accession
stringlengths 6
10
| name
stringlengths 6
11
| Full Name
stringlengths 1
147
⌀ | taxon
stringlengths 3
46
⌀ | sequence
stringlengths 16
2.75k
| function
stringlengths 6
5.51k
| AlphaFoldDB
stringlengths 6
10
|
|---|---|---|---|---|---|---|
Q9LM84
|
WOX14_ARATH
|
Homeodomain protein PALE-2
|
Arabidopsis
|
MVKKKKEKEKSKEIEEMDREIQNGAYSGRVMTEEQMEILRKQIAVYAVICDQLVLLHNSLSSYHPLSSGVRPMVGGYFDPMGASSSSHRISTRHRWTPTSTQLQILESIYDEGSGTPNRRRIREIATELSEHGQITETNVYNWFQNRRARSKRKQPQTTTANGQADDVAVTTEERRSCGDSGGLESYEHILFPSPDLGIEHLLSIGKFMET
|
Transcription factor which may be involved in developmental processes.
|
Q9LM84
|
P32748
|
PYRD_DROME
|
Dihydroorotate dehydrogenase (quinone), mitochondrial
|
Sophophora
|
MDQDHLKNAKNATRRVGRLRSLGIVTVGGAALVAGITAYKNQDQLFRTFVMPAVRLLPAEASHQLAVLACKYRLCPVSQYHDDQNLHTSFFGRMLSNPIGIAAGFDKNAEAVDGLQDLGFGFIEVGTVTPAAQEGNPKPRVFRLTEDKAIINRYGFNSDGHQAVLQRLRLLRKKENFNGVVGVNLGRNKTTMSPIADYVQGVRVFGPVADYLVINVSSPNTKGLRDMQSKEKLRELLEQVNDTKSSLDKNKNVPILLKLSPDLSLDDMKDIVWVIKRKKSRVDGLIVSNTTVSRENIEKNKLAEETGGLSGPPLKARSTEMIAQMYQLTDGKIPIIGVGGVASGYDAYEKIEAGASYVQIYTALVYEGPALVEDIKAELSALITRLGHTNVADVVGTNSKFYLPK
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
P32748
|
Q2P6P9
|
RPIA_XANOM
|
Phosphoriboisomerase A
|
Xanthomonas
|
MSEAKRLAAEKAIDYVEDGMIVGVGTGSTVAYFIDALGHIGHRIKGAVSSSEQSTARLRQHGIEVLDLNHTGNLSLYVDGADECDPNRCLIKGGGAALTREKIIAEASERFICIVDPSKQVPVLGKFPLPVEVIPMARSLVARQILALTGGQPVWRDGVVTDNGNVVLDVHNLQITDPVALERSLNQIPGVVCVGLFARRPADVVIVGGEPPRVL
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q2P6P9
|
Q7L2H7
|
EIF3M_HUMAN
|
PCI domain-containing protein 1
|
Homo
|
MSVPAFIDISEEDQAAELRAYLKSKGAEISEENSEGGLHVDLAQIIEACDVCLKEDDKDVESVMNSVVSLLLILEPDKQEALIESLCEKLVKFREGERPSLRLQLLSNLFHGMDKNTPVRYTVYCSLIKVAASCGAIQYIPTELDQVRKWISDWNLTTEKKHTLLRLLYEALVDCKKSDAASKVMVELLGSYTEDNASQARVDAHRCIVRALKDPNAFLFDHLLTLKPVKFLEGELIHDLLTIFVSAKLASYVKFYQNNKDFIDSLGLLHEQNMAKMRLLTFMGMAVENKEISFDTMQQELQIGADDVEAFVIDAVRTKMVYCKIDQTQRKVVVSHSTHRTFGKQQWQQLYDTLNAWKQNLNKVKNSLLSLSDT
|
(Microbial infection) May favor virus entry in case of infection with herpes simplex virus 1 (HSV1) or herpes simplex virus 2 (HSV2).
|
Q7L2H7
|
Q3MAN8
|
CHLN_TRIV2
|
Light-independent protochlorophyllide reductase subunit N
|
Trichormus
|
MTIAQEPTALNFECETGNYHTFCPISCVAWLYQKIEDSFFLVIGTKTCGYFLQNAMGVMIFAEPRYAMAELEEGDISAQLNDYAELKRLCEQIKRDRNPSVIVWIGTCTTEIIKMDLEGLAPKLEGELGIPIVVARANGLDYAFTQGEDTVLAAMAHRCPDKAPVAEAEKNERNAVQKLLNFGKKKELVAQEESEYVDHPPLVLFGSLPDPVVTQLTLELKKQGIKVSGWLPAKRFTELPVLEEGYYVAGVNPFLSRTATTLMRRRKCKLIGAPFPIGPDGTRAWIEKICSVFGITPQGLDEREAQIWAGLEDYVKLIRGKSVFFMGDNLLEVSLARFLVRCGMTVQEVGIPYMDKRYQAAELAMLEKACQEMGVPSPKMVEKPDNYNQVQRIYDLKPDLVITGMAHANPLEARGINTKWSVEFTFAQIHGFTNARDILELVTRPLRRNNNLKDLGWDKLVREEAKI
|
Component of the dark-operative protochlorophyllide reductase (DPOR) that uses Mg-ATP and reduced ferredoxin to reduce ring D of protochlorophyllide (Pchlide) to form chlorophyllide a (Chlide). This reaction is light-independent. The NB-protein (ChlN-ChlB) is the catalytic component of the complex.
|
Q3MAN8
|
Q3E989
|
PME54_ARATH
|
Pectin methylesterase 54
|
Arabidopsis
|
MGVIDMVLFWVLLVNALLIVDASSRNMPFAYQNEMQRHCSSTKYTSLCVQNLREFRHGSLDGLDFVSFLVNKTISDSNLLIPPLSSSMGSSKLVSLEDSTYTLPSPSVSDSCERLMKMSTRRLRQAMEALNGSSRKRHTKHDVQTWLSAAMTFQQACKDSILDSGGSSSASAISHISQKMDHLSRLVSNSLTLVDTIMKNPKPKTKSTALPRWVTAGERRLLVGRARAHVVVAKDGSGDYRTVMEAVTAAHGNGKDLTVIVGDDSATGGTSVPDTATMTVTGDGFIARDIGIKNIAGPRGHQAIALSITSDQSVLYRCSISGYQDTLYAAALRQFYRECDIYGTIDFIFGNAAAVFQSCNIFLRRPHGVKAYNVILANGRTDQRQNTGFALHSCRIRTDSDLSPVKHKYSSYLGRPWRKYSRAIVMESYIDDAIAEGGWAGWLDSGDEVLKTLYFGEFKNYGPKARISKRVTWEGFHSIGFEEANYFSVVKRRNGEDVTNGFKYKFKIKIQI
|
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
|
Q3E989
|
B1L6E9
|
RTCA_KORCO
|
RNA 3'-terminal phosphate cyclase
|
Candidatus Korarchaeum
|
MEFIRIDGSYGEGGGSLLRYAIALSSVTMKPVEIYNIRVKRANPGLRPQHLNAVRALARITEATVEGDEVGSTALRFIPRKRAGGSFEIDIGTAGSISLIIQAILPACISSEEEISLRIRGGTDVPLAPPIDYMAEVFLRNMAPLGVRAELKLLRRGHYPRGGGIVELHASPSKLFPIDKVRGEKFDRVLGRCHAVKLPRSVVERISSSAIDTLRKEGLRVEIEEEWSEDGHLGPGAGIVLWTDSNPRIGADELGEKGKPSEVVGKNAASKLLDEIKAGMAFDSHMGDMIIPYLALARGRSRVGISKLTLHAESNIWLVERFLPVKFIVQGGVGSPTVIEVEGAGLEL
|
Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
|
B1L6E9
|
C1CST6
|
DDL_STRZT
|
D-alanylalanine synthetase
|
Streptococcus
|
MKQTIILLYGGRSAEREVSVLSAESVMRAVNYDRFTVKTFFISQSGDFIKTQEFSHAPGQEDRLMTNETIDWDKKVAPSAIYEEGAVVFPVLHGPMGEDGSVQGFLEVLKMPYVGCNILSSSLAMDKITTKRVLESAGIAQVPYVAIVEGDDVTAKIAEVEEKLAYPVFTKPSNMGSSVGISKSENQEELRPALELAFRYDSRVLVEQGVNAREIEVGLLGNYDVKSTLPGEVVKDVAFYDYDAKYIDNKITMDIPAKISDDVVAVMRQNAETAFRAIGGLGLSRCDFFYTDKGEIFLNELNTMPGFTQWSMYPLLWDNMGISYPELIERLVDLAKESFDKREAHLI
|
Cell wall formation.
|
C1CST6
|
Q31JJ8
|
CMOB_HYDCU
|
tRNA U34 carboxymethyltransferase
|
Hydrogenovibrio
|
MKHYHQHYSSFWPKLEEARLGHWQNALEAALETALDPDANGNLPKWLPALETVMAFPSSDSAELSQSAIKAHSQPFSEDDKEKLTQALKAFMPWRKGPFEIEGIYIDTEWHSDWKWDRVSPHLSSLKGRKVLDIGCGSGYHLWRMLGDGAELALGVDPGLLFMTQFLAIKHFVGESLPAYFLPLTLEQLPKTQPSEVFDTVFSMGVLYHRRSPIDHIMDLKRYLKPGGELVLETLVIPDAQGQLLVPKERYAQMNNVWFIPSVQELGHWLEKCGFKNVRCVDLDQTSVKEQRTTEWMNWNSLADFLDPNDSNKTIEGYSAPLRAVMIADKPC
|
Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
|
Q31JJ8
|
B8GTF1
|
PYRE_THISH
|
Orotate phosphoribosyltransferase
|
Thioalkalivibrio
|
MKTYQSEFLAFCLERGVLRFGEFTLKSGRISPYFFNAGLFNTGSDLARLGRFYAQAISESGAAFDMLFGPAYKGIPLAAATAIALAEHHGRDLPWCFNRKEAKDHGEGGSLVGAPLTGRVLIVDDVITAGTAIRESVDIIRAAGAEPVGVAIALNRQERGKGEHSAIQEVEAEYGLKVINIASLGDLIEFMREQGGLDEHLKAVEAYRAQYGV
|
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
|
B8GTF1
|
A4WHI5
|
VATB_PYRAR
|
V-ATPase subunit B
|
Pyrobaculum
|
MLTPVVSYSTVREVKGPLIVIEKTRGVSYGEIGEVVGPDGEPRRVQVIEVGTDYAVAQVLGGTLGLPARGSTVRFYGKTLKIPVSEQLIGRILDGKGQPRDHMPLPPPEDFRDVNGEPLNPYSREYPEEPIETGISAIDGLYTLVRGQKLPIFSGTGLPHNLMAAQVVRQSTVRGSEEGFAVVFVGVGIKTEEALFFMDEFRKTGALRRAVAVLNLASDPVAERVLAPRVGLTIAEYLAWQLGYHVLVVITDMTNYCEGLRELSSGRGELPGRRGYPGYMYTDLATIYERAGKAHGRKGSVTQFPILTMPHDDITHPIPDLTGYITEGQLVLSRAMWGKGIYPPFDVIMSLSRLAKDAIGEGKTREDHKDVANTLIAAYSKALEIRNLATLVGERNLGWRERRYLRFADAFEQKFIKQGYYERRSFEETLDIGWDVLSILPEDELTNARPQITQKFYRRHVYESVQL
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The archaeal beta chain is a regulatory subunit.
|
A4WHI5
|
Q73UN2
|
AROA_MYCPA
|
5-enolpyruvylshikimate-3-phosphate synthase
|
Mycobacterium avium complex (MAC)
|
MTTWTAPLAPQPVHATVTVPGSKSQTNRALVLAALAAAQGRGTPTLSGALRSRDTDLMIGALRTLGLRVDGTGPELTVSGHIAPGPHARVDCGLAGTVLRFVPPLAALADAVVEFDGDEQARARPIAPLLDALRGLGVRIEGTALPFRVHGSGALAGGTVAIDASASSQFVSGLLLCAASFTEGLTVQHTGAALPSAPHIAMTVAMLRQAGVDVDDSVPNRWQVRPGPVAARHWEVEPDLTNAVPFLAAAVVSGGTVRITGWPADSVQPADNILSVLGKLNAVVSQTDSSLEVRGSGSYDGFDVDLRAVGELTPSVAALAALATPGSVSRLSGIAHLRGHETDRLAALSAEINRLGGDCTETPDGLVITATPLRPGVWHAYADHRMAMAGAIVGLRVAGVRVDDIGATSKTLPDFPRLWARMLDASLPDGEEHGM
|
Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
|
Q73UN2
|
Q5F9R5
|
HFQ_NEIG1
|
RNA-binding protein Hfq
|
Neisseria
|
MTAKGQMLQDPFLNALRKEHVPVSIYLVNGIKLQGQVESFDQYVVLLRNTSVTQMVYKHAISTIVPARSVNLQHENKPQAAPASTLVQVETVQQPAE
|
RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
|
Q5F9R5
|
Q53212
|
PRX5_SINFN
|
Glutathione-dependent peroxiredoxin
|
Sinorhizobium
|
MPVKKRVPFVAFRTRVRDETIGGPNPYRWEVRTTEDYFSGKRVVLFSLPGAFTPTCSTQQLPDFERLYDEFGKVGIEAVYCLSVNDAFVMNAWGKALGLEKVRLIPDGSGEFTRKMGMLVAKDNLGFGMRSWRYAAVVNDSVVEQWFEEEGFSDNCESDPYWASSPQNILETLRTFDTARLGRVPIKF
|
Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides.
|
Q53212
|
Q5N4X3
|
ANMK_SYNP6
|
AnhMurNAc kinase
|
Synechococcus
|
MRVLGLISGTSADGIDVAIAEIQGFQADLSVALLAFETIAYEPSLRDRILEVAAGFPLSVAELTALDAAIAQAFATAAQTLIQQHGAVDLIGSHGQTVYHQPLQAGQLGWSVQLGWGAAIAQQTGITTVSNFRSADLALGGQGAPPVPAVDLWLLGSDSENRCVQNIGGIGNLTWLPRRDHPDWQSEVRGWDTGPGNSLLDLAVQKLSQGRLSYDDGSQWAATGQIDQVLCDRWLQEDDYFRLPPPKSTGRERYGWQFLETWAAELDRLTAADQLATLTEFTAASIVNNYRHFLPALPDRVLVCGGGLHNQFLLQRLQQQLPTVKIASTDDFGVNSQAKEAIAIAVLAYWRQHNVPGNLPAVTGASGPALLGDVFART
|
Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
|
Q5N4X3
|
P00236
|
FER2_EQUTE
|
Ferredoxin II
|
Equisetum
|
AYKVTLKTPDGDITFDVEPGERLIDIASEKADLPLSCQAGACSTCLGKIVSGTVDQSEGSFLDDEQIEQGYVLTCIAIPESDVVIETHKEDEL
|
Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
|
P00236
|
Q8R3P6
|
INT14_MOUSE
|
von Willebrand factor A domain-containing protein 9
|
Mus
|
MPTVVVMDVSLSMTRPVSVEGSEEYQRKHLAAHGLTMLFEHMATNYKLEFTALVVFSSLWELMVPFTRDYNTLQEALSNMDDYDKTCLESALVGVCNIVQQEWGGAIPCQVVLVTDGCLGIGRGSLRHSLATQNQRSESNRFPLPFPFPSKLYVMCMANLEELQSTDSLECLERLIDLNNGEGQIFTIDGPLCLKNVQSMFGKLIDLAYTPFHAVLKCGHLTADVQVFPRPEPFVIDEEIDPIPKVINTDLEIVGFIDIADISSPPVLSRHLVLPIALNKEGDEVGAGITDDNEDENSANQIAGKIPNFCVLLHGSLKVEGMVALVQLGPEWHGMLYSQADSKKKSNLMMSLFEPGPEPLPWLGKMAQLGPISDAKENPYGEDDNKSPFPLQPKNKRSYAQNVTVWIKPSGLQTDVQKILRNARKLPEKTQTFYKELNRLRKAALAFGFLDLLKGVADMLERECTLLPDTAHPDAAFQLTHAAQQLKLASTEYAIYDHNITPLHTDFSGSSTERM
|
Probable component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing.
|
Q8R3P6
|
Q144D8
|
URED_PARXL
|
Urease accessory protein UreD
|
Paraburkholderia
|
MSLHENHATLATAQAGAHSQWRARLELGFVREGERTTLKHRLHDGPLRVQRPLYPEGYGVCHAVIVHPPGGIAGGDQLAIDVDVGAGAHAVIATPGATKWYKSNGRAAQQCVGVRVGAGGKLDWLPQNNIVFDQANAKLDFSLMLGDGATALGWDATQLGRQAAGERWSEGSLHAVSRIVGADGELLWFERASLAANDSLREAAQGLDGFSAYGTLWAVGAACDDALAEALTAQLGFDESIRAAASCVTSGVLVVRAVSRSMEMLQKALTRCWVQLRPVVHGVQGVPLRIWAT
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q144D8
|
O14917
|
PCD17_HUMAN
|
Protocadherin-68
|
Homo
|
MYLSICCCFLLWAPALTLKNLNYSVPEEQGAGTVIGNIGRDARLQPGLPPAERGGGGRSKSGSYRVLENSAPHLLDVDADSGLLYTKQRIDRESLCRHNAKCQLSLEVFANDKEICMIKVEIQDINDNAPSFSSDQIEMDISENAAPGTRFPLTSAHDPDAGENGLRTYLLTRDDHGLFGLDVKSRGDGTKFPELVIQKALDREQQNHHTLVLTALDGGEPPRSATVQINVKVIDSNDNSPVFEAPSYLVELPENAPLGTVVIDLNATDADEGPNGEVLYSFSSYVPDRVRELFSIDPKTGLIRVKGNLDYEENGMLEIDVQARDLGPNPIPAHCKVTVKLIDRNDNAPSIGFVSVRQGALSEAAPPGTVIALVRVTDRDSGKNGQLQCRVLGGGGTGGGGGLGGPGGSVPFKLEENYDNFYTVVTDRPLDRETQDEYNVTIVARDGGSPPLNSTKSFAIKILDENDNPPRFTKGLYVLQVHENNIPGEYLGSVLAQDPDLGQNGTVSYSILPSHIGDVSIYTYVSVNPTNGAIYALRSFNFEQTKAFEFKVLAKDSGAPAHLESNATVRVTVLDVNDNAPVIVLPTLQNDTAELQVPRNAGLGYLVSTVRALDSDFGESGRLTYEIVDGNDDHLFEIDPSSGEIRTLHPFWEDVTPVVELVVKVTDHGKPTLSAVAKLIIRSVSGSLPEGVPRVNGEQHHWDMSLPLIVTLSTISIILLAAMITIAVKCKRENKEIRTYNCRIAEYSHPQLGGGKGKKKKINKNDIMLVQSEVEERNAMNVMNVVSSPSLATSPMYFDYQTRLPLSSPRSEVMYLKPASNNLTVPQGHAGCHTSFTGQGTNASETPATRMSIIQTDNFPAEPNYMGSRQQFVQSSSTFKDPERASLRDSGHGDSDQADSDQDTNKGSCCDMSVREALKMKTTSTKSQPLEQEPEECVNCTDECRVLGHSDRCWMPQFPAANQAENADYRTNLFVPTVEANVETETYETVNPTGKKTFCTFGKDKREHTILIANVKPYLKAKRALSPLLQEVPSASSSPTKACIEPCTSTKGSLDGCEAKPGALAEASSQYLPTDSQYLSPSKQPRDPPFMASDQMARVFADVHSRASRDSSEMGAVLEQLDHPNRDLGRESVDAEEVVREIDKLLQDCRGNDPVAVRK
|
Potential calcium-dependent cell-adhesion protein.
|
O14917
|
B3LN00
|
MKAR_YEAS1
|
Microsomal beta-keto-reductase
|
Saccharomyces
|
MTFMQQLQEAGERFRCINGLLWVVFGLGVLKCTTLSLRFLALIFDLFLLPAVNFDKYGAKSGKYCVITGASDGIGKEFARQMAKRGFNLVLISRTQSKLEALQKELEDQHHVVVKILAIDIAEDKESNYESIKELCAQLPITVLVNNVGQSHSIPVPFLETEEKELRDIITINNTATLLITQIIAPKIVETVKAENKKSGTRGLILTMGSFGGLIPTPLLATYSGSKSFLQSWSNSLAGELSKDAIDVELIISYLVTSSMSKIRRSSLMIPNPQQFVKSTLRSVGRRCGSQERYATMTPYWAHAVYQFVITETFGVYSKIVNSINYSFHKSIRIRALKKAARQVKKE
|
Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
|
B3LN00
|
Q9HCN3
|
PGAP6_HUMAN
|
Transmembrane protein 8A
|
Homo
|
MGRAGTGTGGEAVAAVVAGPLLLLLLARPPPASAGYSGKSEVGLVSEHFSQAPQRLSFYSWYGSARLFRFRVPPDAVLLRWLLQVSRESGAACTDAEITVHFRSGAPPVINPLGTSFPDDTAVQPSFQVGVPLSTTPRSNASVNVSHPAPGDWFVAAHLPPSSQKIELKGLAPTCAYVFQPELLVTRVVEISIMEPDVPLPQTLLSHPSYLKVFVPDYTRELLLELRDCVSNGSLGCPVRLTVGPVTLPSNFQKVLTCTGAPWPCRLLLPSPPWDRWLQVTAESLVGPLGTVAFSAVAALTACRPRSVTIQPLLQSSQNQSFNASSGLLSPSPDHQDLGRSGRVDRSPFCLTNYPVTREDMDVVSVHFQPLDRVSVRVCSDTPSVMRLRLNTGMDSGGSLTISLRANKTEMRNETVVVACVNAASPFLGFNTSLNCTTAFFQGYPLSLSAWSRRANLIIPYPETDNWYLSLQLMCPENAEDCEQAVVHVETTLYLVPCLNDCGPYGQCLLLRRHSYLYASCSCKAGWRGWSCTDNSTAQTVAQQRAATLLLTLSNLMFLAPIAVSVRRFFLVEASVYAYTMFFSTFYHACDQPGEAVLCILSYDTLQYCDFLGSGAAIWVTILCMARLKTVLKYVLFLLGTLVIAMSLQLDRRGMWNMLGPCLFAFVIMASMWAYRCGHRRQCYPTSWQRWAFYLLPGVSMASVGIAIYTSMMTSDNYYYTHSIWHILLAGSAALLLPPPDQPAEPWACSQKFPCHYQICKNDREELYAVT
|
Involved in the lipid remodeling steps of GPI-anchor maturation. Lipid remodeling steps consist in the generation of 2 saturated fatty chains at the sn-2 position of GPI-anchor proteins (GPI-AP). Has phospholipase A2 activity that removes an acyl-chain at the sn-2 position of GPI-anchors during the remodeling of GPI. Required for the shedding of the GPI-AP TDGF1, but not CFC1, at the cell surface. Shedding of TDGF1 modulates Nodal signaling by allowing soluble TDGF1 to act as a Nodal coreceptor on other cells . Also indirectly involved in the translocation of RAC1 from the cytosol to the plasma membrane by maintaining the steady state amount of CAV1-enriched plasma membrane subdomains, stabilizing RAC1 at the plasma membrane . In contrast to myomaker (TMEM8C), has no fusogenic activity .
|
Q9HCN3
|
A5EX78
|
RS19_DICNV
|
30S ribosomal protein S19
|
Dichelobacter
|
MARSLKKGFFIDLHLAHKVDVAVETKSKKPIKTWSRRSMIIPDMIGLTIAIHNGKQHVPVLITEDMIGHKLGEFAPTRNYRGHTAADKKGK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
A5EX78
|
Q3JAM9
|
QUEA_NITOC
|
Queuosine biosynthesis protein QueA
|
Nitrosococcus
|
MQLSDFTYNLPKQLIAQYPPKRRGESRLLSLEGASGIVKDRQFIELPELLSTKDLLIFNNTKVIPARIQGTKDSGGKIEILIERFLDQHRALAHIRANNPPRAGRRLVMEQSVEVEVKGRVKELFELRFLDPRPLPQLLEAIGQMPLPPYIQRKTVPVDKERYQTIYASRPGAVAAPTAGLHFDKPLLKRLQAQGIRSGYITLHVGAGTFQPVRVKNITQHQMHSEYVEVSEQICAQIRDTQQAGGRVVAVGTTTVRALEAASAKGVIAPYQGETEIFIFPGHRFHTVNALITNFHLPETTLLMLVCAFAGSEHVLAAYRHAIKKGYRFFSYGDAMFITEAKTG
|
Transfers and isomerizes the ribose moiety from AdoMet to the 7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give epoxyqueuosine (oQ-tRNA).
|
Q3JAM9
|
Q6AR56
|
ARGB_DESPS
|
NAG kinase
|
Desulfotalea
|
MNDTVEKSIERAKVLIESLPYMQEFRHKTIVIKYGGHAMVDEALKKQFALDVILLKQIGINPIIVHGGGPQINNLLDRLDIKPSYVQGMRVTDGETMDVVEMVLVGKVNKEIVGLINHCGGKAVGLSGRDGDLVCAEQLQMNQAQVGDNPPELIDVGRVGQVTKINSHVLETLSQDDFIPIIAPVGVGEDGRAFNINADLVASAIAAELSAEKLILLTDVPGVKNKAGDLLTTLEWQELNGLIEDGTIMGGMIPKVRCCEDAVKGGVAKTYIVDGRVEHAILLEIFTRDGVGTEIY
|
Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate.
|
Q6AR56
|
P07451
|
CAH3_HUMAN
|
Carbonic anhydrase III
|
Homo
|
MAKEWGYASHNGPDHWHELFPNAKGENQSPVELHTKDIRHDPSLQPWSVSYDGGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLPGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFKEALKQRDGIAVIGIFLKIGHENGEFQIFLDALDKIKTKGKEAPFTKFDPSCLFPACRDYWTYQGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLLSSAENEPPVPLVSNWRPPQPINNRVVRASFK
|
Reversible hydration of carbon dioxide.
|
P07451
|
Q83IC2
|
RL9_TROW8
|
50S ribosomal protein L9
|
Tropheryma
|
MTRVILVQDVNGLGSVGDVVEVKAGYSRNYLVPKGMAVRWTEGAQKHIGDISAARRAREAAALQEARDIANTLTKEAVTRELRLAANAGEDGRLFGSVTAANIAKVLSSASGHKIDRGKIEIDSPIKTLGEHTVKVKLHPNVKVDINVVVYAE
|
Binds to the 23S rRNA.
|
Q83IC2
|
Q7N963
|
THIC_PHOLL
|
Thiamine biosynthesis protein ThiC
|
Photorhabdus
|
MSHNTVIPTTDISPKPDPARPRKAQRDAAQEFINSIQGVTFPNSRRIYLQGSRDDIQVPMREIQLSPTLIGGTKEEPQYEENEAIPVYDTSGAYGDPDAKLDVHVGLTQLRQPWIDERQDTEPVAALSSDFTQQRLTDAGLDHLRFNHRPHPLKARKDKRVTQLHYARQGIITPEMEFIALRENMGRERIRGDVLRQQHPGQSFGAQLPENITPEFVRQEVAAGRAIIPANINHPESEPMIIGRNFLVKVNANIGNSSVTSSIEEEVEKLIWSTRWGADTVMDLSTGRYIHETREWILRNSPVPIGTVPIYQALEKVNGGAENLTWEIFRDTLLEQAEQGVDYFTIHAGVLLRYVPMTAKRLTGIVSRGGSIMAKWCLSHHQENFLYQHFREICEICAAYDVSLSLGDGLRPGSIQDANDEAQFAELHTLGELTKIAWEYDVQVMIEGPGHIPMQMIRRNMTEELEHCHEAPFYTLGPLTTDIAPGYDHFTSGIGAAMIGWFGCAMLCYVTPKEHLGLPNKDDVKQGLITYKIAAHAADLAKGHPGAQIRDNAMSKARFEFRWEDQFNLALDPDTARAYHDETLPQASGKIAHFCSMCGPKFCSMKISQEVRDYAAGMEQMSEAFRAHGSELYHSVEDVSHEQSA
|
Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction.
|
Q7N963
|
P06284
|
ATPB_MARPO
|
F-ATPase subunit beta
|
Marchantia
|
MKTNFLAFGMSTLVAKNIGSITQVIGPVLDVAFSPGKMPNIYNSLIVKDQNSAGEEINVTCEVQQLLGNNKVRAVAMSATDGMMRGMKVIDTGAPLTVPVGEATLGRIFNVLGEPVDNLGPVEVTTTFPIHRAAPAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNILKAHGGVSVFGGVGERTREGNDLYMEMKESKVINEQNISESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGTLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPWIVGEEHYETAQGVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVSLRETIKGFQMILSGELDSLPEQAFYLVGNIDEATAKAATLQVES
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
P06284
|
Q744V6
|
RS6_MYCPA
|
30S ribosomal protein S6
|
Mycobacterium avium complex (MAC)
|
MRPYEIMVILDPTLDERTVAPSLETFLNVVRKDGGSVEKVDIWGRRRLAYEIAKHAEGIYVVIDLKAEPATVSELDRQLSLNESVLRTKVMRTDKH
|
Binds together with S18 to 16S ribosomal RNA.
|
Q744V6
|
Q0BZ42
|
RL21_HYPNA
|
50S ribosomal protein L21
|
Hyphomonas
|
MFAVIKTGGKQYKVAEGDTIVIERLAAAAGETVTFDSVLMVGAGAGVTVGAPMVAGATVTGEVAAEVRGPKLITRKKRQRQTYRRTIGHRQDLMEVTITSINTDGKAPAKKAAAKKEEAPKADTAPKAAAAPTEEAAAGGDNLKKITGIGPALEKKLNAAGITTFAQIAALSADDIAKLEEELSLAGRFAKDGWVEQAAELAKEA
|
This protein binds to 23S rRNA in the presence of protein L20.
|
Q0BZ42
|
Q68EZ2
|
FOXJ2_XENLA
|
Forkhead box protein J2
|
Xenopus
|
MASDLGSSLTSIDWLPQLTIQASIKGSQQNSVGRKGPGSPADPSAMLSKEEAAAHRDGKPPYSYANLIQYAINSAPAKRMTLSEIYRWICDNFPYYRSAGVGWKNSIRHNLSLNKCFRKVPRPRDDPGKGSYWMIDSCPKEDITLPRRKRPHPDDEVSQDSFEQEVNKSPLSSASEVSMPQEATQGHPMNNNSPLPTYSQANPTQMPPDSRAPTYNNNDCYKFSFSESTFPDLSCSFRSLYHSLLGKQGERGDKDLYNSMQSKQVLPPVHSEVQSSSCCMYQQNSGAAPSNLHPHNVPSISGLPPSHHQAQHQQPPYLPQQQMPRPPAPGMSLGLPSDWCSNIDSLKESFKIVSSLDWSSVDLSQFSDLMESLRQAELKNWSLDQDHIASLCDSLSHLLSTTGLLPQNHGQPPSCQAPCMPPTTSSACALRGGKPGHNMAVNSYGQNQPPPVSCGHTFTVSSGYPTQSQAPPTYSQQGRHPHRALYPPQRPTLRYPQSSDDIQDDFDWDSIA
|
Transcriptional activator.
|
Q68EZ2
|
Q2YAI3
|
APT_NITMU
|
Adenine phosphoribosyltransferase
|
Nitrosospira
|
MQIKSRIRTIAHYPHEGIMFRDITTLLKDPVGLRATIQEIASRYKSMKIDKVAGIESRGFIIGAPVAYELGVGFVPVRKKGKLPAETRGRDYQLEYGSDRIEIHVDAIQKGDRVLLVDDLIATGGTAEAAAGLIHEMGGEVVECSFVIDLPDIGGRARLEDQGLKVFALCEFEGN
|
Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis.
|
Q2YAI3
|
P85045
|
LYS_BUFGA
|
1,4-beta-N-acetylmuramidase C
|
Bufo
|
SGKYISWEDSCSYLQLQKYERCELAKALKKGGLADFKGYSLENWICTAFHESGYNTASTNYNPPDKSTDYGIFQINSRWWCNDYKTPRSKNTCNIDCKVLLGDDISPAIKCAKRVVSDPNGMGAWVAWKKYCKGKNLSQWTQGCKL
|
Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has antibacterial activity against the Gram-positive bacterium S.aureus and against the Gram-negative bacterium E.coli with a MIC of 1 uM and 8 uM respectively. No antifungal activity against C.albicans.
|
P85045
|
A4XI31
|
RPOC_CALS8
|
Transcriptase subunit beta'
|
Caldicellulosiruptor
|
MDLFNFDAIKISLASPEKIREWSRGEVKKPETINYRTLKPEKDGLFCEKIFGPTKDWECHCGKYKKVKYKGVVCDKCGVEVTKSKVRRERMGHIELAAPVSHIWYFKGVPSRMGLILDMTPRNLEKVLYFAAYVVIDPGDVPNLEKKQILSEKEYRELKEKYGDRFRAGMGAEAIKELLKEIDLDKLSQELRQELETATGQKKLKIIKRLEVVEAFRKSGNRPEWMILDVIPVIPPELRPMVQLDGGRFATSDLNDLYRRVINRNNRLKKLMELGAPDIIIRNEKRMLQEAVDALIDNGRRGRPVTGPGNRPLKSLSDMLKGKQGRFRQNLLGKRVDYSGRSVIVVGPELKIYQCGLPKEMALELFKPFVMKKLVEKGICNNIKNAKKAVERQRSEVWDILEEVIKDHPVLLNRAPTLHRLGIQAFEPVLVEGRAIRLHPLVCTAYNADFDGDQMAVHVPLSAEAQAEARFLMLSANNLLKPADGKPIVVPTQDMVLGIYYLTLEKKGDKGEGKIFSSEDEALLAYEHKVVGLHARIKVRRTIEKDGEVVSGIVETTPGKIILNQVIPQDLGFVDRSKKENLLKYEIDTLVDKKMLGKIIDRCIKVYGTTRTAEILDEIKELGFRFSTRGAITISVSDMVIPEVKQKLIAEAEQKVENIEKLYRHGLISDEERYEQVISIWNETKDKLTEELIQNLDEFNPIFMMASSGARGSKNQISQLAGMRGLMANPSGKTIEMPIKSNFREGLNVIEFFISTHGARKGLADTALRTADSGYLTRRLVDVAQDIIVREEDCGTEKGIEVSEIRDGTEVIETLEERIIGRYAAKDIINEKTGEVIVKRNELITEEIAKKIVDAGEKSVYVRSVLECKTRYGVCTKCYGLDLGTGQPVNVGEAVGIIAAQAIGEPGTQLTMRTFHTGGIAGQDITQGLPRVEELFEARKPKGVAIISEIEGYVSIKEDKKRTITVRNDNGEERTYEVPYGARLKVNDGDYVKAGDELTEGSINPHDLLRIKGPRGVQSYLLAEVQKVYKMQGVDINDKHIEIIIRQMMKKVKIEDPGDTELLPGDIVEIYRFEEENDRAIAEGKRPALGRRVLLGITKAALSTESFLSAASFQETTRVLTDAAIKGKVDPLIGLKENVIIGKLIPAGTGMAKYRNIIVEEKA
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
A4XI31
|
Q0DHE3
|
ZIP9_ORYSJ
|
ZRT/IRT-like protein 9
|
Oryza sativa
|
MAFDLKLTACLLLAVFSLAAAADCECQPSDEGHDAAKSRTLKVIAIFCILVGSSAGCAIPSLGRRFPALRPDTSLFFALKAFAAGVILATAFVHILPVSFDKLGSPCLVDGPWRKYPFTGLVAMLAAVATLLLDTIATGYFLQRAQDSRGAVAAVAACGGDASSSHDHERGNAHGVSSAVIASATMPNDAADDCDDAEDRAKLVRHRVISQVFELGIIVHSIIIGISLGASESPSTIRPLVAALTFHQFFEGIGLGGCIVQARFHLKSAVTMAIFFSLTTPVGIMIGIGISSAYNENSPTALIVEGILDAAAAGILNYMALVDLLAEDFMNPRVRKSGRLQLIISILLLVGIALMSLLGIWA
|
Zinc transporter that may be involved in zinc uptake from the rhizosphere.
|
Q0DHE3
|
B7LUN8
|
ARGE_ESCF3
|
N-acetylornithinase
|
Escherichia
|
MKNKLPPFIEIYRALIATPSISATEEALDQSNAGLITLLADWFKDLGFNVEVQPVPGTRNKFNMLASTGQGAGGLLLAGHTDTVPFDDGRWTRDPFTLTEHDGKLYGLGTADMKGFFAFILDTLRDVDVTKLKKPLYILATADEETSMAGARYFSETTSLRPDCAIIGEPTSLQPVRAHKGHISNTIRVMGQSGHSSDPARGVNAIELMHDAIGHILQLRDTLKERYHYEAFTVPYPTLNLGHIHGGDAANRICACCELHMDIRPLPGMTLNDLNGLLNEALAPVSERWPGRLTVEELHPPIPGYECPPDHQLVEVVEKLLGTHTEVVNYCTEAPFIQTLCPTLVLGPGSINQAHQPDEYLETRFIKPTRELITQVIHHFCWH
|
Catalyzes the hydrolysis of the amide bond of N(2)-acetylated L-amino acids. Cleaves the acetyl group from N-acetyl-L-ornithine to form L-ornithine, an intermediate in L-arginine biosynthesis pathway, and a branchpoint in the synthesis of polyamines.
|
B7LUN8
|
B2ZBA0
|
DSK_DROTE
|
Drosulfakinin II
|
Sophophora
|
MGLRSCTHFATLVMPLWALAFCFLVLVPVPAQTTSLQISKGDRRLQDLESNMGAESDQPNANLVGTSLSRFGDKRNQKIITFGRRVPRPIIPIELDLLMDNDDENTKAKRFDDYGHMRFGKRGGDDQFDDYGHMRFGR
|
Drosulfakinin-0 (DSK 0) plays diverse biological roles including regulating gut muscle contraction in adults but not in larvae.
|
B2ZBA0
|
Q1IHH2
|
RL10_KORVE
|
50S ribosomal protein L10
|
Candidatus Koribacter
|
MAVTKAKKIEVTEKLTEDFKKANHAIVGTFNKLTVSKDYELRKAVRSVGGKYSVVKNTLAERAAKGTKIEDAVKGLAGVTSVAFTDGDPVQLAKVLSKYAKDNPEYEFKAGVVDGKVIKLADIDALANMPSKEELYSKLLFLISAPAQRLVTVMNATGRDLAVVLNQGVEKQKFSGGEAPAQ
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q1IHH2
|
Q326G3
|
LEUC_SHIBS
|
Isopropylmalate isomerase
|
Shigella
|
MAKTLYEKLFDAHVVYEAENETPLLYIDRHLVHEVTSPQAFDGLRAHGRPVRQPGKTFATMDHNVSTQTKDINACGEMARIQMQELIKNCKEFGVELYDLNHPYQGIVHVMGPEQGVTLPGMTIVCGDSHTATHGAFGALAFGIGTSEVEHVLATQTLKQGRAKTMKIEVQGKAAPGITAKDIVLAIIGKTGSAGGTGHVVEFCGEAIRDLSMEGRMTLCNMAIEMGAKAGLVAPDETTFNYVKGRLHAPKGKDFDDAVAYWKTLQTDEGATFDTVVTLQAEEISPQVTWGTNPGQVISVNDNIPDPASFADPVERASAEKALAYMGLKPGIPLTEVAIDKVFIGSCTNSRIEDLRAAAEIAKGRKVAPGVQALVVPGSGQVKAQAEAEGLDKIFIEAGFEWRLPGCSMCLAMNNDRLNPGERCASTSNRNFEGRQGRGGRTHLVSPAMAAAAAVTGHFADIRNIK
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
Q326G3
|
Q0HT42
|
QUEF_SHESR
|
PreQ(0) reductase
|
Shewanella
|
MTHNHDPYSDAKELAGLTLGKATDYQAEYDASLLQGVPRSLNRNAINLTAESLPFHGADIWTAYELSWLNAKGKPMVAIADIQLSHESQNLIESKSFKLYLNSFNQTKFDNIDAVQKTLVQDLGECAQGQVTVKIIEPKSFGIQRVVELPGTCIDDLDIEVSDYDFNPDYLENSTDDKQIVAETLNSNLLKSNCLITSQPDWGSVMIRYQGPKIDREKLLRYLISFRQHNEFHEQCVERIFVDLKHYCHCTKLTVYARYTRRGGLDINPYRSDFEHPGESHRLARQ
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
|
Q0HT42
|
B2INX0
|
PLSY_STRPS
|
Lysophosphatidic acid synthase
|
Streptococcus
|
MITIVLLILAYLLGSIPSGLWIGQVFFQINLREHGSGNTGTTNTFRILGKKAGMATFVIDFFKGTLATLLPIIFHLQGVSPLIFGLLAVIGHTFPIFAGFKGGKAVATSAGVIFGFAPIFCLYLAIIFFGALYLGSMISLSSVTASIAAVIGVLLFPLFGFILSNYDFLFIAIILALASLIIIRHKDNIARIKNKTENLVPWGLNLTHQDPKK
|
Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP.
|
B2INX0
|
P06615
|
REDF_ECOLI
|
Protein D
|
Escherichia
|
MSGSVIHSQSAVMVPAVYSAGQPASLPVAIDYPAALALRQMSMVHDELPKYLLAPEVSALLHYVPDLHRKMLLATLWNTGARINEALALTRGDFSLAPPYPFVQLATLKQRTEKAARTAGRMPAGQQTHRLVPLSDSWYVSQLQTMVAQLKIPMERRNRRTGRTEKARIWEVTDRTVRTWIGEAVAAAAADGVTFSVPVTPHTFRHSYAMHMLYAGIPLKVLQSLMGHKSISSTEVYTKVFALDVAARHRVQFAMPESDAVAMLKQLS
|
Acts as a repressor of transcription and as a site-specific resolvase that cleaves at the RfsF site.
|
P06615
|
B2UC26
|
YCIB_RALPJ
|
Inner membrane-spanning protein YciB
|
Ralstonia
|
MKFLFDLFPVILFFAAFKVAGIYVATTVAMVATVLQIAWVWFKHRKVDAMQWLSLLIIGVFGGATLIFHNETFIKWKPTVLYWLFGVVLLGSVVVVRKNLIRAMMEQQVSLPETMWGRLNLVWALFFLVMGCLNLYVAYNFDTDVWVNFKLFGSMGLMVVFILAQSVWLARHMQERPANAANDANIGDDR
|
Plays a role in cell envelope biogenesis, maintenance of cell envelope integrity and membrane homeostasis.
|
B2UC26
|
Q5E5B6
|
PYRD_ALIF1
|
Dihydroorotate oxidase
|
Aliivibrio
|
MLYRIARAGIFKLDAEKAHDLAIQNFKRFNGTPLDIFYRQNLASKPVEVMGIKFKNPVGLAAGLDKNGECIEAFGAMGFGFVEVGTVTPRPQSGNDKPRLFRLIEAEGIINRMGFNNLGVDNLVENVKKAKYDGVIGINIGKNKDTPIEKGTEDYLICMEKVYQYAGYIAVNISSPNTPGLRTLQYGEALDDLLSQLKEKQKELAEKYGKYVPVALKIAPDLEDDELTQIAESLIKYKIDGVIATNTTLDRSMVEGMKHAEEMGGLSGRPVQTRSTEVVRRLKELLGDNLPIIGVGGIDSYVAAKEKMVAGAELVQVYSGFIYKGPGLVRDIVNNI
|
Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor.
|
Q5E5B6
|
C3PFX1
|
ILVC_CORA7
|
Ketol-acid reductoisomerase type I
|
Corynebacterium
|
MAIETLYDSDADLTIIQGRKVAIIGYGSQGHAHAMNLRDSGVEVAIGLREGSKSREKAEEAGFKVLTNAEAAKWADVIMLLAPDTSQAAIFTEDIEPNLEDGNALFFGHGLNIHFGLIKPAENITIGMVAPKGPGHLVRRQFVDGKGVPCLIATEQDPKGEGRELTLSYAAAIGGARAGVIPTTFKDETETDLFGEQAVLCGGVEYLIMNGFEVLTEAGYEPEMAYFEVCHELKLIVDLIVEGGIKNMNYSCSDTAEFGGYLSGPRVIDASVKERMKDVLTDIQDGTFVKRLVANVEGGNKELEDLRAKVNSHPIEQTGSQLRDLMSWVKNPLDATA
|
Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
|
C3PFX1
|
A5G9J8
|
GATB_GEOUR
|
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
|
Geotalea
|
MKYQVVIGLEVHVQLLTNSKIFCGCSTRFGAEPNSQTCPVCLGMPGALPVLNKKVVEYAIRAGLATNCRIAPRSVFARKNYFYPDLPKGYQISQFELPICIDGHLDIEVEGGMKRIGITRIHMEEDAGKLVHADVPGVGDDSCVDLNRACTPLLEIVSEPDMRSADEAVAYLKKLHQIVVYLGISDGNMEEGSFRCDANVSVMPAGSDKFGTRTETKNVNSFKFVKQAIEYEIERQIEVIEEGGKIVQETRLFDPNTGSTRSMRGKEEAHDYRYFPDPDLVPLVIGNDWVEDARLSLPELPDAKRQRYTDELGLPVYDAEVLTATRELAGYFEACLALSPQPKPVANWVMGEVTRALNEENRSIADCPVTPPLLADLLRLIEKGTISGKIAKTVFDEMWRSGKAPEKIVEEKGLVQVSDTGAIEAIIDEVLAKEAGQVEEYRSGKDKLFGFFVGQVMRASKGKANPALVNEILLKKLNG
|
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
|
A5G9J8
|
C3PLI9
|
LPXK_RICAE
|
Lipid A 4'-kinase
|
spotted fever group
|
MIKLLYPEFWQKRNIIAYLLLPISVIYQFLGYLRASLARPIMLPAKVICVGNCSVGGTGKTQIVMYLAKLLKARNVSFVIVTKAYGSNLTSATTIHQGHTALEVGDEGVILAKYGAVIATKNIKEIVPLLNELKPDIIIVDDFLQNPYFHKDFTIVSVDSQRLFGNGFLIPAGPLRQYPNKALDAADLIFLVSSHQDKIPNILTPYVNKLINAQIVPSNNIDKTKNYFAFSGIGNPERFFATLKNYGLNITGYKIFPDHYNYLQADLENLYSLAKEHNATLVTTRKDHVKFNDLNNNIVCLDVELSINHPDLLNEKIFKKA
|
Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
|
C3PLI9
|
Q6DE15
|
B3G5B_XENLA
|
UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5B
|
Xenopus
|
MLISARRLRRCQSLQLLASCFVLSLMALLVQEDNSLVNHVKSYSYRYLINSYNFVNDSLSVPRDRSDGAAGYRYLINNRHKCLNEDVLLLLFVKTAPENRRRRNAIRKTWGNEDYIRSRYAANIKVVFALGVERDPVKSHHTQQDLVNENKRFKDLIQQDFSDTFHNLTLKLLLQFGWVNSFCPSAKFIMSADDDIFVHTPNLVTYLKSLPIETQDFWIGRVHRGSPPIRSKASKYYVPYEMYPWSSYPDYTAGAAYVVSRDVAAKVYEASQTLNTSLYIDDVFMGICANKMGVVPQYHVYFSGEGKSPYHPCIYNKMMTSHGHLGDLDYLWRQATDSNVKSLSSGFLGNVYCKIVNIMLLCKIGYVDTYPCSAAWS
|
Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids.
|
Q6DE15
|
C0Q067
|
ARNT_SALPC
|
Undecaprenyl phosphate-alpha-L-Ara4N transferase
|
Salmonella
|
MMKSIRYYLAFAAFIALYYVIPVNSRLLWQPDETRYAEISREMLASGDWIVPHFLGLRYFEKPIAGYWINSLGQWLFGATNFGVRAGAILTTLLAAALVAWLTFRLWRDKRTALLASVIFLSLFAVYSIGTYAVLDPMIALWLTAGMCCFWQGMQATTRTGKIGMFLLLGATCGLGVLTKGFLALAVPVVSVLPWVIVQKRWKDFLLYGWLAVLSCFVVVLPWAIAIARREADFWHYFFWVEHIQRFAMSDAQHKAPFWYYLPVLLAGSLPWLGLLPGALKLGWRERNGAFYLLGWTIMPLLFFSIAKGKLPTYVLSCFAPIAILMARFVLHNVKEGIAALRVNGGINLVFGLVGIVTAFVVSSWGPLKSPVWTHIETYKVFCVWGVFTVWAFVGWYSLCHSQKYLLPAFCPLGLALLFGFSVPDRVMESKQPQFFVEMTQAPLASSRYILADSVGVAAGLAWSLKRDDIMLYGHAGELRYGLSYPDVQNKFVKADDFNAWLNQHRQEGIITLVLSIDKDEDISALSLPPADNVDYQGRLVLIQYRPK
|
Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
|
C0Q067
|
B5Z950
|
RSMA_HELPG
|
S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase
|
Helicobacter
|
MVVAKKSLGQHFLTDESFLDRIVNALPPLNPLKLIEIGVGLGDLTLKLLDRYPLKTYEIDSNLCEKMRARLKAQKKPFQLELVEKDALFLKEEEPYFLISNLPYYIATRLVLNALKDPKCRGLLVMTQKEVALKFCTKDSQNALSVLVHTIGNATLLFDVPPSAFSPPPKVFSSVFEVIKEPLKEKALASLLQAPFFEEALQKGFETLEDFLKACFSSPRKTLSNNLKKSVSYREKLDKVLDFLALENQPTSVRASEIKDYLKLLEYLLKG
|
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
|
B5Z950
|
Q7NPZ4
|
MURE_CHRVO
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Chromobacterium
|
MKSRLTALPDWDPALLQQLGLPIKRVEADSRRVLPGDVFLACRGEYADGRDFIPAALEKGAAAVLWDEADGFAWKAEWQAPNLAVPNLRERAGIVAAHVLGLPSRDLTVVGITGTNGKTSISHWLAQAFSLLGQKAALIGTVGNGFYGHLTETTHTTPDPVTVQQKLAEYRRQGAHVVTMEVSSHGLDQFRVNGVEFATAVFTNLTRDHLDYHGSMEAYGESKKKLFFWEGLKHAVINADDAFGRQLAAGIDPKQTRVVTYGLEQGDVRPLALAATLEGLQLTVATPWGTVDVRTGLVGRFNAANLLACLATLCVNGVSLQDAAAVMARIQPARGRMQSVGGAHEPLVVIDYAHTPDALEKALATLSEIRPAGGRLFCVFGCGGDRDPGKRPMMGAIAEKHADVAVLTSDNPRSEDPQAIIRDVLAGMDAARAHVEADREAAIHWAVAQARVGDVVLVAGKGHEEYQDIAGVKRPFSDFRVAEEALTAWGKRP
|
Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan.
|
Q7NPZ4
|
F4HUC4
|
ATCA5_ARATH
|
Alpha carbonate dehydratase 5
|
Arabidopsis
|
MKIPSIGYVFFLIFISITIVSSSPDHGEVEDETQFNYEKKGEKGPENWGRLKPEWAMCGKGNMQSPIDLTDKRVLIDHNLGYLRSQYLPSNATIKNRGHDIMMKFEGGNAGLGITINGTEYKLQQIHWHSPSEHTLNGKRFVLEEHMVHQSKDGRNAVVAFFYKLGKPDYFLLTLERYLKRITDTHESQEFVEMVHPRTFGFESKHYYRFIGSLTTPPCSENVIWTISKEMRTVTLKQLIMLRVTVHDQSNSNARPLQRKNERPVALYIPTWHSKLY
|
Reversible hydration of carbon dioxide.
|
F4HUC4
|
Q824Y6
|
NQRA_CHLCV
|
NQR-1 subunit A
|
Chlamydia
|
MKIAITRGLDLSLQGSPKESGFLKRIDPALVSVDLRPYSALALKLKVEQDDVISSGSPIAEYKNFPGVFITSPVSGIVKEIRRGEKRSLLDVVIKKTPGQNLTEYSYDLSKLSRAELLEIFKKEGLFALFKQRPFDIPALPTQTPRDVFINLADNRPFTPSTEKQLAVFSSREEGFYVFNVGVRAVAKLFGLCPHIVSTDRLALPEKDLKSIAHLHKITGPYPSGSPSTHIHYIAPITNEKDIVFTLSFQEVLTIGHLFLKGRILNEQVVALAGSGLKSSLRRYVITTKGANFESLLPLQDISSDVSLISGDPLTGRLCDRESLPCLGMRDSTISVLPNPKTRQAFNFLRLGINKPTHTRTYLSGFLKRKHTYMDPDTNLHGETRPIIDTEIYDKVMPLKIPVVPLIKAVITKDFELACMLGFLEVCPEDFALPTFIDPSKTEMLTIIKDALKDYAKETGILNLEYEDKE
|
NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
|
Q824Y6
|
B9DI94
|
RNPA_STACT
|
Protein C5
|
Staphylococcus
|
MEKAYRIKKNSDFQAIYRRGKSVANRQFVIYMMPDKGLTHFKLGISVSKKLGNAVTRNRIKRAIRENFKVHKDDMLPRNIIVIARHPAKDMTVLEIQKSLEHVLKVAKLFNKRIK
|
RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
|
B9DI94
|
Q2YTP0
|
MENE_STAAB
|
o-succinylbenzoyl-CoA synthetase
|
Staphylococcus
|
MDFWLYKQAQQNGHHIAITDGQESYTYQNLYCEASLLAKRLKAYQQSRVGLYIDNSIQSIILIHACWLANIEIAMINTRLTPNEMKNQMRSIDVQLIFCTLPLELRGFQIVLLDDIEFAGRDITMNGLLDNTMDIQYDTSNETVVPKDSPSNILNTSFNLDDIASIMFTSGTTGPQKAVPQTFRNHYASAIGCKESLGFDRDTNWLSVLPIYHISGLSVLLRAVIEGFTVRIVDKFNAEQILTMIKNERITHISLVPQTLNWLMQQGLHEPYDLQKILLGGAKLSATMIETALQYNLPIYNSFGMTETCSQFLTATPQMLHARPDTVGMPSANVDVKIKNPNKEGHGELMIKGANVMNGYLYPTDLTGTFENGYFNTGDIAEIDYEGYVMIYDRRKDLIISGGENIYPYQIETVAKQFPGISDAVCVGHPDDTWGQVPKLYFVSESDISKAQLIAYLSQHLAKYKIPKHFEKVDTLPYTSTGKLQRNKLYRG
|
Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).
|
Q2YTP0
|
Q0HH38
|
PSTB_SHESM
|
Phosphate-transporting ATPase
|
Shewanella
|
MISIDSTAMKTNNFDLANLSQNDTALEIRNLDLRYGDKQALFNVSMKIPKKQVTAFIGPSGCGKSTLLRCINRMNDLVDNCHIDGEILLHGQNIYDKKIDVAALRRNVGMVFQRPNPFPKSIYENVVYGLRLQGINNRRELDEAAERSLRGAAIWDEVKDRLHDNAFGLSGGQQQRLVIARAIAIEPEVLLLDEPTSALDPISTLTIEELITELKTKYTVVIVTHNMQQAARVSDQTAFMYMGELVEYADTNTIFTTPKKRKTEDYITGRYG
|
Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system.
|
Q0HH38
|
Q9SHC8
|
VAP12_ARATH
|
Vesicle-associated protein 1-2, N-terminally processed
|
Arabidopsis
|
MSNELLTIDPVDLQFPFELKKQISCSLYLGNKTDNYVAFKVKTTNPKKYCVRPNTGVVHPRSSSEVLVTMQAQKEAPADLQCKDKFLLQCVVASPGATPKDVTHEMFSKEAGHRVEETKLRVVYVAPPRPPSPVREGSEEGSSPRASVSDNGNASDFTAAPRFSADRVDAQDNSSEARALVTKLTEEKNSAVQLNNRLQQELDQLRRESKRSKSGGIPFMYVLLVGLIGLILGYIMKRT
|
Vesicle-associated protein that binds the oxysterol-binding protein ORP3A and allows its targeting to the ER.
|
Q9SHC8
|
Q68VY3
|
KGUA_RICTY
|
GMP kinase
|
typhus group
|
MQFKHKGLIIILSSPSGTGKSSLAKELLKIDNNLRLSISVTTRKPRLGEVDGINYYFKTDLEFKTLVKQNKFLEYAKIYNDYYGTPKEYVKMLLKQGLDVLFDIDWQGVRSIKKNTNNVVTIFVLPPSLEILEQRLRNRATDNEETIKLRMQSAQHEISYANEYDYVVINDDFGQTLKKIHEIIVAERAKNFSYHAH
|
Essential for recycling GMP and indirectly, cGMP.
|
Q68VY3
|
O84172
|
TRPB_CHLTR
|
Tryptophan synthase beta chain
|
Chlamydia
|
MFKHKHPFGGAFLPEELLAPIQNLKAEWEILKTQQSFLSELDCILKNYAGRQTPLTEVKNFARAIDGPRVFLKREDLLHTGAHKLNNALGQCLLAKYLGKTRVVAETGAGQHGVATATACAYLGLDCVVYMGAKDVERQKPNVEKMRFLGAEVVSVTKGSCGLKDAVNQALQDWATTHSFTHYCLGSALGPLPYPDIVRFFQSVISAEVKEQIHAVAGRDPDILIACIGGGSNAIGFFHHFIPNPKVQLIGVEGGGLGISSGKHAARFATGRPGVFHGFYSYLLQDDDGQVLQTHSISAGLDYPSVGPDHAEMHESGRAFYTLATDEEALRAFFLLTRNEGIIPALESSHALAHLVSIAPSLPKEQIVIVNLSGRGDKDLPQIIRRNRGIYE
|
The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
|
O84172
|
O34691
|
NAIP_BACSU
|
Putative niacin/nicotinamide transporter NaiP
|
Bacillus
|
MGKQQPISQRKLLGVAGLGWLFDAMDVGILSFIIAALHVEWNLSPEEMKWIGSVNSIGMAAGAFLFGLLADRIGRKKVFIITLLCFSIGSGISAFVTSLSAFLILRFVIGMGLGGELPVASTLVSEAVVPEKRGRVIVLLESFWAVGWLAAALISYFVIPSFGWQAALLLTALTAFYALYLRTSLPDSPKYESLSAKKRSMWENVKSVWARQYIRPTVMLSIVWFCVVFSYYGMFLWLPSVMLLKGFSMIQSFEYVLLMTLAQLPGYFSAAWLIEKAGRKWILVVYLIGTAGSAYFFGTADSLSLLLTAGVLLSFFNLGAWGVLYAYTPEQYPTAIRATGSGTTAAFGRIGGIFGPLLVGTLAARHISFSVIFSIFCIAILLAVACILIMGKETKQTELE
|
Probably involved in the uptake of amidated and deamidated forms of niacin. Increases the growth rate of E.coli that is unable to make niacin de novo; confers increased sensitivity to the toxic niacin analog 6-amino-nicotinamide to wild-type E.coli. There is probably another mechanism for niacin uptake.
|
O34691
|
A8A7B3
|
ACEK_ECOHS
|
Isocitrate dehydrogenase kinase/phosphatase
|
Escherichia
|
MPRGLELLIAQTILQGFDAQYGRFLEVTSGAQQRFEQADWHAVQQAMKNRIHLYDHHVGLVVEQLRCITNGQSTDAAFLLRVKEHYTRLLPDYPRFEIAESFFNSVYCRLFDHRSLTPERLFIFSSQPERRFRTIPRPLAKDFHPDHGWESLLMRVISDLPLRLRWQNKSRDIHYIIRHLTETLGTDNLAESHLQVANELFYRNKAAWLVGKLITPSGTLPFLLPIHQTDDGELFIDTCLTTTAEASIVFGFARSYFMVYAPLPAALVEWLREILPGKTTAELYMAIGCQKHAKTESYREYLVYLQGCNEQFIEAPGIRGMVMLVFTLPGFDRVFKVIKDKFAPQKEMSAAHVRACYQLVKEHDRVGRMADTQEFENFVLEKRHISPALMELLLQEAAEKITDLGEQIVIRHLYIERRMVPLNIWLEQVEGQQLRDAIEEYGNAIRQLAAANIFPGDMLFKNFGVTRHGRVVFYDYDEICYMTEVNFRDIPPPRYPEDELASEPWYSVSPGDVFPEEFRHWLCADPRIGPLFEEMHADLFRADYWRALQNRIREGHVEDVYAYRRRQRFSVRYGEMLF
|
Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation.
|
A8A7B3
|
Q8R092
|
CA043_MOUSE
|
Protein C1orf43 homolog
|
Mus
|
MASSSNWLSGVNVVLVMAYGSLVFVLLFIFVKRQIMRFAMKSRRGPHVPVGHNAPKDLKEEIDIRLSRVQDIKYEPQLLADDDTRLLQLETQGNQSCYNYLYRMKALDAIRASEIPFHAEGRHPCSLMGKNFRSYLLDLRNTSTPFKGVGKALIDTLLDGYETARYGTGVFGQSEYLRYQEALSELATVVKARIGSSQRQHQSAAKDLTQSPEMSPTTIQVTYLPSSQKSKRPKHFLELKSFKDNYNTLESTL
|
General regulator of phagocytosis. Required to uptake Gram negative bacterium by macrophages.
|
Q8R092
|
B8EE63
|
CYSC_SHEB2
|
Adenosine-5'-phosphosulfate kinase
|
Shewanella
|
MTNIVWHQHPVDQAARAEQKGQNPVLLWFTGLSGAGKSTLAGALERALFEAGFHTYLLDGDNVRHGLCKDLGFTVEDRDENLRRVGEVAKLMVDAGLVVLSAFISPTREERDSIRARFPASQFIEVHVSTPLSVCEQRDPKGLYVKARSGEISNFTGISSPYEAPLAAELTIDTSKGDLATQVRALIDYLTAINVINADKAKALA
|
Catalyzes the synthesis of activated sulfate.
|
B8EE63
|
Q0G9V9
|
NDHJ_DAUCA
|
NADH-plastoquinone oxidoreductase subunit J
|
Daucus sect. Daucus
|
MQGRLSAWLVKHGLIHRSLGFDYQGIETLQIKPEDWHSIAVILYIYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGVDQPEEVCIKVFSPRKNPRIPSVFWVWKGVDFQERESFDMLGISYDNHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAH
|
NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
|
Q0G9V9
|
Q9X5X3
|
ATCU_SINMW
|
Copper-transporting P-type ATPase
|
Sinorhizobium
|
MTALKQTEKSTSLPMSFDFDIEGMTCASCVRRVEKAIAAVPGVASANVNLATERATVQFNGVPETTSVLRAVEKAGYAPRIVTEEIQIEGMTCASCVSRVEKALKAVPGVADASVNLATEKATVRLVSGSAEISALAAAVKGAGYGIRKATPAEAMKEDVDHRTAELRSLKSAVTISSLMTLPLFLLEMGSHFIPGVHDFIMGTIGMRNNLYLQFALATLVLFGPGLRFFRKGVPNLLRWTPDMNSLVVLGTTAAWGYSVVTTFVPAILPSGTANVYYEAAAVIVTLILVGRYLESRAKGRTSQAIKRLVGLQPKTAFVLHSGEFVETEITEVVTGDVIRIRPGEKIPVDGTVTDGSSYVDESMITGEPVPVQKATDSAVIGGTINKTGSITFKATKVGSDTLLAQIIRLVEAAQGSKLPIQALVDRVTAWFVPVVILAALLTFAAWYVLGPSPALSFALVNAVAVLIIACPCAMGLATPTSIMVGTGRAAELGILFRKGEALQSLRDADVVAVDKTGTLTKGRPELTDLVAAEGFEPDEVLCLVASLETLSEHPIAEAIVSAAKSRGIATVAVSAFEATPGFGVSGTVSGRRVLVGADRALVKNGIDITGFADEAERLGSGGKSPLYAAIDGRLAAIVAVSDPVKESTPQAIKSLHALGLKVAMVTGDNRRTAEAIAKKLGIDEVVAEVLPEGKVDAVRKLRQGGRSVAFIGDGINDAPALAEADVGIAVGTGTDIAIESADVVLMSGDLNGVAKALALSKATIRNIKQNLFWAFVYNISLVPVAAGVLYPVNGTLLSPIFAAAAMAMSSVFVLGNALRLKSFDPA
|
Involved in copper efflux.
|
Q9X5X3
|
Q3BNL9
|
DTD_XANC5
|
Gly-tRNA(Ala) deacylase
|
Xanthomonas
|
MLALIQRVTRAAVTVDDQIVGQIGPGLLALIGVEPGDSDAQIRRLAERLLSYRVFGDDAGKMNRSLTDTGGGLLLVSQFTLAADTSSGNRPGFSTAAPPLEAEPAFNQLVAICREKHRGGVEAGRFGAHMVVDLVNDGPVTFLLRP
|
An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA-based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo and helps enforce protein L-homochirality.
|
Q3BNL9
|
Q0UWF6
|
PXR1_PHANO
|
PinX1-related protein 1
|
Parastagonospora
|
MGLAAPKNRSKISNDPQNTTWANNTSRFGHRILTSQGWQPGDSLGASDAAHAAHYTVASQSHIRVLLKDDNLGLGAKRGSERAENFGLAGLESILGRLNGKEAEVKKEEERREEIEKRAFVYRKYGMMNFVSGGFLVGDKIKSRDEVKTETQAKVEVKSEPESDGAKEDDRKKKRKRKDRDEAGVEGEEEPKLKRKKKSMDLRDQAKKDIAAESSKDKKGKKSKKDKKAVTSDPEPTSSGVASPASDPEPLTDKARRKAEKKARKEEKRLKKALKKAAKEAAKPMGDVEDLSSESEDESTPSASRPATGTSTPTVSAAGLTFNPRGMHSVRQKWIRSKKSATMDAQAMREIFMIKTPS
|
Involved in rRNA-processing at A0, A1 and A2 sites and regulates negatively telomerase.
|
Q0UWF6
|
Q0HJT7
|
MNMA_SHESM
|
tRNA-specific 2-thiouridylase MnmA
|
Shewanella
|
MTSIEPTHTGKKVIVGMSGGVDSSVSAYLLMQQGYQVEGLFMKNWEEDDNDEYCAAAEDLKDAQAVCDKLGIKLHTVNFAAEYWDNVFEYFLAEYKAGRTPNPDIMCNKEIKFKAFLDFADDILDADYIAMGHYVRRRDNADGTTQMLRGVDNNKDQSYFLYTLSHEQVARSLFPVGELEKHEVREIAKKMGLITHDKKDSTGICFIGERKFTEFLGNYLPAQPGNIETAEGEVIGKHQGLMYHTLGQRKGLGIGGMKNSNDDPWYVVDKDLKRNVLVVGQGGHHPRLMSNGMLVNQLHWVDRKGPAEGSQIVVKTRYRQQDIPCTLTYLDDNTLKVVFDEPVAAVTPGQSAVFYDGEVCLGGGIIDQLIRG
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
Q0HJT7
|
B1P1G5
|
JZT40_CHIGU
|
Jingzhaotoxin-40
|
Chilobrachys
|
MKVSVLITLAVLGVMFLLTSAEERGSDQMDSPAWLKSMERIFQSEERECRWLFGGCEKDSDCCEHLGCRRTKPSWCGWDFTFGK
|
Probable ion channel inhibitor.
|
B1P1G5
|
C3MAY2
|
RL23_SINFN
|
50S ribosomal protein L23
|
Sinorhizobium
|
MTDLRHYDVIVSPSITEKSTLVSEQNQVVFNVAKGASKPEIKAAVEALFGVKVTAVNTLVRKGKLKRFRGFAGKQKDVKKAIITLAEGQSIDVSTGL
|
One of the early assembly proteins it binds 23S rRNA. One of the proteins that surrounds the polypeptide exit tunnel on the outside of the ribosome. Forms the main docking site for trigger factor binding to the ribosome.
|
C3MAY2
|
Q58597
|
SYT_METJA
|
Threonyl-tRNA synthetase
|
Methanocaldococcus
|
MKMLLIHSDYLEFEAKEKTKIAEETENLKGKLDECLACFIAVEREDENNPEGTAIGAVEEIEKVANQLKVNNIVVYPYAHLSSDLSSPETAVKVLKDIESILKERGYNVLRAPFGWYKAFKISCKGHPLSELSRKIVAKEEKKEEGEESKFYLLNPETEEIIELNENNINIIKDEELLALAKHELGIREHKEHDEPPHVKFIKEKDICSYEEASDPGHFRWYPKGKLMRDLLADYVYNLVVNMGAMPVETPIMYDLGNPAIREHADKFGERQYRFRQGNKELMLRFAACFGQFMMKKDMYLLPRYLPLKLYELSTYSFRYEQRGELVGLKRLRCFTMPDMHTVCLNLEQAMEEFEKQFWECLKTGDDLNLSYSVIFRFTKDFFDEHRDWFFKIAKEYKNKYGKDVILEILPKRKHYWVGKVDIAVIDSLGRPIENPTVQIDVESAKRFDIKVHTNEGEIYPIILHCSPTGSIERVLCGLLEKAAIEAEKGNAPMLPVWLSPIQVRVIPVAERHYDYALKVAEKLRENNIRADFDDREESVSKKIRNAGKEWVPYVVVIGDEEMESDKLTVTIREKSTLKKPYKEKMTLDELIERIKKETANYPYRPLPLPIRCSLQPKFH
|
Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) . Also activates L-serine, but does not detectably transfer it to tRNA(Thr) . Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain . Has no activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-tRNA(Thr) . Deacylates correctly charged glycyl-tRNA(Gly), but not glycyl-tRNA(Gly)(2'-dA76) (the terminal 2'-OH of tRNA adenine 76 has been dehydroxylated) nor the 2'-fluoro tRNA derivative, strongly suggesting the editing function is tRNA catalyzed .
|
Q58597
|
A1TQ97
|
KDSB_ACIAC
|
CMP-2-keto-3-deoxyoctulosonic acid synthase
|
Acidovorax
|
MSGGAASAGFTVLIPARLASTRLPDKPLADIGGIPMVVRVAQQAARSRAARVVVAADHPRILEACAAHGVQAVATRADHPSGSDRLAEACVQLGLADDDVVVNVQGDEPLIAPALIDAVAALLPARPEADMGTAAHAIHAREDFANPNVVKVVLDARGLAHYFSRAPIPHARGHADTAWWQGGQAGVPAGCAPLRHIGIYSYRAAFVRAFAALPPAPTEALEALEQLRALWHGHRIAVHVADAAPGPGVDTPEDLERVRSLLG
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
|
A1TQ97
|
A1A900
|
GAL1_ECOK1
|
Galactose kinase
|
Escherichia
|
MSLKEKTQSLFANAFGYPATHTIQAPGRVNLIGEHTDYNDGFVLPCAIDYQTVISCAPRDDRKVRVMAADYENQLDEFSLDAPIVAHENYQWANYVRGVVKHLQLRNNSFGGVDMVISGNVPQGAGLSSSASLEVAVGTVLQQLYHLPLDGAQIALNGQEAENQFVGCNCGIMDQLISALGKKDHALLIDCRSLGTKAVSMPKGVAVVIINSNFKRTLVGSEYNTRREQCETGARFFQQPALRDVTIEEFNAVAHELDPIVAKRVRHILTENARTVEAASALEQGDLKRMGELMAESHASMRDDFEITVPQIDTLVEIVKAVIGDKGGVRMTGGGFGGCIVALFPEELVPAVQQAVAEQYEAKTGIKETFYVCKPSQGAGQC
|
Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P).
|
A1A900
|
Q730U2
|
TCYP_BACC1
|
Transporter of cystine TcyP
|
Bacillus cereus group
|
MNTLLVGINVAVMLILVGVLYYMQRKHVSFNKRVFTALGVGIIFGLILQFIYEPTSKVIIESNTWFGLIGNGYVKLLQMIVMPLILVSIISAFTKLQLTKNLGKISGLIIGILILTTGIAAAVGIAASAGFDVSATGLQQGDAESARLKLVEERFTSIEKTTIPDKLLELLPTNPFLDLTGARPTSTISVVIFAAFIGIAFIGVKRKYPEQAELFKKMLDAVYAIVMRMVTLILRLTPYGVLALMAKTVAGSDINAILKLGNFVLASYVALIVMFVIHLLLIALSGLNPIQYLKKVFPVLTFAFTSRSSAGAMPLNIEAQKEKLGISEGIANFAASFGVSIGQNGCAGIYPAMLAMMVAPTVGIDPLQPQFILTLIAVVAISSFGVAGVGGGATFAALIVLSTMNLPIGIVALVISVEPLIDMGRTALNVSGSMTAGLISSKWLGELDQDTYNQDDTKTGEIAS
|
Mediates uptake of L-cystine, the oxidized form of L-cysteine.
|
Q730U2
|
Q9SXW9
|
PLAS_PHYPA
|
Plastocyanin, chloroplastic
|
Physcomitrium
|
MASVAAAAVSVPSFSGLKAETKAAPARLSSTSVVRMAPVVRASASSDALKTVGKALLAASSSLLLVASANAATVKMGGDDGALGFYPKDISVAAGESVTFVNNKGFPHNVVFDEDAVPAGVKTEDINHEDYLNGPNESFSITFKTPGTYEFYCEPHQGAGMKGVVTVS
|
Participates in electron transfer between P700 and the cytochrome b6-f complex in photosystem I.
|
Q9SXW9
|
O75601
|
CASPD_BOVIN
|
Caspase-13 subunit 2
|
Bos
|
MAEDKHNKNPLKMLESLGKELISGLLDDFVEKNVLKLEEEEKKKIYDAKLQDKARVLVDSIRQKNQEAGQVFVQTFLNIDKNSTSIKAPEETVAGPDESVGSAATLKLCPHEEFLKLCKERAGEIYPIKERKDRTRLALIICNTEFDHMPPRNGAALDILGMKQLLEGLGYTVEVEEKLTARDMESVLWKFAAREEHKSSDSTFLVFMSHGILDGICGTMHSEEEPDVLPYDTIFRTFNNRNCLSLKDKPKVIIVQACRGANRGELWVSDSPPALADSFSQSSENLEEDAVYKTHVEKDFIAFCSSTPHNVSWRDIKKGSLFITRLITCFQKYAWCCHLEEVFRKVQQSFEKPNVKAQMPTVERLSMTRYFYLFPGN
|
Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival.
|
O75601
|
Q97GF7
|
RECX_CLOAB
|
Regulatory protein RecX
|
Clostridium
|
MEENTITKIEAQKKKKDRVNVYIDNEYSFSCNTELIYIHGLKKGKVVDLDYLQDIIEEDNYLYAKSRALSFIEKTFKTEKEIRVKLREKEFNEKIIERVIEFLRKYDFVDDSRYAELYIKERINKQGKVKIKYGLIKKGINDSIIDEKLSKYSANNENYIEAMREVALKKFNNIAKRETDKLKIKRKLSSYLLGRGYSWSEIGEVLKEIFSENN
|
Modulates RecA activity.
|
Q97GF7
|
Q5FQB9
|
TOLB_GLUOX
|
Tol-Pal system protein TolB
|
Gluconobacter
|
MSFIPNTEAEALSALFSRRSVLGATAAGGLLATPLAAFAQSGAASGPGEAEITVDQARQEPIPIVVPNFGAGLGEQISGVITSDLNGTGLFKVMSGSVPPGSTPDFSALKAQGARAAVAGQAVGAGSVRVEMRLWDVLSGQQLQGTAYTASNSNWRRIAHIIADVIYERMLGEKGYFDTRIAYIARTGPRHHQITRLALMDQDGANERMLTGGEWLTLTPRFNPVRDQIAFMSYANNRPRVYLFDLASGRQQILGEFAGISFAPRFSPTGGSVVLSATRGGGSDIFVVDLASRAKRQITNSNGAIDTSPCFSPDGSQIVFNSDRGGSPQLYIMSASGGAAKRISYGSGQYGSPVWSPRGDLIAFTRIGSGGFSLGVMNPDGTGERILTQGFTVDGATFCPNGRVLAFCRQSASGAGGAGFASGIGTIDITGFNERPIRISTGASDPAWSPRNG
|
Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity.
|
Q5FQB9
|
B1ZKE5
|
NDK_METPB
|
Nucleoside-2-P kinase
|
Methylorubrum
|
MANERTFSILKPDATRRNITGAVNAVIEAAGLRIVGQRRIRMTRAQAEKFYEVHKERPFFGELVEFMTSGPVVVQVLEGENAVAKYREVMGATNPAQAADGTIRKQFAESVGENTVHGSDSADNAKIEIAQFFTDADIAA
|
Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
|
B1ZKE5
|
A4XBL2
|
THIE_SALTO
|
Thiamine-phosphate pyrophosphorylase
|
Salinispora
|
MSSLGRLHLITDARAGRNPLTVVQAALSVARTELVVQVRVADDATDRQAYDLARRVIALCARYDATCLVNDRLHVALAVGAAGGHVGADDLPVGAARAVLGSAAVLGVTARDADTAVEAVAAGASYLGVGPVHPTTSKEGLPPAIGVAGVGVVAAAVSVPVIAIGAVTAADVPVLRAAGAYGVAVIGALSHAADPAGATAALLEALTW
|
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).
|
A4XBL2
|
P10322
|
NO25_MEDSA
|
Nodulin-25
|
Medicago
|
MVYSNTYMLLGLGVFVLLSSHVLAYNMRADPSIHDSTLDDQKSNDFVKTASIAECPPGPDTYLELSDSTLDDQKSMDYVKDASTVDHNCPPGPHTYLELSAWLQEEQNSIDKVKKVLRTDEAPDNQKGLEYKDARHNDGPIEISTRTEKDNFIPSDGPIEISTRTENENFIPSDEPIEISTGTEKENFISSDEPSEISSGAEKENFIPSVSQVDWRTFHAKYPWIKKDGPNTVTGSRKLLNDIAIK
|
Involved in the development and function of nodules. It might participate in the biological process of symbiotic nitrogen fixation.
|
P10322
|
O94339
|
MUG96_SCHPO
|
Meiotically up-regulated gene 96 protein
|
Schizosaccharomyces
|
MVIFSSYFSKQMNRFSTPFVFFFKKLNNTLKKSLQFIMRFHSYHPMFICLLRDSSRNENRKKKVSIGLRTIMRAFSFLMQVATCLIRYSLILTCLVAILLSVLWRIQFAALRMHDLIEEELKMFVLQHNCTLADLWSGKCPSSEDE
|
Has a role in meiosis.
|
O94339
|
B8DHE9
|
THII_LISMH
|
tRNA 4-thiouridine synthase
|
Listeria
|
MEFDRMLIRYGELSTKGKNRKQFVTKLAQNVKRAMTDLPEVRIHGERDRMYIILNGADYQLAEERLKPIFGIQSFSPAVRVNLDLEEVKAAALALVQDAHEENGTFKVAARRSHREFPLDSNEINQEIGAHVLQNIEDLTVNVKNPDVKLTIDVRKEGVFLSCRTILGAAGLPVGSSGRAMLMLSGGIDSPVAGYLAQKRGVEIEAVHFHSPPYTSEQAKQKAIDLAAKLAKYSGQVQMHIVPFTEIQEVIKQQIPESVIMTVTRRMMLRITDELRRKRNGLAIVNGESLGQVASQTLESMLAINAVTATPIIRPVVSMDKNEIIQIAQKIDTYNLSVQPFEDCCTIFTPPSPKTKPKLDKIEHYESFTDFDALIAKALDNIETISVNVAETVQVKDEFADLF
|
Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
|
B8DHE9
|
Q3ZXL7
|
HISX_DEHMC
|
Histidinol dehydrogenase
|
Dehalococcoides
|
MKIIRGFAQAEKRLSRRDKAGFFLDETERTELARRLGVDPEKAVNGIIADVRKQGDEAVLGYTLKFDRANLSKLEVGQPEIQQAASEIPAELFEALQLAASQIRAYHRFQKEAVWKTAEIMQGKQLIRPLERVGLYVPGGKAFYPSTVLMTAIPAREAGVKEIILVTPPGANGKIPAPTLAAAQIAGVDRIFACGGAQAVAALAFGTKSIPKVDKICGPGNIFVTLAKKAVFGVVDIDGLQGPSEVLIVADQYANAEYCASDILAQAEHDALASSILITTSEDLANRVNDIVESKADTCSRRDIIKQSLRDNGLIAVVDNINEAIKLANMYAAEHLCLLVKDSEKYLTQINHAGCIFYGEKASVVMGDYVAGPSHALPTSGTARFSSPLNILDFVKYIDIVKVDKQDIAKLGQAAATIAKAEGLECHAEAVLKRLE
|
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
|
Q3ZXL7
|
B3GZE5
|
RL21_ACTP7
|
50S ribosomal protein L21
|
Actinobacillus
|
MYAVFQSGGKQHRVSEGQVVRLEKLEIATGEKFEFDSVLMVVNGEDVKIGAPVVAGAKVVAEVVAQGRGDKVKIVKFRRRKHSRKQQGHRQWFTEVKITGIQA
|
This protein binds to 23S rRNA in the presence of protein L20.
|
B3GZE5
|
Q5R5Y3
|
B3GT2_PONAB
|
UDP-galactose:2-acetamido-2-deoxy-D-glucose 3beta-galactosyltransferase 2
|
Pongo
|
MLQWRRRHCCFAKMTWNAKRSLFRTHLIGVLSLVFLFAMFLFFNHHDWLPGRAGFKENPVTYTFRGFRSTKSETNHSSLRNIWKETVPQTLRPQTATNSNNTDLSPQGVTGLENTLSANGSIYNEKGTGYPNSYHFKYIINEPEKCQEKSPFLILLIAAEPGQIEARRAIRQTWGNESLAPGIQITRIFLLGLSIKLNGYLQRAILEESRQYHDIIQQEYLDTYYNLTIKTLMGMNWVATYCPHIPYVMKTDSDMFVNTEYLINKLLKPDLPPRHNYFTGYLMRGYAPNRNKDSKWYMPPDLYPSERYPVFCSGTGYVFSGDLAEKIFKVSLGIRRLHLEDVYVGICLAKLRIDPVPPPNEFVFNHWRVSYSSCKYSHLITSHQFQPSELIKYWNHLQQNKHNACANAAKEKAGRYRHRKLH
|
Beta-1,3-galactosyltransferase that transfers galactose from UDP-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Can also utilize substrates with a terminal galactose residue, albeit with lower efficiency. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.
|
Q5R5Y3
|
Q7TS73
|
RFLA_MOUSE
|
Regulator of filamin protein A
|
Mus
|
MVGHLHLQAMGDTREQSRDGLLDSPDSGLPPSPSPSPPFYALSPGTLDTRTTTEAPAAPSLFQTPPALEMRSRLLPVFFGESIEVDPEPAHEIRCNSEITYASERYFRDKIFYAPVPTVTAYSETIVAAPNCTWRSYRSQLTLEPRPRALRFGSTAIIFPKLARSSFRTTLHCSLGQPRHWYSSSLQLRRCGDPTPGPSCPDVL
|
Involved in the regulation of the perinuclear actin network and nuclear shape through interaction with filamins. Plays an essential role in the formation of cartilaginous skeletal elements.
|
Q7TS73
|
C4L2E7
|
OAT_EXISA
|
Ornithine--oxo-acid aminotransferase
|
unclassified Exiguobacterium
|
MSKTHDVIELTEKFGAHNYHPLPIVISEAKGIWVTDPEGNRYMDMLSAYSAVNQGHCHPKIIQALKDQADKITLTSRAFYNDQLGRFYDKVVTLTKKQMVLPMNTGAEAVETAVKTARRWAYDVKGIPGQAEIIVCSGNFHGRTMAAVSMSTEAEYQRGFGPLLPGFKVVPYGDIDAFEAAITENTAAFIVEPIQGEAGIIIPPAGYLKRASELCKEHNVLFVADEIQSGLGRSGKWFAIEWEDVTPDMYILGKALGGGVFPISCVAADQEILSVFNPGSHGSTFGGNPLASAVSVAALEVLEEENLPERSLELGTYFMDRLKSIDNPMIRDVRGRGLFIGIELTESARPYCEALKERGLLCKETHETVIRLAPPLVITKEELDQAFEAIEAVLAPAAIS
|
Catalyzes the interconversion of ornithine to glutamate semialdehyde.
|
C4L2E7
|
Q6BIS2
|
YPT35_DEBHA
|
PX domain-containing protein YPT35
|
Debaryomyces
|
MTASNRRGSTHRNSVTQLNKVLPVPIQLEDETSSGHFNSTSHITDVLVGDYHVIQGEGGSSYVVWSIRIIVDDSVYSSMVIYKRYSDIQRFREALLEHYPNTEIPPLPPKDNFSFQRLSMSDYWLENRRKGLQWFMTNVMLNPKHQHSPVITHFILN
|
Recruits the lipid transfer protein VPS13 to endosomal and vacuolar membranes.
|
Q6BIS2
|
Q3ZJ62
|
PSBI_TUPAK
|
PSII 4.8 kDa protein
|
Tupiella
|
MLTLKIFVYTVVTFFVSLFIFGFLSNDPGRNPNQR
|
One of the components of the core complex of photosystem II (PSII), required for its stability and/or assembly. PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
|
Q3ZJ62
|
Q04837
|
SSBP_HUMAN
|
PWP1-interacting protein 17
|
Homo
|
MFRRPVLQVLRQFVRHESETTTSLVLERSLNRVHLLGRVGQDPVLRQVEGKNPVTIFSLATNEMWRSGDSEVYQLGDVSQKTTWHRISVFRPGLRDVAYQYVKKGSRIYLEGKIDYGEYMDKNNVRRQATTIIADNIIFLSDQTKEKE
|
Binds preferentially and cooperatively to pyrimidine rich single-stranded DNA (ss-DNA) . In vitro, required to maintain the copy number of mitochondrial DNA (mtDNA) and plays a crucial role during mtDNA replication by stimulating the activity of the replisome components POLG and TWNK at the replication fork . Promotes the activity of the gamma complex polymerase POLG, largely by organizing the template DNA and eliminating secondary structures to favor ss-DNA conformations that facilitate POLG activity . In addition it is able to promote the 5'-3' unwinding activity of the mtDNA helicase TWNK . May also function in mtDNA repair .
|
Q04837
|
P56990
|
GLYA_NEIMB
|
Serine hydroxymethyltransferase
|
Neisseria
|
MFSKSVTLAQYDPDLAAAIAQEDQRQQDHVELIASENYVSCAVMDAQGSQLTNKYAEGYPGKRYYGGCEYVDIVEQLAIDRVKELFGAAYANVQPHSGSQANQAVYASVLKPGDTILGMSLAHGGHLTHGASVNISGKLYNAVTYGLDENEVLDYAEVERLALEHKPKMIVAGASAYALQIDWAKFREIADKVGAYLFVDMAHYAGLVAGGEYPNPVPFCDFVTTTTHKTLRGPRGGVILCRDNTHEKALNSSIFPSLQGGPLMHVIAAKAVAFKEALQPEFKQYAKQVKINAAAMAEELVKRGLRIVSGRTESHVFLVDLQPMKITGKAAEAALGKAHITVNKNAIPNDPEKPFVTSGIRIGSAAMTTRGFNEADARVLANLVADVLSNPEDEANLAKVRKQVTALCNKYPVYGA
|
Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
|
P56990
|
B4JXP7
|
MOCOS_DROGR
|
Protein maroon-like
|
Hawaiian Drosophila
|
MGDYTAEFTPDEQALIDAEFARLSDSTYLDHAGTTLYAHNQVSDAAQQLQRDVICNPHTCRVTGDYVDQVRYKILEFFNTNADEYHVVFTANASAALRLVADHFDFGTNGNFHYCQENHTSVLGMRQLVSANRIYMLTKDQILLNNGTPAGATAAAATAHSDNSLVVFSAQCNFSGYKMPLTVIEKIQQDGLREPGKCIDCKLQSDPGQSNYYVCLDAASYAASSPLDLRRHRPDYVCLSFYKIFGYPTGVGALLVSKRGAELLKKRFYGGGTVNFAYPHTMEHQLRSTFHERFEDGTLPFLSIVELLQGFQTLQRLVPGRSMERISRHVHSLARYCEQQLLQMQYPNGAPLVTLYNHAGYEDRMQQGGIVAFNVRTAAGDYVGFGEIASVAALHRILLRTGCFCNVGACQHFMNLNGDAMDAIYKLAGRICGDYYDLLDGRPTGAVRVSFGYMTRLQDVDRLLQMLRDSYLSVKWHQRLDFIEQRVQQLPKLLQQRAQQLRPQLLQLAIYPVKSCAALKMPASALTDQGLQYDREWMIVDLNGMALTQKRCTDLCLIQPRIVADQLQLHFNGDGSTTFVSVPLSLTDQATNSARCQSKVCRQSVEGYDCGDEVANWLCQQLGLDGLRLLRQSAQRRAPGDRQQLSLVNQAQFLLVNRASVRSLGFEEPLDETVDRFRSNIVIDTGVPFEELEFGQLRIGEVLFQVEGPCQRCDMICINQRTGQRSPDTLTTIARIQSGKMRFGIYISRLPNENRMQPQLACGDPITVLR
|
Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
|
B4JXP7
|
Q5M1E2
|
NRDR_STRT1
|
Transcriptional repressor NrdR
|
Streptococcus
|
MRCPKCQHNKSNVIDSRQAEDGNTIRRRRECDACHARFTTFERVEEVPLLVVKKDGTREQFSRDKIFNGILMSAQKRPVSSEDIENAITRIEQNIRRNHDGEVDSEVIGNLVMKELADLDEITYVRFASVYRSFKDVDEIEELLQEITKTVRAKKESKK
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
Q5M1E2
|
Q92RM4
|
RNH2_RHIME
|
Ribonuclease HII
|
Sinorhizobium
|
MSRRKQPDSPLFPLQAPVPDFTFERAAHRDGFWPVAGADEAGRGPLAGPVVAAAVILDPDAIPAGLNDSKLLTAEQREALFEEILATSTVSIASSSSARIDTTDILKASLDAMRRAVHGLELAARIVLVDGRDVPPGLSCHAKAIVKGDSRSVSIAAASIVAKVTRDRMMARADATFPLYGFAHHAGYATVKHRTAIESHGPCSLHRMSFRPFRQV
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q92RM4
|
Q8D252
|
RPIA_WIGBR
|
Phosphoriboisomerase A
|
Wigglesworthia
|
MIEEKLKKQAAWAAIKYIKPGDIVGVGSGSTAEYFIDALGSIKNLIKGTVSSSRISSSKLKDLNIPLFDLNEVSLLNIYVDGADEINQKKHMIKGKGAALTREKIIASAAKKFICIVDSSKFVHVLGRAPLPIEVIPMARTLVSKKIIDIGGSPKYRKGIITENGNVLLDVHNLIILDSLFLEEKINNIPGVVSVGLFAHRAADIAIISGKNGIKIID
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q8D252
|
O95935
|
TBX18_HUMAN
|
T-box transcription factor TBX18
|
Homo
|
MAEKRRGSPCSMLSLKAHAFSVEALIGAEKQQQLQKKRRKLGAEEAAGAVDDGGCSRGGGAGEKGSSEGDEGAALPPPAGATSGPARSGADLERGAAGGCEDGFQQGASPLASPGGSPKGSPARSLARPGTPLPSPQAPRVDLQGAELWKRFHEIGTEMIITKAGRRMFPAMRVKISGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKDCGDDLSPIKPVPSGEGVKAFSFPETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRMGLEALVESYAFWRPSLRTLTFEDIPGIPKQGNASSSTLLQGTGNGVPATHPHLLSGSSCSSPAFHLGPNTSQLCSLAPADYSACARSGLTLNRYSTSLAETYNRLTNQAGETFAPPRTPSYVGVSSSTSVNMSMGGTDGDTFSCPQTSLSMQISGMSPQLQYIMPSPSSNAFATNQTHQGSYNTFRLHSPCALYGYNFSTSPKLAASPEKIVSSQGSFLGSSPSGTMTDRQMLPPVEGVHLLSSGGQQSFFDSRTLGSLTLSSSQVSAHMV
|
Acts as transcriptional repressor involved in developmental processes of a variety of tissues and organs, including the heart and coronary vessels, the ureter and the vertebral column. Required for embryonic development of the sino atrial node (SAN) head area.
|
O95935
|
P46904
|
NATB_BACSU
|
ABC-type Na(+) transporter
|
Bacillus
|
MLSHIYKKEMIDALRDRKTILLTILVPMIMMLGLVFFYESMLSDKGEQYTLAVGHSLPPALESKLNEIDEISVKTFAKPEEAVDEGKADAYLNVPKEFDSYVNSMTPFKVDVYGNSIDQGSSNAMQLVQSALDQYKNEIVQQRLTNKHIDQSVIQPFTIQQKEADEEKGTSAIMLSAILPMLILTSIVSGAMPIALDIMAGEKDRKSIEALLLTPVSRNKVLVGKWLAVSTFGVASGVFALVFLILSTVLFTENLKTAFQLGDHMWSVIGASALIIVLSALLISAMELFISIMSSSVKEAQSYMSLVVFLPVFPMFFIFSKAPNQFDLSYFLIPFLNLHALFKQLLFGMVDPATILSTSGTIAVLIAIFFLLARACFLKDKWVLPK
|
Part of an ABC transporter that catalyzes ATP-dependent electrogenic sodium extrusion.
|
P46904
|
B0KFT9
|
GMHA_PSEPG
|
Sedoheptulose 7-phosphate isomerase
|
Pseudomonas
|
MDMQSRIRRLFQASIDTKQQAMDILAPHIEQASLVMVNALLNEGKMLACGNGGSAGDAQHFSSELLNRFERERPSLPAIALTTDSSTLTSIANDYSYNEVFSKQIRALGQPGDVLLAISTSGNSANVIQAIQAAHDREMIVVALTGRDGGGMASLLLPEDVEIRVPSTVTARIQEVHLLAIHCLCDLIDSQLFGSEE
|
Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.
|
B0KFT9
|
Q5WM31
|
DNAA_ALKCK
|
Chromosomal replication initiator protein DnaA
|
Alkalihalobacillus
|
MENIDDLWNKVLEEMKKKVSKPSYETWLRATKANALQNNDTIIVTAPNEFARDWLEDHYSGLTSDIIEQLTGARLTPKFVIPQHNQEEEALPEQTPQTPPEKDVAGQSTLSQTMLNDKYTFNTFVIGSGNRFAHAASLAVAEAPARAYNPLFIYGGVGLGKTHLMHAIGHYVMEHNPNAKVVYLSSEKFTNEFINAIRDNKAVHFRNKYRNVDVLLIDDIQFIAGKIQTQEEFFHTFNALHEESKQIVISSDRPPKEIPTLEDRLRSRFEWGLITDITPPDLETRIAILRKKAKAENLDIPNEVMLYIANQIDTNIRELEGALIRVVAYSSLINQDMNADLAAEALKDIIPNAMPKTLTITDIQKLVGEHFQVKLEDFKAKKRTKSVAFPRQIAMYLSREMTDASLPKIGSEFGGRDHTTVIHAHEKISKLLATDQELQQKVQAITEQLRQ
|
Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
|
Q5WM31
|
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