cell membrane
Sequence Length: 399
Sequence Mass (Da): 42851
Location Topology: Peripheral membrane protein
|
A0A7C1KQ22 | MQRALNLADRARGMTSPNPTVGAVLVRGGEVIGEGYHERAGADHAEVAALKSVDGDARGATAYVTLEPCCHTGRTGPCTEALITAGVTRVLVAALDPSDKVDGKGVAALKQAGIEVEVLDGTVAARARAQNEAFRKYAVTGRPLVTLKSAMSLDGKIATASGDSQWISGEESRRQVHALRGEVDAIAVGSGTAHIDDPLLTCRLPGARRQPLRVVFDSEANLDSDSRLVRTAGEFQTLVFVTDAAPADRVEALRRDGVEVARVQALRGRVDVNDALGFLGSREIPILSLMLEGGPTLASSFVAAGAVDKVMTYIAPMIIGGESARTPVAGEGFNMISEAVELYRMTHTRVGDDVLITAYTSKDEW | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 365
Sequence Mass (Da): 38461
|
A0A938DQS6 | MTDPAEEAAPDAPVRYERTSTGLEFDRVAFFSDAVFAIAMTLLVVGIGIPTVSDADLGDALREKRAEITSFFISFVVIGAYWRSHHRFWAGLKAVDNRLIVVNLFYLAAIAFTPFPTALAGKYTAEPVSIVIYAITLAIASGLQAVSMWLAHRHDLLRERLSSRSLRYLLVASVIPVAVFLASIPIALHDTVWALYSWLLIIPLEWGVDRWLRPDDLGPAYR | Catalytic Activity: K(+)(in) = K(+)(out)
Subcellular Location: Membrane
Sequence Length: 222
Sequence Mass (Da): 24690
Location Topology: Multi-pass membrane protein
|
A0A938DZM8 | MSAPVFQHTDLPDVTVGDVVVITGPEAHHALAVQRLRAGEPIEVVNGSGTRIYGVVDSASSRDLHVRVIECVEEPEASPRVVVVQAIPKGDRGERAVELLTEVGVDVVIPWQAQNCVTRWSGERGEKAHAKWDSTARESAKQSRRSWSLVVEQPSITAEVCDRVRAAQERGATVWLLHESTELQDPGIPDADEVWLIVGPEGGVSQSEVRALTQAGATPVRLGSTVFRTSSAGAVAAAVVSTLTGRWTNARARMT | Function: Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
Catalytic Activity: S-adenosyl-L-methionine + uridine(1498) in 16S rRNA = H(+) + N(3)-methyluridine(1498) in 16S rRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.193
Subcellular Location: Cytoplasm
Sequence Length: 255
Sequence Mass (Da): 27363
|
A0A965MPI2 | MARVDADVHGLLVIDKPLGVTSHDVVARTRREFGTRRVGHAGTLDPQASGVLVLGLGKATRLLTYLVADDKEYIATIRLGATTVTDDAAGEVLEQADAAAVSAVTDEAIAQAVASLTGDIMQRPSAVSAIKIDGQRAYAKVRAGEQVEIAARPVTVYEFEPREIRRSDEWIDLDVNVRVSSGTYVRALARDLGEKLGIGGHLTALRRIRSGRFAIDDAAAGLIPVGDALRSALPSIVIDDTAVTDVRFGRQISETAFASEEEGDVNASSVVGLLDSRGDAIAIARRVDGTFAPIVVFT | Function: Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
EC: 5.4.99.25
Catalytic Activity: uridine(55) in tRNA = pseudouridine(55) in tRNA
Sequence Length: 298
Sequence Mass (Da): 31542
|
A0A966P8R0 | RFPHGILIVNLAGSFLLGVTANQESDITFLLFGFCGALTTWSAFALDLFEERREVKLFAVNLFGNYLLGVFAALLGLWIGR | Function: Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Subcellular Location: Membrane
Sequence Length: 81
Sequence Mass (Da): 8953
Location Topology: Multi-pass membrane protein
|
A0A847DGI7 | MAEKERDEREDEAVKSEEAPKRKKVPINMIIIIILVLCLVGGGVFVWKSGLFSKGTDGSAIDTEKQNKELIGPILTLDTFIVNLIGDRGKNYLKAKVELELDSEKTIVEINKRLPQIRDSILTLLSSKSSEDINTLDGKFQLRAEIMTTINQYLRTGKIRNVFLTDFIIQ | Function: Controls the rotational direction of flagella during chemotaxis.
Subcellular Location: Cell membrane
Sequence Length: 170
Sequence Mass (Da): 19194
Location Topology: Single-pass membrane protein
|
A0A4Q7DGL1 | MTHKWLTKHSKAKLNLFLHIIGRKNNGLHLIESFFVLLHELYDIIKVRNSNSSQCTVVGQNIHGKNIAITTLEAMQHFAPSMSVEIEIQKQIPIGAGLGGGSSNAATLMILLNQLWNLNLTVPQLQQIATSIGADVPFFLHQDNAFVSNTGETITHCQIGISSHMLVVYPMFPISTKDVYQISVQSFRQPLSQLSKVNLIEAIVRGQNDLQQAAIRLEPQLTDLIDYMSKQEGVITTSMSGSGSACFSSFQNKEKATLALQRLRNKYPRFFLHYEEISI | Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 3/6.
Function: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.
EC: 2.7.1.148
Catalytic Activity: 4-CDP-2-C-methyl-D-erythritol + ATP = 4-CDP-2-C-methyl-D-erythritol 2-phosphate + ADP + H(+)
Sequence Length: 279
Sequence Mass (Da): 31164
|
A0A951JY05 | MGDDVVAALRAELAPERVHAGAPLSDHTTMRVGGPAAALARVESVAELQAIAGVIRRTGLPWLVIGRGSNLLIADAGWPGIAVILGRGLRGVDVDGTAVRAGAAEPMPALARAVARHGLGGLAFGVAIPGTVGGAVRMNAGAHGREIRDVLVWAEVARMGADGALERWTADRLGFRYRHSDLAADAVVTRVELVLAHTDAERLAAQMAEMRQWRRDNQPINEPSCGSVFRNPDGDSAGRLIEAAGCKGLRVGGAQVSRRHANFVTVTPDARASDVHAIIRTVQRRVYETAGVRLQTEVVLAGFDDDSEGRGRASASRRAGSREDAAGEESAEVWT | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 335
Sequence Mass (Da): 35237
|
A0A7C0W3S1 | MGSEIEDLREQIRYHDYRYYVLDEPEISDFEYDELMRRLRKLEAEHPELVTPDSPTQRVGPPISDQFAPVRHREPMFSLDNIESFEELDAWEARVVRTLEAPPDSYVCELKIDGLAVSLVYEQGSLAVAATRGDGTVGEDITANVRAINPIPLRLLGDAPAVLEVRGEVYMPDAAFEELNRRQSEAGDQLFVNPRNAAAGSLRQKDPAVTASRKLSAWMYQLGTVQGGPVLETHWEALEWLRSLGFPVNPASERVQDLGEVKAYLQTAEDARHAKGYATDGVVIKVNRFEQQQALGFTARAPRWAIAYKFPPEEQVTRLLDIRIGVGRTGRVTPYAMLEPVFVGGAMVSRATLHNEDEVHRKDVRIGDEVIVRRAGEVIPEVIGPIVSRRDGSERVWTMPATCPFCGSRIVKPEGEKVARCTGGLTCPSRLREWLFHFASRSALDIEGLGYKTIDLLIEKGLIRDPADIFFLEPGDLEGLEGWGEVSVANLMTAIAEAKHRPLSKLLIGLGIRHVGGTVARMLARRFCSIDALLAASEEEIAAIEGVGPIIAQSVHAWAQSPETVALIEKLRAAGLQLTEDASGEEDLLAGLRVVLTGRLEGWSREEAKEAIEARGGTVVGSVSKSTSVVVAGDSPGSKLARAQSLGIPVIDAEGFERLLARGPAVLEG | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
EC: 6.5.1.2
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Length: 669
Sequence Mass (Da): 73293
|
A0A9E5HV87 | MRSSLQSFERGEGMDQARKLALIERANEISLRGMGKTFPNPIVGAVIADEQGRVVSEGFHQGGPHAEVVALANFKGDPAEASLYLTLEPCNHHGKTGPCSEAIIKSGIRKVFYAVEDPNPIAEGGARRLREAGIEVEKVHSDRALFFNRDWLTKISLGRARMVWKVAHSLDGAIAAEDGTSKWITNEESRSDVKRVRDGVDAIITGTGTVLADNPTLNGKERNPVRVVVGERDLPSDFNIFDDSAETVHLKTRLIDEVLSFIKERGFNRVLVESGPKLGSSLFKAGLIDELLLYQAPSILGNGRRFTENLGISSIEDQIKLLDRGIEFFAQDLKRTLFTDNENNRRFVCSPV | Cofactor: Binds 1 zinc ion.
Pathway: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4.
Function: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate.
Catalytic Activity: 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)
Sequence Length: 352
Sequence Mass (Da): 38824
|
A0A249KHC3 | MGLFNRLIAKVRGTSTASALDWSEIEVELLASDLGPSLVSELLAASKKMRGDDAESAVKEILTSKLSSKPRALRSDLSTNVIMVVGVNGTGKTTSVAKLATLLHKNGESVTLAAADTFRAAAVDQLKTWGQRIGVEVIAGKENAEPASVAFDSVKRAVELGSKYLIVDTAGRLHNKSDLMAELGKVKRVIEKGAPLAEVLLVIDGTTGQNGLAQAKIFSEAVEVTGLIVTKLDGSARGGVALAIESELDIPIKFIGTGEAAQDFAPFEPEAYIAGLLA | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC).
Subcellular Location: Cell membrane
Sequence Length: 278
Sequence Mass (Da): 29054
Location Topology: Peripheral membrane protein
|
A0A662ZGN1 | MDNPQTLEQMLEQIDELVKKMESGKLPLSEHLSLFEQGVGLIKDCEKALKDAEGKVKILTDSQSLANGTKTGDDVVSDFNAGI | Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides.
Catalytic Activity: Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates.
EC: 3.1.11.6
Subcellular Location: Cytoplasm
Sequence Length: 83
Sequence Mass (Da): 9034
|
A0A2H9L966 | MDAAIDVATKQAKQQLDEYFEGARSQISVGGAYQEGKLPPKASASLPEGFSPRSIHKILKGVLQRIKPSPEEMTEEQRVAKTVTRKLKTALPNHVEIRLMGSVAKGTHLKGNKEMDIFLLFPKSFTKHHMLVSAFHYIRKALAGHRLEQHYAEHPYLKCIVDDHGIDLVPSFKIAHAGELGTAVDRSQLHTKYINRHLSAQQKEDVRLLKQFAKALGIYGAELRVEGFSGYLCELLILQYGSFSSAIENAQNWKIPVCLEPVGKSETEKSKIETRNHCGSELRVPSSETRNSSTRRGELFASWRSTAIAVENFSNWRNASRRIQKPETNFTSPLVVLDPVDKNRNVAAVVSTTSLARFIFAARMFLEKPNAGMFFRKEIRAAPKALGKMIVARKTSLLMLEFKSPKLVEDMLWPQLKKTSLAIGRELIYHGFAIMGYYYWSNGERCLLLYELEQGVLPSVVKVAGPTVSMGKNIGQFIKAHNRAAIHIEHDRLVAIEERMVRTPNQVVALVKMKKCEIGIPDEFKHRVMAARTITVGEFVNKFKEVATDYFLRDLRSII | Function: Catalyzes the addition and repair of the essential 3'-terminal CCA sequence in tRNAs without using a nucleic acid template. Adds these three nucleotides in the order of C, C, and A to the tRNA nucleotide-73, using CTP and ATP as substrates and producing inorganic pyrophosphate. tRNA 3'-terminal CCA addition is required both for tRNA processing and repair. Also involved in tRNA surveillance by mediating tandem CCA addition to generate a CCACCA at the 3' terminus of unstable tRNAs. While stable tRNAs receive only 3'-terminal CCA, unstable tRNAs are marked with CCACCA and rapidly degraded.
EC: 2.7.7.72
Catalytic Activity: a tRNA precursor + ATP + 2 CTP = a tRNA with a 3' CCA end + 3 diphosphate
Sequence Length: 559
Sequence Mass (Da): 63054
|
A0A966JJN4 | VCDFASVKSDLLLKVKELSANPENFFSMHPMAGREINGAENARADLFDGRAWIGISDSVNNAKIKEIAQNLVQKCGGTLYWLTSKEHDELVAKISHLPQILSSVIAGSLEGLSNENLNLAGQGLRDLTRLASSDAALWSQILLENHASIAPVIDSIINDLNNVKESIVSKNPTELNDFFRKGNNGKSKIPGKHGAKNRDYSYLPIVIDDKPGQLAKIFNECAKVSVNIEDLSIEHSPGQETGLITLALSNIDCIKLSNHLENLGFKVHPVKNR | Pathway: Amino-acid biosynthesis; L-tyrosine biosynthesis; (4-hydroxyphenyl)pyruvate from prephenate (NAD(+) route): step 1/1.
EC: 1.3.1.12
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Length: 273
Sequence Mass (Da): 29815
|
A0A965KN03 | AIQGGMEKAERAQVEAERALAQYTAQLNEARGEAQKIREDARVQGAAIIEDLRSKAAEEAARITAAATEAIQSERQQAMTALRNEVGALATELAGKIVGEALDDQVRQSRIVDRFISDLEKSK | Function: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
Subcellular Location: Cell membrane
Sequence Length: 123
Sequence Mass (Da): 13335
Location Topology: Single-pass membrane protein
|
A0A951N1C5 | MTAVPLLALLVDRWAGEPFAHVHPVVWMGRYLDGCAARRRTDAPRARQRVTGGVGVAVGCALAGAGAALLRRCLRPLPPLARVLAEAAVLSTLLAERMLADEIAGVGRTVGRDLDGARSRLAMLVSRDVADLDHAQVREAAIESLAENASDSIVAPLWWYGLAGLPGAAVYRFVNTADAMWGYRTESWRWWGAAAARADDVANWLPARATAVLLAPTRDLRRVASAASVTASPNAGWPMAAVAVRWDLRLRKPGVYVVNPTGRTPGDADVDRAITAIRAAATAAAIGASVCGRPAR | Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis.
Function: Converts cobyric acid to cobinamide by the addition of aminopropanol on the F carboxylic group.
Subcellular Location: Cell membrane
Sequence Length: 296
Sequence Mass (Da): 31304
Location Topology: Multi-pass membrane protein
|
A0A2E8A4J6 | MNVGIIGASGYTGRELVSMLSDHPHVNLSMITSRALQGKSLSSQIPKLRGKGIDLEFQNPSPEELGKENSIDLFFLALPHGTASEYAIPLLQGGKKVVDLSADFRIRSKDTYEEYYESPYPAPEWQEKAQYALPELHELSWEISSLLASPGCYPTSILIPLAPLLKNKLVSTSEIVVNSMSGVSGAGRTPSEKLLFCERNESSGAYGLPKHRHLSEIEEQLSVLSDRKVILSFHPHLIPLTRGLHSTISIPCMGKLDRQEIISCWNEFYQGREFVHILDENEFPETAQVVGTNRVDLSVHADSRTNRYVLCSAEDNLIKGAGGQAIQAMNICQGYKENSGLS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Function: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde.
Catalytic Activity: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + N-acetyl-L-glutamyl 5-phosphate + NADPH
EC: 1.2.1.38
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 37756
|
A0A960ELD4 | MSELVTITVDGREVQVPAGQLLIKALQDSGTYVPHFCWHERLKPAGMCRACLVEVDGPRGMALMTACTLPVADGMNVATRSENAVAAQEGVLEFLLINHPLDCPVCDKGGECPLQDQTVAFGPGESRFVEDKRHYAKPIPISDLVLLDRERCILCARCTRFADEIAGDPLITFTERGGSTQVLNYVEDPFVSYFSGNTVQICPVGALTSSSYRFKARPWDLATTDSSCTICSVGCRSALQSSSDELIRMIGVDSEPVNHGWLCDRGRYGFGYIHSVERRSEPVVRRSSEGSAEFETVSWPDALDEVADRLGAIVSEHGGQSVGIIGGSNGTNEDAYVWSKFARTVLGTNNVDAQLDDGIPAQVIQGLPRAEISDLESSSAIILVAPDLKEELPVLYLRVRRAAEEKGVPLIEVAPYPTGLTPYAAVRVAPVPGHTGEVVERIVKASTSGPSAPGSHLSDDERRAAELLSTDGKVTVILGRPSLAEGSGIVVRAAAALSTIPQARFLSALRRSNVHGALEMGLSPDMLPGRVTLEAARDYYANAWALDGKPAKLSTTQGWSTGDMLRAAVDGRIKALVLLGSDPIGDFPDRELAERALDRVSFLVSVDGFDTASTSKADVVLPPMMQGEQDGTFTNLEGRILPLGAKVTGAGTSMEDWRIAGELAWRFGVDFGFLTASEIQDEIAAVAPAMAGIDSGAIASSPVGLLPRAFDDPPASPEAPEAIDADATEADAADADADVEAAESEGSEDASSMPTLHVWDGSTFVSGEVPAPDAYGLRLIVGRKLYTSSVRTIESPTIAALAAEPVLLVNPADRDKLGFQEGESVRVHTVTGSSNVGLRMLSDESMPRGLALIWHDPESGAATLLLDAGKPAQDIRIDRVEAMS | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
EC: 7.1.1.-
Catalytic Activity: a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) + NAD(+)
Sequence Length: 884
Sequence Mass (Da): 93932
|
A0A0K0NMA7 | ISNVGLNVSLHLKEKGTKQEENLTCTTINQNNTTVVENTYLNNTTIITKEADWKTPSYLLLNKSLCNVEGWVVIAKDNAIRFGESEQIIVTREPYVACDPTGCKMYALHQGTTIRNKHSNGTIHDRTAFRGLISTPLGTPPTVSNSDFMCVGWSSTTCH | PTM: N-glycosylated.
Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates.
EC: 3.2.1.18
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Subcellular Location: Membrane
Sequence Length: 159
Sequence Mass (Da): 17589
Location Topology: Single-pass type II membrane protein
|
A0A829ZXI1 | MIVIGGGPAGYAAALTAARKGRETILVEEAELGGTCLNRGCIPTKALAKSAGVFSLLKGAKEFGIRSSDVGVDWASVMARKKSIVDGLRRGLQGLIKGAGISVVSGRATLQGGGKVEVVDASGKATALEGDAIIVASGSTVKNPFPCAIDEKDILSSTGILELAELPSSLIIVGGGVIGLEFANIFNSLGVKVTVIEALPRLLYGIDEEASTLLMKILKARGVEFRLSAKVSKIEKAKGKVRVSLEGGNGVEEFVADKVLLAVGRAPNVNGLGLDKAGVQVEGGRIKVDAKMRTTAKGVYAAGDVIGNPMLAHAGFLEGEVAARVACGEEASVDWRAIPSCVYTTPEIAQVGLSEEEARKQFDKVIVGKYPLRGNGRALIEDEGGQDGFIKIVADRKYGEVLGVTMVGPFATELIGLGVLAITNELTIDQMADTVQGHPTVCEAIREAALIAVGRPLHFGR | Cofactor: Binds 1 FAD per subunit.
EC: 1.8.1.4
Catalytic Activity: (R)-N(6)-dihydrolipoyl-L-lysyl-[protein] + NAD(+) = (R)-N(6)-lipoyl-L-lysyl-[protein] + H(+) + NADH
Sequence Length: 461
Sequence Mass (Da): 47838
|
A0A9C8C5S2 | MPELRQDPVTGYWAVIATERAKRPESFTQERKESVKSNAVCPFCYGNEAMTPPEVLAFRPDGGEPNTSHWKVRVVLNKFPAFTIEDKIKTSASNMLYGKQKKSEIYANMPGLGIHEVIISGPDHSKSLALLNVDEVELIIEAYRSRLLKIKDDQRIKHVLIIVNHGKEAGASLEHPHSQLFGTTLIPRLVADELDCSRRYFCEKGHCIFCDIIEEETKLGDRVIKESEHFLVFSPYASRQPFETWIVPKNHSANFECISSAEKRDLAFMLKDTLLKIYEGLNDSPYNYYLHTSPYRINSGEFYHWHIEIFPKLAIQAGFEMGSGMMINVVLPEGSARFLKNL | Cofactor: Binds 1 zinc ion per subunit.
Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 2.7.7.12
Catalytic Activity: alpha-D-galactose 1-phosphate + UDP-alpha-D-glucose = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
Sequence Length: 342
Sequence Mass (Da): 39012
|
A0A194AJA2 | MQKSKKVQTAVNHIQKRFAPGYSPVLGITLGSGLGSFVDMFSSALWLDFEDIPGFPRSTVKGHTGRLGIVRHGQTDCLVLQGRNHLYEGYSPDEVCFATRVLAGLGVNTIILTNAAGALNPLFEVRGIMLITDHVNLMGTNPLVGANVDAWGPRFPDMTEVYCPVLRDKVLDVALDVGVRLEQGVYVGVHGPCLETPAETRAYRLLGGDAIGMSTVMEAIAAHHMGVKVIGLSCLTNKNLPDCMAQTSHDAILEQANRTANNLTNVLQAIIVSGMFAS | Pathway: Purine metabolism; purine nucleoside salvage.
Function: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.
EC: 2.4.2.1
Sequence Length: 278
Sequence Mass (Da): 29826
|
A0A9D8EA15 | MIGTSGPTLSADPGNSPGAPGGGRARKNGGRPGLQRSGPTDREVRRAGTTPRNRPSVSLLWGPHRRRTVLVGLTGGIGSGKSTVARLLEARGAVIIDADRIAREVVEPGMPAFAALVEWFGPGVVGPDGHLDRPALAALAFATPEATAALNAITHPAVGAEFLRRMQEAPPDAVVVCDVPLLAESDEARSRGYEHVIVVEAPRALRLDRLEVRGVPRPDAEARMANQATDAERRALATWVVDNSGDLEHLERQVDDIWAALQAARAD | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
EC: 2.7.1.24
Subcellular Location: Cytoplasm
Sequence Length: 267
Sequence Mass (Da): 28211
|
A0A365Z5G8 | MPDYHDDLRLAHVLADAADAATMERFKALDLTVETKPDMTPVTEADRAAEEVIRSVLQRARPRDAVLGEEFGNEGQGPRRWVIDPIDGTKNYVRGVPVWATLIALVERGAGGDRPVVGVVSAPALSRRWWAALGAGAYTGRSLTSATRLRVSGVERLADASFSYSSLTGWEERDRLDGLLRLSRDCWRTRAYGDFWSYMMVAEGSVDLCAEPELSLWDMAAPAIVVQEAGGRFTGLDGRDGPHGGDAAASNGLLHDELLGYLGG | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 264
Sequence Mass (Da): 28615
|
A0A7C1KPZ2 | MTSGPEEIRERLRALLVAKAYLEGDFVLTSGKHSNHYFDCKQVTLHPEGLALAAEMLVMKMHEAAIPAIGGLAIGADPLVAGVVACSLKLGYPVKGFIVRKEPKAHGTCSWIEGPVEPGTRVAIVDDVVTSGGSVIKAVNNSRAEGLEPVIAYALVDREEGGAARIEQEAHFPFEPLFRYSELFNGENS | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 189
Sequence Mass (Da): 20270
|
A0A7C5GQC5 | MPQRAIGVFDSGLGGLSVLREIHHQLPYERLIYVADSAYAPYGDKPTDTILQRCDIITRFFLTQNIKAMVIACNTATAVAANHLRQRYPHLHIIAIEPAIKPATKLTQKACIGVFATQQTIQSQRLQQLIEQHANHVQVVKQACSGLVEMVEQGRFADAEVRALLQRYLQPIHQANVDVLVLGCTHYPFLHQTIQQLSPHLRIIEPSVAVTRQLNQRLLDQALHAPTVTRPAGVTFYTSKQQAITKQYAVLQHLWYAHALSHHKACHSQPIAQSTHSASALSSALGKSTKSSIHLLALPTAFC | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Provides the (R)-glutamate required for cell wall biosynthesis.
EC: 5.1.1.3
Catalytic Activity: L-glutamate = D-glutamate
Sequence Length: 303
Sequence Mass (Da): 33638
|
A0A938ADT8 | MTSPPWGRSCSRRLGATVPDTSAPVPDTSAPVPDTPAPVPDTPAPVQRDAPLAPLTSIRVGGPADALATCTSFAAVTRALAWAAGEGAPVAVVGKGSNLIVDDAGFRGLVIRLAGRLSSISVRGERTLWCGGGASLPRAVQRAAAAGLAGLEFGASIPGTVGGAVAMNAGAYSSDLSQVLAWAVVCDASGRRKVGRDDLAMGYRTTSVQGDQVVAAVGFLLQPGVTDAIRDRLSELRAHRRSTQPQGVRTFGSVFTNPEGDSAGRLIEATGLKGHAIGGARISPVHANFIEAGPHASARDVIALMDEARRRVRDAGGPVLHAEVRYLHPEWGIGAPPLAEIA | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Cell wall formation.
Catalytic Activity: NADP(+) + UDP-N-acetyl-alpha-D-muramate = H(+) + NADPH + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
EC: 1.3.1.98
Subcellular Location: Cytoplasm
Sequence Length: 342
Sequence Mass (Da): 35011
|
A0A938FEC9 | MYEVLIGSSKPNHSALHQKLESRHTRLSAKEFSLKVALASTSVLALPTYRALKDSSHQLPAIITKSEKESGRGLKIEESAFIASLEGEKVIRVEDQQGLVAALKEEKVDLVVTVSFGMLIKEEALKIPSLGWINLHFSLLPKYRGAAPVQRAILAGEKKTGVSVFQLDKGMDTGALYTSKSIEMGEKSSGELLDELAEIGSQELLRAIEMMEKGVAPTPQMGEASLAPKIDSAETALDFKASVDVVVRKVRAFAPKPGAWSKLRGGRVKILEAERSNLPPKKPGEILSLNPLIISTSDDAITIKTVQEAGKKVMHAQDWVRGARLAIGEFFE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
EC: 2.1.2.9
Catalytic Activity: (6S)-10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N-formyl-L-methionyl-tRNA(fMet)
Sequence Length: 332
Sequence Mass (Da): 36077
|
A0A937VLI2 | MLPAAVLPADYHMHTAFSDGEGTPDDLVRRAQELDLPEIGICDHLVPPALDDGFGIPPQRLDEYVTAVRSAAAGAGIRVLLGLEADYSPETAAETAAQLARWRPDYVIGSIHSVDGFAFDDPRLRDDPRQRDLELLWLGYFRLLGQAAESGLVDVLGHADLVKKFGRRPAMTPSLTAAALEALSCAAERGVAIEINTCGWRQAAGEQYPSLTLLEQACRLGVSLTFGSDAHVPADVGSRFAAAVAVARSAGYSRWLRLSDRAEVPLP | Pathway: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
EC: 3.1.3.15
Catalytic Activity: H2O + L-histidinol phosphate = L-histidinol + phosphate
Sequence Length: 267
Sequence Mass (Da): 28670
|
A0A938AQ78 | MKVFRPRLAVMVSGNGSNLQAILDACEHGLLRADVVGVVSSKEGVPAIARAERSKVSVVVVAPVPNETRAAYDLRLLEVVKGFSPDIVVLAGFMRILSNNFLQQFPSQVVNLHPALPGELPGTHSIERAFAESRDNWRTHSGITVHLVPNEGVDTGPVLASEVVPIHAHDTLESFTERMHEREHILLVQTLNDLCQNFVAGQEIDSVS | Pathway: Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1.
Function: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
EC: 2.1.2.2
Catalytic Activity: (6S)-10-formyltetrahydrofolate + N(1)-(5-phospho-beta-D-ribosyl)glycinamide = (6S)-5,6,7,8-tetrahydrofolate + H(+) + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide
Sequence Length: 208
Sequence Mass (Da): 22651
|
U4KX21 | MSCSPASSTTRHILHHLHLGRIPFTKTGALQSLLVSKHLRAKASATTSPPPTLLTSEFNPVYTLGRRETSVTDEQLSHLRYDGKAEVHSTLRGGQTTFHGPGQMTGYLICDLKSHNLTPRCYIRKLESSIISLLEKYGVKAFTTEDPGVWVTTEEKICAVGVHMRRNVTSYGVGLNVNTDLRWLDRIVGCGLVGKRATSLQRLGVEGKTVEEVAGDWATELVRTIGMAGTKRVGVEELLGDEEKGAWERGEVLGKEE | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 257
Sequence Mass (Da): 28209
|
A0A942KK50 | MRKALISLTLLVIAALTGALLGCARQAEPLRDARQALGTIVSVTAWPADNANAESLTAIDSAYSAMSAVEGVLNVHDPDSVIATIPAGSESLPAEASAIISAVERLGVEQYFSPHLFEVVALYDFEGEGRVPTETELRAALIRPRYDFGGAAKGLALDEAASVLARSPAIGAALVSAGSTTITTGEKPDGSPWRIGVEHPREPGQTIAAITARGEISVSTSGDYQRYFMRDEVRYHHILDPTTGRPAQGLRSLTVVGEIPGLDSDILSTALFVMGQKAATTYARKHGLGLVLVTDQGETLIVDGPAEATWQITQPD | Cofactor: Magnesium. Can also use manganese.
Function: Flavin transferase that catalyzes the transfer of the FMN moiety of FAD and its covalent binding to the hydroxyl group of a threonine residue in a target flavoprotein.
EC: 2.7.1.180
Catalytic Activity: FAD + L-threonyl-[protein] = AMP + FMN-L-threonyl-[protein] + H(+)
Subcellular Location: Cell inner membrane
Sequence Length: 316
Sequence Mass (Da): 33242
Location Topology: Lipid-anchor
|
X7EF92 | MTEDTVKTTHFGFDEVPEAEKAGRVQGVFTSVASRYDLMNDAMSLGIHRLWKDAMMDWLAPRRGQRLLDVAGGTGDISFRFLNRAGSGHATVLDLTESMLLAGRDRAEAEAMSGMLDWVVGDAMALPFPDNSFDVYTISFGIRNVTRPEDALAEAYRVLKPGGRLMVLEFSQVPVPALAWAYDRYSFNLIPAMGQVLAGDRDSYQYLVESIRRFPDQETFLGMIETAGFEQAKYRNLSMGIACLHSGWKI | Pathway: Cofactor biosynthesis; ubiquinone biosynthesis.
Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
EC: 2.1.1.163
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Length: 250
Sequence Mass (Da): 27851
|
A7XP42 | TXYLIFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMK | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 156
Sequence Mass (Da): 16488
Location Topology: Multi-pass membrane protein
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.