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
|
|---|---|---|---|---|---|---|
Q75D88
|
SET1_ASHGO
|
SET domain-containing protein 1
|
Eremothecium
|
MSGYYNHVKHQGYSRYGQNSTVRNGQHDGLRYRNPSPAHNGTNEGEGLQGSRYENAGGVTHARRPPPVVKWGEAAFRAKYHYFDVEERKLLHLDEMKHWQNGRLPANGYVLVADAGSKGRPVMRERNPEEQAVDPRGARAAHTVRRVRSLLTALPRIPYDAHWVGPEPPKEVVVFPKQREQALSVQDPIIKNFFGTFGEVAHFESFNDPNNALPLNIYLVRYINVEGNPDSPYKAAYKAVKQFAKQDYLVSGARFAVRLNMNGFLQKTIDKFVTENLQRAAKLRHEQAKQQSTVQKVTNVSAVPSGVPPPKIPLGLERIVNNKPILRVSARFCALHGITSEDFKYGLKNYHWTRVINHYSGIYIIFDDIAEAEKCLQMESLRLTFFSRRRKIPVKIKFMLIEPSHQPPASQPLTDQDEVPKVYETEAELIEETLKHIINELKTTLYKDIRRRLLGPTIFDALNPGNYPDIVARRQKEEEAKKEKEKAMVEKTKKEAPSAAAFDIFNLYGTAYKKRDGTKGKKRHVAEGRPEESSGRRRIQSKGTAPMAHMLNYESLKVNGTASPIKEAESETCSSDEEDDDNFDVEMTDQSSIKKLKRESTATTPEQEPLQERVAGLSAERTKELLSYPEKYRPLAGDQPEPIYPEFLIEKYDDPLLSIVDLQRSVKDKEDMELLKKVIAYDREEVKDVINDIEFFAWRLHRDYKEHKENMQHQSKLSESTYKNLLNAHGGCFKQQGFRKMPDKLKSIYLPHRRKLNQPLNTVYHHGIEDFANTDNNKMDTDPPEDTFTPEQTSSRVNRALQRRFQQDIEAQKAAIGTESELLSLNQLTKRKKPVTFARSAIHNWGLYALEPISAKEMIIEYVGERIRQPVAEMREKRYLKSGIGSSYLFRVDESTVIDATKKGGIARFINHCCDPSCTAKIIKVGGMKRIVIYALRDIAANEELTYDYKFERETDDEERLPCLCGAPNCKGFLN
|
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
|
Q75D88
|
A4W9J6
|
ASTA_ENT38
|
AOST
|
Enterobacter
|
MMVIRPVERGDLAGLMQLAGKTGGGLTSLPADEKTLSSRIDRALQTWQGTLPKSEQGYVFVLEESDTGTVVGICAIEVAVGLNDPWYNYRVGTLVHASKELNVYNALPTLFLSNDHTGSSELCTLFLDPDWRKEGNGYLLSKSRFMFMAAFRDRFNEKVVAEMRGVIDETGYSPFWESLGERFFSMEFSRADYLCGTGQKAFIAELMPKHPIYTDFLSPQAQAVIGQVHPQTAPARAVLEKEGFRYHNYVDIFDGGPTLECDVDRVRAIRKSRLVTVAEGQPAPGEWPACLVANEQYDQFRAMLIHTNPTCERLVLTAAQLDVLKCNAGDTVRLVRLCPEEKTA
|
Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine.
|
A4W9J6
|
A7E5J5
|
EIF3L_SCLS1
|
Eukaryotic translation initiation factor 3 subunit L
|
Sclerotinia
|
MSAFQNGGIASRALDDDSDIEEEALANDYKEQVQYEGMEELEQVNSMSMAQQTDDIQSRLAAAAQPLDFSAPLEVKFASYDNYCSLFHFILNSDGPVDLEPPSYYWAWDVIDEFIYQFNSFCSYRNRVARQGTNEEEIQILREAPNTWGCYSVLNVLYSLIQRSQINEQLAAMRRNEEPMAVAGDYGSKSLYRMLGYFSIIGLLRVHCLLGDFSLALKTLDDIELNKKAMFARVMAAHFTTYYYVGFSYMMMRRYADAIRMFSHILIYVSRTKNFQKNAQYDSISKKNDQMYALIAICVAFHPTRLDDTIHTALREKYGDQLLKLQRGGPESLPIFEELFRSACPKFISPTPPDFDNPELNVDPLEHHLSIFMDEVKTNMWSPTVKSYLRLYTTMDLKKLAGFLEVEPEKLRGWLLVNKQRSRQIRWTDNGLLDGEVVNSNDLDYAMQGDLIHISEAKVGRKLVDWYLRNLARTY
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
A7E5J5
|
Q82DQ7
|
RL10_STRAW
|
50S ribosomal protein L10
|
Streptomyces
|
MARPDKAAAVAELADQFRSSNAAVLTEYRGLTVAQLKTLRRSLGEDAQYAVVKNTLTKIAANEAGINTLDDLFNGPTAVAFITGDPVVSAKGLRDFAKDNPNLVIKGGVLDGKALSADEIKKLADLESREVLLAKLAGAFKGKQSQAASLFQALPSKFVRTAEALRAKKAEQGGAE
|
Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors.
|
Q82DQ7
|
P12660
|
PCP2_MOUSE
|
Purkinje cell-specific protein L7
|
Mus
|
MAGSPDQEGFFNLLTHVQGDRMEEQRCSLQAGPGQNPESQGGPAPEMDNLMDMLVNTQGRRMDDQRVTVNSLPGFQPIGPKDGMQKRPGTLSPQPLLTPQDPAALSFRRNSSPQPQTQAP
|
May function as a cell-type specific modulator for G protein-mediated cell signaling.
|
P12660
|
Q8ZCH3
|
NANT_YERPE
|
Sialic acid/H(+) symporter
|
Yersinia
|
MSISVGPSREDKPLSGGAKPPRWYKQLTPAQWKAFVAAWIGYALDGFDFVLITLVLTDIKQEFGLTLIQATSLISAAFISRWFGGLVLGAMGDRYGRKLAMITSIVLFSFGTLACGLAPGYTTLFIARLIIGIGMAGEYGSSSTYVMESWPKNMRNKASGFLISGFSIGAVLAAQAYSYVVLAFGWRMLFYIGLLPIIFALWLRKNLPEAEDWEKAQSKQKKGKQVTDRNMVDILYRSHLSYLNIGLTIFAAVSLYLCFTGMVSTLLVVVLGILCAAIFIYFMVQTSGDRWPTGVMLMVVVFCAFLYSWPIQALLPTYLKMDLGYDPHTVGNILFFSGFGAAVGCCVGGFLGDWLGTRKAYVTSLLISQLLIIPLFAIQGSSILFLGGLLFLQQMLGQGIAGLLPKLLGGYFDTEQRAAGLGFTYNVGALGGALAPILGASIAQHLSLGTALGSLSFSLTFVVILLIGFDMPSRVQRWVRPSGLRMVDAIDGKPFSGAITAQHARVVTQK
|
Catalyzes the proton-dependent transport of sialic acid.
|
Q8ZCH3
|
A3PLD1
|
TYSY_CERS1
|
Thymidylate synthase
|
Cereibacter
|
MAHPEQQYLDLLAQTLERGDRRVDRTGVGTLSLFGAMLRFDLSDGQVPILTTKRVYWKTAVKEMLWFLTGGTNIRPLLQENVRIWSDWPLAAYRRESGEEISQAAFEQRILEDEAFAARWGELGPVYGRQWRRWLGPDGREHDQIAALIETLRTNPSSRRMLFHAWNVAEVGQMALPPCHMVYQYHVTSDGRLNALLYQRSVDLLLGAPFNFVGAAALQLMIAQQAGLVPGDLVWVGGDTHLYLNHLDQAREQTGRAPRDWPRMRLLRQADGIDDYRIEDFAVEGYDPHPAIAAEVAV
|
Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis.
|
A3PLD1
|
Q5E960
|
S39A3_BOVIN
|
Zrt- and Irt-like protein 3
|
Bos
|
MVKLLVAKILCMVGMFFFMLLGSLLPVKIIEMDFEKAHRSKKILSLCNTFGGGVFLATCFNALLPAVREKLKEVLTLAHISTDYPLAETIMLLGFFMTVFLEQLVLTFRKERPAFIDLETFNASSDAGSDSEYESPFMGGPRGHALYAEPHGHSHGLSVQELSRSSPLRLLSLVFALSAHSVFEGLALGLQEEGEKVVSLFVGVAIHETLVAVALGINMARSAMALRDAAKLAVTVSAMIPLGISLGLGIESAQGMPSSVASVLLQGLAGGTFLFVTFFEILAKELEEKSDRLLKVLFLVLGYTVLAGMVFIKW
|
Acts as a zinc-influx transporter.
|
Q5E960
|
P17953
|
ASA1_ENTFA
|
Aggregation substance
|
Enterococcus
|
MKQQTEVKKRFKMYKAKKHWVVAPILFIGVLGVVGLATDDVQAAELDTQPGTTTVQPDNPDPQVGSTTPKTAVTEEATVQKDTTSQPTKVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEKSAQEQPVVSPETTNEPLGQPTEVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPNITVVEKPAEDLGNVSSKDLAAKEKEVDQLQKEQAKKIAQQAAELKAKNEKIAKENAEIAAKNKAEKERYEKEVAEYNKHKNENGYVAKPVNKTLIFDREATKNSKVVSVKAAEYIDAKKLTDKHKDKKLLISMLSVDSSGLTTKDSKKAHFYYNNGAGGTLVVLHKNQPVTITYGNLNASYLGKKIASAEFQYTVKATPDSKGRLNAFLHDDPVATIVYGINIDPRTKKAGAEIEMLVRFFGEDGKEILPTKENPFVFSGASLNSRGENITYEFVKVGNTDTVHEINGSKVARHGNKVYSKTDIDVGTNGISISDWEAVQGKEYIGATVISTPNRIKFTFGNEIVNNPGYDGNSMWFAFNTDLKAKSITPYQEKGRPKQPEKATIEFNRYKANVVPVLVPNKEVTDGQKNINDLNVKRGDSLQYIVTGDTTELAKVDPKTVTKQGIRDTFDAEKVTIDLSKVKVYQADASLNEKDLKAVAAAINSGKAKDVTASYDLHLDQNTVTAMMKTNADDSVVLAMGYKYLLVLPFVVKNVEGDFENTAVQLTNDGETVTNTVINHVPGSNPSKDVKADKNGTVGSVSLHDKDIPLQTKIYYEVKSSERPANYGGITEEWGMNDVLDTTHDRFTGKWHAITNYDLKVGDKTLKAGTDISAYILLENKDNKDLTFTMNQALLAALNEGSNKVGKQAWSVYLEVERIKTGDVENTQTENYNKELVRSNTVVTHTPDDPKPTKAVHNKKGEDINHGKVARGDVLSYEMTWDLKGYDKDFAFDTVDLATGVSFFDDYDETKVTPIKDLLRVKDSKGEDITNQFTISWDDAKGTVTISAKDPQAFILAHGGQELRVTLPTKVKANVSGDVYNLAEQNTFGQRIKTNTVVNHIPKVNPKKDVVIKVGDKQSQNGATIKLGEKFFYEFTSSDIPAEYAGIVEEWSISDKLDVKHDKFSGQWSVFANSTFVLADGTKVNKGDDISKLFTMTFEQGVVKITASQAFLDAMNLKENKNVAHSWKAFIGVERIAAGDVYNTIEESFNNEKIKTNTVVTHTPEKPQTPPEKTVIVPPTPKTPQAPVEPLVVEKASVVPELPQTGEKQNVLLTVAGSLAAMLGLAGLGFKRRKETK
|
Aggregation substance allows donor and recipient strains to form tight aggregates which allow the non-motile bacteria to maintain physical contact over a period of time sufficient to permit conjugative transfer of the sex pheromone plasmid from donor to recipient strains.
|
P17953
|
Q9LEW3
|
AED1_ARATH
|
Apoplastic EDS1-dependent protein 1
|
Arabidopsis
|
MSIMRNFLSMIIMLCVCLNWCFAEGAEKSDSGKVLDSYTIQVSSLFPSSSSCVPSSKASNTKSSLRVVHMHGACSHLSSDARVDHDEIIRRDQARVESIYSKLSKNSANEVSEAKSTELPAKSGITLGSGNYIVTIGIGTPKHDLSLVFDTGSDLTWTQCEPCLGSCYSQKEPKFNPSSSSTYQNVSCSSPMCEDAESCSASNCVYSIVYGDKSFTQGFLAKEKFTLTNSDVLEDVYFGCGENNQGLFDGVAGLLGLGPGKLSLPAQTTTTYNNIFSYCLPSFTSNSTGHLTFGSAGISESVKFTPISSFPSAFNYGIDIIGISVGDKELAITPNSFSTEGAIIDSGTVFTRLPTKVYAELRSVFKEKMSSYKSTSGYGLFDTCYDFTGLDTVTYPTIAFSFAGSTVVELDGSGISLPIKISQVCLAFAGNDDLPAIFGNVQQTTLDVVYDVAGGRVGFAPNGC
|
Aspartyl protease involved in a homeostatic feedback mechanism regulating systemic immunity. Has only mild or no influence on local defenses. Acts downstream of salicylic acid to suppress systemic immunity.
|
Q9LEW3
|
Q9LH85
|
RLA23_ARATH
|
60S acidic ribosomal protein P2-3
|
Arabidopsis
|
MKVIAAFLLAKLGGNENPTSNDLKKILESVGAEIDETKIDLLFSLIKDHDVTELIAAGREKMSALSSGGPAVAMVAGGGGGGAASAAEPVAESKKKVEEVKDESSDDAGMMGLFD
|
Plays an important role in the elongation step of protein synthesis.
|
Q9LH85
|
Q7VRV9
|
NUOI_BLOFL
|
NDH-1 subunit I
|
Candidatus Blochmannia
|
MMKLKEFFINIISIFRSVYMVGMQAFSKRETYMYPDVACKLSSRYRGRIVLTRDSAGHERCVACNLCAVSCPVGCISLKKSENSEGRWYPEFFRINFSRCIFCGMCEEACPTAAIQLISDFEMSDYKRSDLVYEKSDLLISGPGKYKNYDFYQISGVKYSNKYKKESSFEEKPISVKTILP
|
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 ubiquinone. 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.
|
Q7VRV9
|
B2FRM5
|
QUEC_STRMK
|
Queuosine biosynthesis protein QueC
|
Stenotrophomonas maltophilia group
|
MKKAVVLLSGGMDSAAVIAMAQEQGFAVHALSVRYGQRHTSELDAAARVAKAQGVVAHKIVDVDLRSIGGSALTDDIDVPEAGGAGIPVTYVPARNTIMLSLALGWAEVLGANDIFCGVNAVDYSGYPDCRPEFVAAFQALANLATKSGVEGAGIKVHAPLQFLSKGQIVSEGVRLGVDFGLTVSCYNADANGAACGHCDACRLRAQGFAEAGVPDPTLYA
|
Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)).
|
B2FRM5
|
A8FJG3
|
RNPA_BACP2
|
Protein C5
|
Bacillus
|
MKKRNRLKKNEEFQKVFKKGQSMANRQFVIYQLDQPNQDELRLGLSVSKKIGNAVMRNRIKRLIRQVFLEEGHKLKQEKDYIVIARKPASELTFEETKKSLQHLFRKSAVYQQQPKKSS
|
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.
|
A8FJG3
|
Q5P089
|
LEPA_AROAE
|
Ribosomal back-translocase LepA
|
Aromatoleum
|
MQHIRNFSIIAHIDHGKSTLADRLIHFCGGLSDREMEAQVLDSMDLERERGITIKAQTAALHYKAKDGQVYNLNLIDTPGHVDFSYEVSRSLSACEGALLVVDASQGVEAQTVANCYTAIEQNVEVVPVLNKIDLPAADPESARKEIEDVIGVDASEAVLCSAKTGLGIEDVLETVVRRVPPPKGDPDAPLKALIIDSWFDNYVGVVMLVRVVDGVLKPKDRILLMANGAQYPCDQVGVFTPRSVARPQLSAGEVGFIIAGIKELQAAKVGDTVTLAMRPASEPLPGFKEIKPQVFAGLYPVESSEYDQLRDSLEKLRLNDASLQYEPEVSQALGFGFRCGFLGLLHMDIVQERLEREFDMNLITTAPTVVYEVVMNSGEVIRVENPAKLPDQSKIAEIREPIITATIFLPQDYVGPVITLCNLKRGAQVDMRYHGRQVQLIYDLPMNEVVMDFFDKLKSVSRGYASLDYEFKEYRAADLVKLDLLVGGEKVDALSVIVHRASAQYRGREVAAKLRGLIPRQMFDVAIQSAIGSHIVARETIKALRKNVLAKCYGGDISRKKKLLEKQKEGKKRMKQVGNVEIPQEAFLAVLRVDEGK
|
Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-dependent manner.
|
Q5P089
|
Q21WX7
|
LPXB_ALBFT
|
Lipid-A-disaccharide synthase
|
Rhodoferax
|
MANQISQHLQVALVAGETSGDLLAGLLLDGLREQWPLMTAVGIGGPQMARRGLVAWWGHDKLSVHGFGWEVLRRYREIVGIRRQLKTRLLRQQPDVFIGVDAPDFNLDLEQDLKAQGIKTVHFVSPSIWAWRPERVEKIRRSVDHVLCIFPFEPALLARHGIAATYVGHPLANVIPMEPDRSAARAALGLADGDQVVAILPGSRQSEINHLALRFFQAAALINKAHPAIKFIVPAIPALRAGIEHAARASGMQAHLQIIAGQSHTVLAACDVTLIASGTATLEAALFKRPMVIAYRMGWLSWQIMRRKQLQPWVGLPNILCQDFVVPELLQDAATAQALADAVLLWIDAKASHPAKIAALQQKFTALHTELQRDTPRLAAHAIQQVLQG
|
Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
|
Q21WX7
|
Q0I1J8
|
TRMD_HAES1
|
tRNA [GM37] methyltransferase
|
Histophilus
|
MWIGIISLFPEMFKAITEYGVTGRAVRQNLLEIQYWNPRDFTFDKHKTVDDRPYGGGPGMLMMVQPLRDAIHCAKSVAGDGVKVIYLSPQGRKLDQNGVQELARNQKMIFVCGRYEGIDERLIETEIDEEWSIGDYVLTGGELPAMTLIDAVARFVPCVLGKQASAQEDSFAEGLLDCPHYTRPEQLNGLTVPPVLMSGNHEEIRKWRLKQSLQRTWLRRPELLESLALTDEQSKLLSQIKQENS
|
Specifically methylates guanosine-37 in various tRNAs.
|
Q0I1J8
|
A8GMY3
|
MNMA_RICAH
|
tRNA-specific 2-thiouridylase MnmA
|
spotted fever group
|
MINLGDKHSTIVVAMSGGVDSSAVAAMLHEQGHNVIGITLQLYDHGMAVGKKNACCAGQDIYDAKMVANKLGIPHYVLDYESKFKESVIDNFVDSYLQGETPLPCVQCNNSVKFRDLIKTARELGASQLATGHYVRKVSGDNGVELHTGLDPAKDQSYFLFTTTKEQLEYLSFPLGWFTKDETRKLASKFGLEVAYKPDSQDICFVPDGNYKSVINTIRPNASESGKIIHINGFALGEHSGIINYTIGQRRGLGIAYNEPLYVVKIDPKDNIVYVGPEAALHVQEFIIKDVNWLADEIKDNKKLEVAVKIRSTRPPRLAAISKLGDDKMKIRFLSAEKAVAPGQACVIYAGERVLGGGWITRDIR
|
Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
|
A8GMY3
|
A2YXU2
|
PSA7A_ORYSI
|
20S proteasome subunit alpha-4-A
|
Oryza sativa
|
MARYDRAITVFSPDGHLFQVEYALEAVRKGNAAVGVRGTDTVVLGVEKKSTPKLQDSRSMRKIASLDTHIALACAGLKADARVLINRARVECQSHRLTVEDPVTVEYITRYIAGLQQKYTQSGGVRPFGLSTLIVGFDPYTEKPALYQTDPSGTFSAWKANATGRNSNSMREFLEKNYKDTSGKETIKLAIRALLEVVESGGKNIEIAVMTHKDGLRELEEAEIDEYVAEIEAEKAAAEAAKKGAPKET
|
The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
|
A2YXU2
|
P0DSK3
|
TX17A_MYRGU
|
U-myrmeciitoxin(01)-Mg7a
|
Myrmecia
|
MKLSCLSLALAIILLLAIVHSPNMEVKALAGPEADAIGFADAFGEADAFGEADAFGEADAFGEADAFGEADAKRSKSSSKTKPKKPKKPKKKIKIPDWVKSGGKMVGEAVAGAVADAAVSAVMDAAVGTTAEPEQ
|
May have antimicrobial properties, like most ant linear peptides.
|
P0DSK3
|
O31699
|
YKUV_BACSU
|
Thiol-disulfide oxidoreductase YkuV
|
Bacillus
|
MKLRQPMPELTGEKAWLNGEVTREQLIGEKPTLIHFWSISCHLCKEAMPQVNEFRDKYQDQLNVVAVHMPRSEDDLDPGKIKETAAEHDITQPIFVDSDHALTDAFENEYVPAYYVFDKTGQLRHFQAGGSGMKMLEKRVNRVLAETE
|
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
|
O31699
|
B4RJF9
|
ATPG_NEIG2
|
F-ATPase gamma subunit
|
Neisseria
|
MAVGKEILTKIRSVQNTQKITKAMQMVSTSKMRKTQERMRLARPYAEKVRMVMSHLAQTNTDHGIPLLESHREIRRVGFILITSDKGLCGGLNANVLKKFLAQVQEYRNQGIEEEIVCLGSKGLMACQSIGLNVVASAVNLGDTPKMEMLLGPLTELFQRYEKHEIDKIHLVYSGFVNTMRQEPRMEVLLPIGENVIGDSAPKPPFSWEYRYEPTALAVLEYLVRRYLESVVYQALSDNMASEQAARMVAMKAATDNAGNAIKELRLVYNKSRQAAITTELSEIVAGAAAV
|
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.
|
B4RJF9
|
A8GNF9
|
RBFA_RICAH
|
Ribosome-binding factor A
|
spotted fever group
|
MKKLTKTNSHRQQKLASIINEALIEILRRGKMLDSRLFNCPLTITKVIVTADLKIANCYFLPFNTKLTINEVMNALNNSKKAIRNFITNKINVKFSPDIRFHYDHGFDNAIKVEELLKNIQVLGDKLNH
|
One of several proteins that assist in the late maturation steps of the functional core of the 30S ribosomal subunit. Associates with free 30S ribosomal subunits (but not with 30S subunits that are part of 70S ribosomes or polysomes). Required for efficient processing of 16S rRNA. May interact with the 5'-terminal helix region of 16S rRNA.
|
A8GNF9
|
A4SL70
|
KDSB_AERS4
|
CMP-2-keto-3-deoxyoctulosonic acid synthase
|
Aeromonas
|
MSFVVVIPARYASTRLPGKPLADIHGKPMVQHVVEKALQSGADRVIVATDDERVHSALASFAEQAGVEVCMTSQDHQSGTERLAEVCRHYGFSADTIVVNVQGDEPLIPPAIIRQVADNLAAASAPMATLSVPIQDAEEAFNPNAVKVVTDKEGYALYFSRACIPWDRDRFAASDRAAGSHEQIGDHYQRHIGIYAYRAGFIQRYVDWAPSVLEQVEALEQLRVLWYGEKIHVAQALQAPPVGVDTQADLDKVRALLAN
|
Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria.
|
A4SL70
|
Q3KME9
|
RPIA_CHLTA
|
Phosphoriboisomerase A
|
Chlamydia
|
MSKQPENSFSSDKFFPIKQKLALEAVALVEPGMCVGLGSGSTAREFILALGDRVRTERLVITAVASSRISQLLAEAVGIPLLDHSLLQDVDLVVDGADEVDPCLRMIKGGGGALFREKILLQSGKRNVILVDERKLVPTLGKFSLPIEIAPFGCSSVQRILNKQGYFGEWRETSAGERFITDNGNYIYDVRTPDSYANPEEDMIRLLQIRGIIDVGFVIAKAEVWVGYADGSIVRKKKHNEY
|
Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
|
Q3KME9
|
Q9Z0T6
|
PKDRE_MOUSE
|
Polycystic kidney disease and receptor for egg jelly-related protein
|
Mus
|
MWPGPALLLLGLGLGLGSQPPPTGPRGLPGVLRGAPGLGQGAESSVRGGDTGGLSPRAAPRHASPTPPRRCPSGAAARVLLKVNSSDPAAAKANVSCQTAPCIMQPVKINRKDQNAPLILSRDEEATLNITVRWYCPDALVIRKSWVYFSVASVNDTPDWNRPVLLPQVAVSKGFSLHIPKYALPYGVYVFNFTLSIFRWDLAWPTVTGSDIIYIWVRKRPLKAVLLGAPRVTVKFSDELILNGSMSYDPEADIPTWGLQFFWYCTTNPRYYSGNYVLVINQAVCHPEQDSLNWPWAVGSVLTIPPKTLRGNGVYYFRMVVQKQNRTAFSDKTVHVLQGLQPKAHISCIENCGPTLGVSDRFSLFLNCPSCGRQDLYSWSILSLTGHEVMFDWAGQAITRRNGPYLSIKAFAFRNFLENRVWVSLILKSWSGMTTTLRHPVVINHGPRVGKCKINPASGISMVTKFAVECSDFKDENLPLKYKIIVSELDSIGAISSVEENTLGSVVYSGAEPITPAFFLPVGTVTDEYNVRLYVQVYDSLGTFSQVTLQATVTAPTVRDSSKDVLQQLLNVTMKPTSLLSTLLQKQDWLQAGYLTYVVISVLNNIKGEQELQDDRARLLEHLVKQSLTFAMNTADEIGQSVMVITKLTQKASDLSQADLEATSFRLRQASQDLQEYQHRHKHLQQVEVVGTGILTSLSNLLKLINPYYTLQDPLFVVESLSDTILANKVPGSKTTALRTSYFNMYVEKVENWNVFKAFRNDSLCPNCLRATLNASTVPRLPAKAPISMMFCEFADDPFPWLTYPENISVDVVGFRMTGVADNNKVIEITPDIAEVYLVRKDLTPSSFNLTVGPGIKSDGFSKVTTGGISFEVDSRWTGELLIHIVTNVTVLFEALVYEGCQLTPTNLMATFLVPNDIPPIVKWSGLFDPTCSVKEARVVCLSSSLLRSIAQRRFSFKYNISMVLQASRFVLKPTNKLVRIALFMVHCLDMYGIQSDWQQSTCVLGEKTTWKTVHCVCRNGRRSRRQLTSVKLTYHHLHTHFVTAKVIVVPNPVDLRLAIISNLTQNPATFLAVLFIMILYAILAFWALHRDVIDLYFRDNVVILTDNDPFDTLCYLVTIFTGSRWGSGTRANVFIQLMGTEGTSDVHCLSHPYFKTLYRGSINTFLLTTKNDLGDIHSIRVWHDNSGEAPSWYLSRIKVENLFNKRIWLFVCRRWLSVDTTLDATFSVTNPDEPLKRTDFFMIDVRDKLRKNHMWISIFTEIVPKPFNRLQRLSCCLAMLLSSLVCNIMFFNLNQKEKIESRHMHIIRSMLIGIESVVITIPVQLLITFFFTYSQKNLKMNLDKVAPQKHPLMSEEGLSWKERLHKWHEYEMKALPRRAAVSTSAPEEKEAFETSQKHEKADTQMSNKNSSNNNQEASEGVPPKAFSSQPHTTESVQKKTQIILPRWCVYIAWFLVFATSGISSFFIVFYGVTYGYAKSIEWLFASFCSFCQSVFLVQPCNILLRSGTRSYKPKYCKNLSWSSKYHYSEIRLQGLTMTQEEMEQLHEDIAYVRSLSMYQPITEDKIQILRRENRIRRRSFLFLSYLVTHFIFLTLLLLLIFSLRHNDSFYYNQFIRHRFSVDLATVMKLGDIYTWLHGVFLPLLHNDPNPTFLPDSSSKILGLPLVRQVRARPSNKTCLLAKKFVQSSVAGEIHCHPQYGIDPEDTQHYSSVWSKAGKQSTDKASHGFTYKPPGKRWVYHSYGVLNTYGSGGYVFYFFPGQQMFNSTVRLKELEGKNWLDELTWAVIVELTTLNPDTSLMCSISVVFEVSPLGVVNSSLSVYSFSLADFNRKTSSEIYLYAAILIFFCAYVVDEGYIIRQERASYIRSVYNLLNFSLKCMFALLIVLFFWKYFLATKMVQLYLADPEAFIPFHAVSRVDHFMRIILAFLLFLTILKTLRYSRFFYNVRLAQKAIQAALPGICHTALVVSIYSFMYVAFGYLVFGQHEWNYSNMIHATQTIFSYCVSAFQNTEFSGNKVLGVLFLSSFMLVMICIFINLFQAVILSAYDEMKQPVYEEPSDEAEAVTYLCNRLKSGFDFLTTRSRDKDQSNFFVDMLYGQPEKNTRRFLGLKARNINGKKMIYLVV
|
May have a central role in fertilization. May generate a Ca(2+) transporting channel directly involved in initiating the acrosome reaction of the sperm.
|
Q9Z0T6
|
P82414
|
GTX3A_NEOGO
|
Ponericin-G1
|
Pachycondyla
|
GWKDWAKKAGGWLKKKGPGMAKAALKAAMQ
|
Shows a broad spectrum of activity against both Gram-positive and Gram-negative bacteria. Has also antimicrobial activity against S.cerevisiae. Has insecticidal and non-hemolytic activity.
|
P82414
|
Q60181
|
RPO2C_METJA
|
DNA-directed RNA polymerase subunit B'
|
Methanocaldococcus
|
MKNLASREVNIYVNGKLVGTTDKPEELVNFIREKRRKGELPQYTTVAYNEESNDIHINTDAGRIVRPLIVVENGKPKLTKEHIEKLKKGEITFSDLVKEGVIEYLDAEEEENAYIALSEEELTEKHTHLEIDPLTILGIGAGVAPYPEHNSAPRITMAAAMGKQSLGIPMSNIKWRLDTRGHYLHYPQVPIVRTKHQEILGFDKRPAGQNFVVAIMSYEGYNMEDAIVFNKSAIDRGLGRSTFFRTYDACERRYPGGQMDRFEIPDKGVRGYRSEECYRYLEEDGIVAVESHVKGGDVIVGKTSPPRFLEEHEITIQVKPQRRDSSVVVRHGEEGYIDKVILTETKEGNRLVKVKVRDLRIPELGDKFASRHGQKGVMGLTVPQEDLPFTESGIVPDIIINPHAIPSRMTVGQLLEMLGGKVGALEGRRIDGTIFSGEKEWDLRKALEALGFKHHGKEVMYDGKTGKKFEVEIYIGIAYYQKLHHLVAGKIHARSRGPVQVLTRQPTEGRAREGGLRFGEMERDVLIGHGAAMLLKERLMDESDPYDICICSKCGDFAILDYKRGLKYCPICGEIENLYSSKKIPFVRIPYAFKLLLDELKSMCILPRIKVRDKVELEDFEEFVEKLEKEKVKQKQ
|
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this organism) is implicated in DNA promoter recognition and in nucleotide binding.
|
Q60181
|
C3K424
|
HEM3_PSEFS
|
Pre-uroporphyrinogen synthase
|
Pseudomonas
|
MSSREIRIATRKSALALWQAEYVKARLEQAHPGLKVSLVPMVSRGDKLLDSPLSKIGGKGLFVKELETALLENEADIAVHSMKDVPMDFPEGLGLFCICEREDPRDAFVSNTYASLDALPLGSIVGTSSLRRQAQLLTRRPDLQIRFLRGNVNTRLAKLDAGEYDAIILAAAGLIRLGFEDRITSAISVEDSLPAGGQGAVGIECRTADSDIHALLKPLDHHDTEVRVTAERALNKHLNGGCQVPIACYAVLEGENLWLRGLVGDPEGGNLLTAEVRGPQCDATALGIQVAQALLDKGAGAILQKVYGEAGPQ
|
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.
|
C3K424
|
B7UFS6
|
MENH_ECO27
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
|
Escherichia
|
MILHAQAKHGKPGLPWLVFLHGFSGDCHEWQEVGEAFADYSRLYVDLPGHGGSATISVDGFDDVTGLLCKTLVSYNILNFWLVGYSLGGRVAMMAACQELAGLCGVVVEGGHPGLQNAEQRAERQRSDRQWAQRFRTEPLTAVFADWYQQPVFASLNDDQRRGLVALRSNNNGATLAAMLEATSLAVQPDLRANLSARTFAFYYLCGERDSKFRALAAELAADCHVIPRAGHNAHRENPAGVIASLAQILRF
|
Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC).
|
B7UFS6
|
B5BIN8
|
ATPA_SALPK
|
F-ATPase subunit alpha
|
Salmonella
|
MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQGEMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVGRGLLGRVVNTLGAPIDGKGPVDNDGFSAVEAIAPGVIDRQSVDQPVQTGYKAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQKASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFRDRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLERAARVNADYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITDGQIFLESNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQYRELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFAAERGYLADVELAKIGSFEAALLAYVDRDHAPLMQEINQSGGYNDEIEGKLKGILDSFKATQSW
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit.
|
B5BIN8
|
Q9CN56
|
KT3K_PASMU
|
Probable ketoamine kinase PM0587
|
Pasteurella
|
MWKHVSQVLADQFGAYYSIKHKEKIHTGEMHEAWIIDDGIQPVFLKVNDKTFRSMFRAEADQLLLLAKTNTINVPNVYTVGCSHTHSFLLLEALPLDKTNPVDAMGKFGEQLAKLHLIKGADNYGLDFDTWLGPEYQPNGWKENWATFFSEQRIGWQLQICREKNLVFGDIEVLVKKVAELLAKHKPQPALLHGNLWIENCATVKQEIFTYDPACYWGDRECDLAFSELFEPFPRQFYESYDRTYPIDEGYPERKAIYQLYYLLNFSHRFNKHYVELTKKFIHDILSR
|
Ketoamine kinase that phosphorylates ketoamines on the third carbon of the sugar moiety to generate ketoamine 3-phosphate.
|
Q9CN56
|
A1JML4
|
ADD_YERE8
|
Adenosine aminohydrolase
|
Yersinia
|
MIDPRLPLTDIHRHLDGNIRAQTILDLGRQFNLSLPADELEALRPHVQITKTEPDLVSFLQKLDWGVAVLGSLEACRRVAYENVEDAANAGLHYAELRFSPFYMAMKHQLPVAGVVEAVIDGIQSGCRDFDIDIRLIGILSRTFGEQACLQELDGLLAHRDAITALDLAGDELGFPGGLFRSHFNRARDAGWRITVHAGEAAGPESIWQAIRELGAERIGHGVKAVEDIKLMDYLAEHNIGIESCLTSNIQTSTVASLAAHPLATFLRHGVLASINTDDPAVQGIEIANEYHIAAPAAGLTPQEIRQAQENGLTMAFISEQEKQVLRDKIRN
|
Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
|
A1JML4
|
A1RWT8
|
RS4_THEPD
|
30S ribosomal protein S4
|
Thermofilum
|
MGDPKKPRKKWQGPSHPWRKETLLEEMQLVGEYGLRNKRELWIAKSLLREIRAKARKLLALPAEERIKLEKPLVSRLYKMGLLPSEDASLDDVLSLTVRDVLERRLQTIVYRKGLATTIRHARQLITHGHIAVNSRRVRSPGYLVSRDEENFISYYEGSPLAKMAQGGAQNV
|
With S5 and S12 plays an important role in translational accuracy.
|
A1RWT8
|
Q7VIE2
|
GRPE_HELHP
|
HSP-70 cofactor
|
Helicobacter
|
MEEQEEKQYNQNIQDNEEGTQMREELQESTSAQQTLQEQEIDYQAKYLELKDQYVRAFADFENTKKRLERDKNQSLEYAYERIMNDLLPVLDTLEKALESAQSNPEAGAIAQGLQLTLEGFLKVLSKHGVEVIATDGEFDPNLHECLMQVPDANKNDGEILQTLQKGFVYKHRVLRPSMVSVVKN
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
|
Q7VIE2
|
P07476
|
INVO_HUMAN
|
Involucrin
|
Homo
|
MSQQHTLPVTLSPALSQELLKTVPPPVNTHQEQMKQPTPLPPPCQKVPVELPVEVPSKQEEKHMTAVKGLPEQECEQQQKEPQEQELQQQHWEQHEEYQKAENPEQQLKQEKTQRDQQLNKQLEEEKKLLDQQLDQELVKRDEQLGMKKEQLLELPEQQEGHLKHLEQQEGQLKHPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPEQQEGQLELPQQQEGQLELSEQQEGQLELSEQQEGQLKHLEHQEGQLEVPEEQMGQLKYLEQQEGQLKHLDQQEKQPELPEQQMGQLKHLEQQEGQPKHLEQQEGQLEQLEEQEGQLKHLEQQEGQLEHLEHQEGQLGLPEQQVLQLKQLEKQQGQPKHLEEEEGQLKHLVQQEGQLKHLVQQEGQLEQQERQVEHLEQQVGQLKHLEEQEGQLKHLEQQQGQLEVPEQQVGQPKNLEQEEKQLELPEQQEGQVKHLEKQEAQLELPEQQVGQPKHLEQQEKHLEHPEQQDGQLKHLEQQEGQLKDLEQQKGQLEQPVFAPAPGQVQDIQPALPTKGEVLLPVEHQQQKQEVQWPPKHK
|
Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
|
P07476
|
Q89YT0
|
END4_BACTN
|
Endonuclease IV
|
Bacteroides
|
MKYIGAHVSASGGVEFAPVNAHEIGANAFALFTKNQRQWVSKPLKEENIRLFKENCTKYNFQTDYILPHDSYLINLGHPEEEGLEKSRAAFLDEMQRCEQLGLKLLNFHPGSHLNKISIEDCLALIAESINLTLEKTKGVTAVIENTAGQGSNLGSEFWQLRYIIDRVNDKSRVGICLDTCHTYTAGYDIVNDYDKVFDEFEKEVGFEYLRGMHLNDSKKELGSHVDRHDNIGQGLIGSAFFERLMKDSRFDNMPLILETPDESKWAEEIAWLRSVE
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
Q89YT0
|
A4QG75
|
PROA_CORGB
|
Glutamyl-gamma-semialdehyde dehydrogenase
|
Corynebacterium
|
MSSTTLTDDQIRDNERTEVLAKATAAKNIVPDIAVLGTGPKNAILRAAADELVARSAEIIEANASDIEAGRANGMEESMIDRLALDESRIEGIAGGLRQVAGLTDPVGEVLRGHVMENGIQMKQVRVPLGVMGMVYEARPNVTVDAFGLALKSGNVALLRGSSTAVHSNTKLVEILQDVLERFELPRETVQLLPCQTRGSVQDLITARGLVDVVIPRGGAGLINAVVTGATVPTIETGTGNCHFYIDAEAKLDQAIAMVINGKTRRCSVCNATETALLDAALSDSDKLAVVQALQEAGVTIHGRVAELEAFGATDVVEATETDWDSEYLSFDIAVAVVDGVDGALAHIAKYSTKHTEAIATQNIETAQRFADRVDAAAVMINASTAYTDGEQYGMGAEIGISTQKLHARGPMALPELTSTKWILQGTGQIRP
|
Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
|
A4QG75
|
Q3BU06
|
FLGI_XANC5
|
Basal body P-ring protein
|
Xanthomonas
|
MNLSSLPFRLLAAAVALCAIAAPASAERIKDLAQVGGVRGNALVGYGLVVGLDGSGDRTSQAPFTVQSLKNLLGELGVNVPANVNPQLKNVAAVAIHAELPPFAKPGQPIDITVSSIANAVSLRGGSLLMAPLKGADGQVYAMAQGNLVVGGFGAQGKDGSRVSVNVPSVGRIPNGATVERALPDVFAGTGEITLNLHQNDFTTVSRMVAAIDSSFGAGTARAVDGVTVAVRSPTDPGARIGLLSRLENVELSPGDAPAKVVVNARTGTVVIGQLVRVMPAAIAHGSLTVTISENTNVSQPGAFSGGRTAVTQQSTITATSEGSRMFKFEGGTTLDQIVRAVNEVGAAPGDLVAILEALKQAGALTAELEVI
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
Q3BU06
|
Q91X60
|
ACHA2_MOUSE
|
Neuronal acetylcholine receptor subunit alpha-2
|
Mus
|
MAPSHPAFQFWIHLYLWCLLLMPAVLAQQGSHTHAEDRLFKHLFGGYNRWARPVPNTSDVVIVRFGLSIAQLIDVDEKNQMMTTNVWLKQEWNDYKLRWDPAEFGNITSLRVPSEMIWIPDIVLYNNADGEFAVTHMTKAHLFFTGTVHWVPPAIYKSSCSIDVTFFPFDQQNCKMKFGSWTYDKAKIDLEQMERTVDLKDYWESGEWAIINATGTYNSKKYDCCAEIYPDVTYYFVIRRLPLFYTINLIIPCLLISCLTVLVFYLPSECGEKITLCISVLLSLTVFLLLITEIIPSTSLVIPLIGEYLLFTMIFVTLSIVITVFVLNVHHRSPSTHNMPNWVRVALLGRVPRWLMMNRPLPPMELHGSPGLKLSPTYHWLETNMDAEEREETEEEEEEEEDENICMCAGLPDSSMGVLYGHGSLHLRAMGPEAKTPSQASEILLSPQIQKALEGVHYIADHLRSEDADSSVKEDWKYVAMVVDRIFLWLFIIVCFLGTIGLFLPPFLAGMI
|
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
|
Q91X60
|
A5WDU0
|
METK_PSYWF
|
Methionine adenosyltransferase
|
Psychrobacter
|
MHDYQLFTSESVSEGHPDKMADQISDALLDAIMREDLHARVACETLVKTGAVVLAGEISTTANIDIERIVRDTVNSIGYNHSDLGFDGETCAVINMIGKQSPEIAQGVDRMNPEDQGAGDQGLMFGYASNETEVLMPAPIEFAHRLMERQSELRRSGELKWLRPDAKAQVTLKYTNGTPSAIDAVVLSTQHDPDISQADLQEAVMENIIKHVLPADLLHAGTRYHINPTGKFVIGGPVGDAGITGRKIIVDTYGGMARHGGGAFSGKDPSKVDRSAAYAGRYVAKNIVAAGLAERCEVQISYAIGVAEPTSISVNTFGTAKVSAEVIIELIRTHFDLRPYGITHMLNLLQPMYQQTATYGHFGRPGSETAFTWEKTDKAEILRADANI
|
Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme.
|
A5WDU0
|
B8CM22
|
RNPH_SHEPW
|
tRNA nucleotidyltransferase
|
Shewanella
|
MRPSNRTPAQSRPVTITRQFTAHAEGSVLVEFGDTKVLCTASFEEGVPRFLKGQGQGWVTAEYGMLPRSTHSRMNREAARGKQSGRTQEIQRLIGRSLRAAVDMKLLGENTIVIDCDVIQADGGTRTAAITGACVALVDALNWARGKGILKTNPLKFLIAAVSVGIYKGEPICDLEYIEDSAAETDMNVVMTETGKMIEIQGTAEGEPFTHEELLSLLDLAKHGIREIVDIQKASLS
|
Phosphorolytic 3'-5' exoribonuclease that plays an important role in tRNA 3'-end maturation. Removes nucleotide residues following the 3'-CCA terminus of tRNAs; can also add nucleotides to the ends of RNA molecules by using nucleoside diphosphates as substrates, but this may not be physiologically important. Probably plays a role in initiation of 16S rRNA degradation (leading to ribosome degradation) during starvation.
|
B8CM22
|
Q03SQ0
|
SECA_LEVBA
|
Protein translocase subunit SecA
|
Levilactobacillus
|
MPNILKRWVESDRRTLRRLSNLADKVGAYADDYAQLSDDDLKAKTPEFKQRYQDGETLDDLLPEAFAAIREGAKRVLGLYPFHVQIMGGIVLHEGNIAEMKTGEGKTLTATMPVYLNALAGKGVHVVTVNEYLSARDATEMGELYNWMGLTVGLNSAEKSPEEKREAYQADITYSTNGEIGFDYLRDNMVVYKEDMVQRPLNFAIVDEVDSILIDEARTPLIISGQSEGTSALYRRVDRFAKTLHEKDDFKIDLESKTVALTDTGIEKAEKYFNLKNLYDTDNTALTHHMDQALRANFIMLRDKDYVVQDGEVLIVDSFTGRVMDGRRYSDGLHQAIEAKEGVEIQEETKTMANITYQNLFRMYKKLSGMTGTAKTEAEEFREIYNMEVVSVPTNKPVVRVDEPDLLYPTLESKFNAVVKEIKDLHEKGQPMLIGTVAVETSEYLSQRLDEENIPHVVLNAKNHAKEADIIQNAGQRGAVTIATNMAGRGTDIKLGPGVVEIGGLAVIGTERHESRRIDNQLRGRSGRQGDPGMTQFYLSLEDDLMRRFGSDRVKSFLERMNVDGEDAVIRSRMITKQVESAQKRVEGNNYDSRKNVLQYDDVMRQQRDVMYGERNQVINQDKSLKWVLMPMIKRTVDRVVSLHTQGEQSDWDLDTLLDFGISAMVSPDKISLDDLKNKSADEIKAFFMELAEDVYAEKQKQLYDPAQMLEFEKVVLLRVVDSHWTDHIDAMDQLRQSIGLRGYGQLNPLVEYQQDGFRMFEEMISDIDYDATRLFMKSEIRQNITR
|
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. Has a central role in coupling the hydrolysis of ATP to the transfer of proteins into and across the cell membrane, serving as an ATP-driven molecular motor driving the stepwise translocation of polypeptide chains across the membrane.
|
Q03SQ0
|
Q482M9
|
RLMF_COLP3
|
rRNA adenine N-6-methyltransferase
|
Colwellia
|
MHKKNRHNQGYNFTALVKAHPGLLQFIIKNQYNNQDTIDFANPQAVKALNLSLLKSEYHVKFWDIPDGYLCPAIPGRVDYIHHLQDLLAATPKTLLPNKTPINVLDIGTGASCIYPILGQREYDWHFVASDVDPISIKVAKHIISSDKSLNRNINCRLQPNSNQIFNGIIAEDEFYHLTICNPPFHSSLAEASKGTARKIKNLNKGNHSSKNQDKTLNFGGQKAELWCPGGELAFIGKMIKESKAYQKQVLWFTCLVSKKDHLSKLKLSLKKSDAKQIKVIDMAQGQKISRFIAWSFYDVN
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
Q482M9
|
Q0TLV0
|
CAIA_ECOL5
|
Crotonobetainyl-CoA dehydrogenase
|
Escherichia
|
MDFNLNDEQELFVAGIRELMASENWEAYFAECDRDSVYPERFVKALADMGIDCLLIPEEHGGLDAGFVTLAAVWMELGRLGAPTYVLYQLPGGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPGAGSDVGSLKTTYTRRNGKIYLNGSKCFITSSAYTPYIVVMARDGASPDKPVYTEWFVDMSKPGIKVTKLEKLGLRMDSCCEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADNGTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQYR
|
Catalyzes the reduction of crotonobetainyl-CoA to gamma-butyrobetainyl-CoA.
|
Q0TLV0
|
Q32BW5
|
GCSP_SHIDS
|
Glycine dehydrogenase (aminomethyl-transferring)
|
Shigella
|
MTQTLSQLENSGAFIERHIGPDAAQQQEMLNAVGAQSLNALTGQIVPKDIQLATPPQVGAPATEYAALAELKAIASRNKRFTSYIGMGYTAVQLPPVILRNMLENPGWYTAYTPYQPEVSQGRLEALLNFQQVTLDLTGLDMASASLLDEATAAAEAMAMAKRVSKLKNANRFFVASDVHPQTLDVVRTRAETFGFEVIVDDAQKVLDHQDVFGVLLQQVGTTGEIHDYTALISELKSRKIVVSVAADIMALVLLTAPGKQGADIVFGSAQRFGVPMGYGGPHAAFFAAKDEYKRSMPGRIIGVSKDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIASLYAVYHGPIGLKRIANRIHRLTDILAAGLQQKGLKLRHAHYFDTLCVEVADKAGVLARAEAAEINLRSDILNAVGITLDETTTRENVMQLFSVLLGDNHGLDIDTLDKDVAHDSRSIQPAMLRDDEILTHPVFNRYHSETEMMRYMHSLERKDLALNQAMIPLGSCTMKLNAAAEMIPITWPEFAELHPFCPPEQAEGYQQMIAQLADWLVKLTGYDAVCMQPNSGAQGEYAGLLAIRHYHESRNEGHRDICLIPASAHGTNPASAHMAGMQVVVVACDKNGNIDLADLRAKAEQAGDNLSCIMVTYPSTHGVYEETIREVCEVVHQFGGQVYLDGANMNAQVGITSPGFIGADVSHLNLHKTFCIPHGGGGPGMGPIGVKAHLAPFVPGHSVVQIEGMLTRQGAVSAAPFGSASILPISWMYIRMMGAEGLKKASQVAILNANYIASRLQDAFPVLYTGRDGRVAHECILDIRPLKEETGISELDIAKRLIDYGFHAPTMSFPVAGTLMVEPTESESKVELDRFIDAMLAIRAEIDQVKAGVWPLEDNPLVNAPHIQSELVAEWAHPYSREVAVFPAGVADKYWPTVKRLDDVYGDRNLFCSCVPISEYQ
|
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
|
Q32BW5
|
O31164
|
RS17_SPICI
|
30S ribosomal protein S17
|
Spiroplasma
|
MERNSRKVLQGRVISDNLKKTITVLVETYKNHPLYKKRVKYSKKYLAHDEQNQAHIGDKVSIMETRPLSKTKHFRLIEVIEKAIG
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
O31164
|
P46380
|
AROQ_AMYME
|
Type II DHQase
|
Amycolatopsis methanolica group
|
MKVFVLNGPNLGRLGKREPA
|
Catalyzes a trans-dehydration via an enolate intermediate. Is involved in both the catabolism of quinate and the biosynthesis of aromatic amino acids.
|
P46380
|
O77418
|
ASP3_ANISI
|
ASPI-3
|
Anisakis simplex complex
|
MMFTPLIVLTLLVLATAEHQCGPNEQWSGCPKCELQSGESDKPCATICGEPKCYCSPDKYRRIPDGRCIRKIQCPQH
|
Defends the organism against the host's proteinases.
|
O77418
|
Q07933
|
ANFD_RHOCA
|
Nitrogenase component I
|
Rhodobacter
|
MPYHEFEVSKCIPERREHAVMKAAGEDLTSCLPKGYLNTIPGTISERGCAYCGAKHVIGTPMKDVIHISHGPNGCTYDTWQTKRYISDNDNFQLKYTFATDVKEKHVVFGAEGLLKKSMHEAFDAFPNIKRMTVYQTCTTALIGDDVDAIAKEVMEERGDVDVFVCNSPGFAGPSQSGGHHKINIAWLNQKVGTVEPDYLGEHVINYVGEYNIQGDQEVMIDYFNRMGIQVLSTFTGNGSYDSLRMMHRAHLNVLECARSAEYICDELRARYGIPRLDIDGFGFEPLANSLRKVALFFGIEDKAEAIIAEEYAKWKPQLDWYKERLKGKKVCLWPGGSKLWHWAHAIEEEMGLKVVSVYTKFGHQGDMEKGVSRCGEGALAIDDPNELESVEAIEMLKPDIIFTGKRPGEFVKKHGVPYLNAHAYHNGPYKGFEGWVRFARDIYNAIYSPMRQLAALDISAPDAAITSGFRTAKMNADLTVSDEVKFSEVLHEYTGKYDSIAEIRARNQPMPPSRKLRDAVQPAAE
|
This iron-iron protein is part of the nitrogenase complex that catalyzes the key enzymatic reactions in nitrogen fixation. Other nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-iron protein.
|
Q07933
|
Q4FK66
|
PR38A_MOUSE
|
Pre-mRNA-splicing factor 38A
|
Mus
|
MANRTVKDAHSIHGTNPQYLVEKIIRTRIYESKYWKEECFGLTAELVVDKAMELKFVGGVYGGNIKPTPFLCLTLKMLQIQPEKDIIVEFIKNEDFKYVRMLGALYMRLTGTAIDCYKYLEPLYNDYRKIKSQNRNGEFVLMHVDEFIYELLHSERVCDIILPRLQKRYVLEEAEQLEPRVSALEEDMDDVESSEEEEEEDEKLERVPSPDHRRRSYRDLDKPRRSPALRYRRSRSRSPRRRSRSPKRRSPSPRRERHRSKSPRRHRSRSRDRRHRSRSKSPGHHRSHRHRSHSKSPERSKKSHKKSRRGNE
|
Involved in pre-mRNA splicing as a component of the spliceosome.
|
Q4FK66
|
Q896Y2
|
MGLA_CLOTE
|
Galactose/methyl galactoside import ATP-binding protein MglA
|
Clostridium
|
MVENNIILEMNGISKNFPGVKALDGVDLKVKKGTVHALMGENGAGKSTLMKCLFGIYRSDDGEIVLGGKKVQFKNAKDALENGISMIHQELHPVPHRSVMENVWLGRFPVKKVFGLGIVDHKKMYEDTKDLLGKLKMNIDPNTLVSKLSVSQVQGLEIAKAVSYNSKIIVMDEPTSSLTENEVTHLFNIISDLKNQGVAIIYISHKMEEILKIADEVTIMRDGKYIGTWEAEGLTTDLIISKMVGRDLTNRFPPKENTPGEVIMKVENLTSANNKSFKDISFELRKGEILGIGGLVGAQRTELVESIFGLRKIETGKIYINGQEVKIKSPINSKKYGIALLTEERRSTGIFPVLTVGDNTIIAGLDKYIDLKFVVNQKRGMKDIKNSIEKLNIRTPSHATQIKNLSGGNQQKVIFSRWLLTEPDVLIMDEPTRGIDVGAKYEIYSIISDLSKMGKSIIMISSEMPELIGMSDRIMIMCDGRLSGIIEGEEATQEEIMKYATRFI
|
Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system.
|
Q896Y2
|
P21866
|
KDPE_ECOLI
|
KDP operon transcriptional regulatory protein KdpE
|
Escherichia
|
MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLRQWSAVPVIVLSARSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATTAPDPLVKFSDVTVDLAARVIHRGEEEVHLTPIEFRLLAVLLNNAGKVLTQRQLLNQVWGPNAVEHSHYLRIYMGHLRQKLEQDPARPRHFITETGIGYRFML
|
Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon.
|
P21866
|
A4FMQ2
|
LEU3_SACEN
|
Beta-IPM dehydrogenase
|
Saccharopolyspora
|
MRLAVIPGDGIGPEVVAEALKVLGEVVPDTEITRYDLGAARWHATGELLPESVLGELRQHDAILLGAVGDPSVPSGILERGLLLRLRFELDHHVNLRPARLYPGVKSPVSDPGEIDMVVVREGTEGPYAGNGGLLRKDTTHEIATEVSINTAFGVERVVRDAFARAASRPRKHLTLVHKTNVLTHAGSLWSRVVEEVSLQHPDVTVAYQHVDATTIHMVTDPSRFDVIVTDNLFGDIITDLAGAITGGIGLAASGNIDATRRNPSMFEPVHGSAPDIAGQGTADPTAAVLSVALLLDHVGQSEAARRVEAAVAFDLATRDHSAPGATFAIGDRLAALVSSREVAQQA
|
Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
|
A4FMQ2
|
A8A0Z3
|
LEUE_ECOHS
|
Leucine efflux protein
|
Escherichia
|
MFAEYGVLNYWTYLVGAIFIVLVPGPNTLFVLKNSVSSGMKGGYLAACGVFIGDAVLMFLAWAGVATLIKTTPILFNIVRYLGAFYLLYLGSKILYATLKGKNSEAKSDEPQYGAIFKRALILSLTNPKAILFYVSFFVQFIDVNAPHTGISFFILAATLELVSFCYLSFLIISGAFVTQYIRTKKKLAKVGNSLIGLMFVGFAARLATLQS
|
Exporter of leucine.
|
A8A0Z3
|
Q2LQ87
|
RPOB_SYNAS
|
Transcriptase subunit beta
|
Syntrophus
|
MGEFRKNFGRIEEILEVPNLIDIQTRSYETFLQEDVAPENRKNFGLQGAFKSVFPISDFSGKCSLEFVSYKIGAVRYDVNECIQKGMTYAAPLKIVVRLVVFDTDRLSDQKNIRDIKEQEIYFGEIPLMTEKGTFIVNGTERVIVSQLHRSPGIFFDHDKGKTLTSGKLIYSARIIPIRGSWLDLEFDSKDLLYVRIDRRRKMPVTILLKAMGYSTEDLLNYFYDVEHIFCEGENFYAAVDESLVGHKLYDDIRDINTGEILFKKGRRINKVILKRIREQRVERIKMDVEELPGRILATDILDPETGEVLFHCNEALSAAGIDVVREKGIRELSVINLGEDLSNVSIRDTLLIDRMETPGDAIIEIYRRLRPSNPPTPDTAQKFFNSLFFENESYDLSTVGRAKMNYKLRLDVSTDVTVLRKEDIMAAVKYLIDLKNGVPECSVDDIDHLGNRRVRSVGELIENQYRIGLVRMERAIKEKMSLQDIETMMPHDLVNVKPVSAVVSEFFGSSQLSQFMDQTNPLSEITHKRRLSALGPGGLTRERAGFEVRDVHPTHYGRICPVETPEGPNIGLIVSLSTYARVNEFGFIETPYRIVKEGRVLPEVKFLTAIEEENQVIAPADQPVNHDGSFKGDLISARKGGDFVNVVPSEVNMVDVSPNQLVSVAATLIPFLEHDDANRALMGSNMQRQAVPLMRPEIPLVGTGMERIVARDSGAVVVAKRSGIVESVDASRIVIKCESAEKTDRDTGVDIYTLIKYQRSNQDTCFNQKAIVNKGQRVRKGDIIADGPATDNGELALGHNVMVAFMSWGGYNYEDSILVSERIVKEDIYTSIHIEEFETMARDTKLGKEDITRDIPNVGEEALRNLDDSGIVRMGVSVKSGDILVGKITPKGETQLSSEEKLLRAIFGEKASDVRDTSLRVPPGVEGTVIDAKVFTRKGAEKDHRSQYIEDEAIAMLQKDREDEIRIITEAVKKEVGTLLQGKQSGAKIVDPKRKKIYLKKGDIITPEILSEIPLHLWKEITVADDEETERAVGQMMANLYDKIEVVEAYFNEKTEKLKASDELPPGVIKMVKVYIAIKRKLQAGDKMAGRHGNKGVLSRILPEEDMPYFKDGRPVDIVLNPLGVPSRMNVGQILETHLGWAAKGLGEKLNDMLDSYQKGNQLRDELKGIYQSREFEKFVDGATEEETYQFVRKLRRGIAVSSPVFDGATESDIRNMLKLANLPSTGQAILYDGRTGEPFDQEITVGMIYMLKLHHLVDNKIHARSIGPYSLVTQQPLGGKAQFGGQRLGEMEVWAMEAYGAAYSLQEFLTVKSDDVAGRTRIYEAIVKGENTSEPGLPESFNVLVKELQSLCLDVELIEEE
|
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
|
Q2LQ87
|
Q7V335
|
GLYA_PROMP
|
Serine hydroxymethyltransferase
|
Prochlorococcus
|
MNILQNLKESDPIISNLINSEKNRQETHLELIASENFASMAVMQAQGSVLTNKYAEGLPQKRYYGGCEFVDEIEELAIERAKQLFDADWANVQPHSGAQANAAVFLSLLKPGDTILGMDLSHGGHLTHGSPVNMSGKWFNAVHYGVDKETNKLNFNEIRDIALATKPKLIICGYSAYPRKIDFESFRRIADEVGAFLMADIAHIAGLVATKLHPNPIPYCDVVTTTTHKTLRGPRGGLILCKDKEFGKKFDKSVFPGTQGGPLEHIIAAKAVAFGEALKPNFVNYSKQVINNAKVLSSTLIKRGIDIVSGGTDNHIVLLDLRSINMTGKVADLLVSEVNITANKNTVPFDPESPFVTSGLRLGTAALTTRGFNDDAFVEVGEIIADRLLNPDDLLTEKKCKERVLTLCNRFPLYEVELEASIK
|
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.
|
Q7V335
|
Q5HX70
|
OBG_CAMJR
|
GTP-binding protein Obg
|
Campylobacter
|
MFIDSVKITLASGDGGKGAVSFRREKHVPLGGPDGGDGGNGGDIIFVCDNNTHTLVNFKGKRELRAQNGAGGMGRNKNGKKGENLELIVPEGTQVIDVQTNEILLDLTKEGQRELFLKGGKGGLGNTHFKHATNQRPDYAQPGIKGESRLVRLELKLIADVGLVGFPNVGKSTLISVVSNAKPEIANYEFTTLTPKLGLVDVDEYNSFVMADIPGIIEGASGGKGLGLAFLKHIERTSFLLFVLDPMRQMPLKEQFIVLRKELEKFSNELFGRKFGIMISKSDSVRLGEEFAEQIALNINELDNYLKEINNPQSFLIKVSSLEKTGLKELKFMLLEEIKTLRNNKKILTI
|
An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control.
|
Q5HX70
|
B2JZ70
|
MUTH_YERPB
|
Methyl-directed mismatch repair protein
|
Yersinia
|
MSVYSLPPAPPSDEHQLFQRAQALSGFTLGELATRAQWVIPADLKRVKGWVGMLLEFYLGASAGSKPEQDFADIGIELKTIPISAQGKPLETTFVCVAPLTGNSGVTWENSHVRHKLARVLWVPVEGERHIPLAERRVGAPLLWSPNVEEEELLRRDWEELMDLIVLGKVESITARHGQVLQLRPKAANSRALTEAIGEFGQPIMTLPRGFYLKKTLTAPMLARHFLL
|
Sequence-specific endonuclease that cleaves unmethylated GATC sequences. It is involved in DNA mismatch repair.
|
B2JZ70
|
Q72ID8
|
ARGR_THET2
|
Arginine repressor
|
Thermus
|
MGNKAERHRAIQEIVRREEIGTQKELVERLRQLGFEVTQATVSRDIAELGLARIALGKGRHRYVLPAADLPENAYEELKRQFGLFVRDVDRGGNLLVVKTAEGHASGIAYLLDRLRRDEIVGTLAGDDTILVVARTEEAAQALEDEFAGLLVEGRALRRALSGS
|
Regulates arginine biosynthesis genes.
|
Q72ID8
|
B5FA81
|
TRUB_ALIFM
|
tRNA-uridine isomerase
|
Aliivibrio
|
MARRRKGRPVNGVILIDKPTGITSNDTLQKVKRIYFAEKAGHTGALDPLATGMLPICLGEATKFSQFLLDSDKRYRVVAKLGERTNTSDSDGEVVQTREVKVDRGQLERCIAKFRGTTDQIPSMFSALKYQGRPLYEYAREGIEVPRESRKITVYSIELLRFEGHEVEMEVHCSKGTYIRTITDDLGEMLGCGAHVTYLRRTGVSNYPYENMVTIEDLEALLEQAHREERAPRELLDPLLMPMDSAVQDLPEVNMIPELADHVLHGQPVQVFGAPQDGIVRMTSGDERLFIGVGHIDDDGRVAPKRLVVFRDEEEK
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
B5FA81
|
A2SSW0
|
RS13_METLZ
|
30S ribosomal protein S13
|
Methanocorpusculum
|
MVEESELKYFVRIINTDLDGTQPVQLALTGIKGIGLHAALIIARRAGVDTRATMGLLGDEDVAAIEEQVKAYPASVPKWMVNRPVDVYSGEPKHLYGSDLSLAKEDDINLMKKMRCYRGIRHENGLKVRGQRTKATGRFGKIVGVSKRRN
|
Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement.
|
A2SSW0
|
Q48KZ1
|
TIG_PSE14
|
PPIase
|
Pseudomonas
|
MQVSVENTSALERRMTIGVPAERIETEVNKRLQQTARKAKIPGFRPGKVPMSVIRQRYEDGARQEALGDLIQATFYEAVVEQKLNPAGAPAVEPKSFEKGKDLEYVATFEVFPEFTVAGFDTIAVERLSADVVDSDLDNMLEVLRKQNVRFEVADRAAQNEDQLNIDFVGKVDGEVFAGGSATATQLVLGSGRMIPGFEDGLVGAKAGEERVLNVTFPEDYQNLELAGKAAEFTVTVNTVSEPKLPELNEEFFKQFGIKETGIEGFRTEVRKNMERELRQAIKSKVKNQVMDGLLAANPIEVPKALLENEVNRLRVQAVQQFGGNIKPDQLPAELFEEQAKRRVELGLIVAEVVKQFDLKPDDARVREMIQEMASAYQEPEQVVAWYYKNEQQMNEVRSVVLEEQVVDTVLQKASVTDKSVSYEEAVKPVEAPKAD
|
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase.
|
Q48KZ1
|
P69589
|
RBL_LUPPI
|
Ribulose bisphosphate carboxylase large chain
|
Lupinus
|
SVGFKAGVKDYKLTYYTPDYETKDTDILAAFRVTPQPGVPPEEAGAAVAAESSTGTWTTVWTDGLTSLDRYKGRCYHIEPVAGEESQFIAYVAYPLDLFEEGSVTNMFTSIVGNVFGFKALRALRLEDLRIPNAYVKTFQGPPHGIQVERDKLNKYGRPLLGCTIKPKLGLSAKNYGRAVYECLRGGLDFTKDDENVNSQPFMRWRDRFLFCAEALYKAQAETGEIKGHYLNATAGTCEEMIKRAVFARELGVPIVMHDYLTGGFTANTSLAHYCRDNGLLLHIHRAMHAVIDRQKNHGMHFRVLAKALRLSGGDHIHSGTVVGKLEGEREITLGFVDLLRDDFVEKDRSRGIYFTQDWVSLPGVLPVASGGIHVWHMPALTEIFGDDSVLQFGGGTLGHPWGNAPGAVANRVALEACVQARNEGRDLASEGNQIIREASKWSPELAAACEVWKE
|
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
|
P69589
|
P47859
|
PFKAP_RABIT
|
Phosphohexokinase
|
Oryctolagus
|
MDNKVSASPRGSYRKFLEHLSGAGKAIGVLTSGGDAQGMNAAVRAVVRMGIYVGAKVYFIYEGYQGMVDGGSNIVEANWESVSSILQVGGTIIGSARSKAFRTREGRLKAACNLIHRGITNLCVIGGSGSLTGANIFRMEWSGLLEELAQDGKIDNEAVQKYAYLNVVGMVGSIDNDFCGTDMTIGTDSACHRIIEVIDAIMTTAQSHQRTFVLEVMGRHCGYLALVSALACGADWVFLPESPPEEGWEEQMCVKLSENRAQKKRLNIIIVAEGAIDTLNRPITSEKIKELVVTQLGYDTRVTILGHVQRGGTPSAFDRILASRMGVEAVLALLEATPETPACVVSLSGNHAVRLPLVECVQMTQEVQKAMDERRFKDAVQLRGRSFENNLNTYKRLAIKLPDDKIQKSNCNVAVINVGAPAAGMNAAVRSAVRVGIADGHKMFAVYDGFDGFAKGQIKEIRWGDVGGWTGQGGSILGTKRILPGKYLEEIATQIRTHNINAILIIGGFEAYLGLLELSAAREKHEEFCVPMVMVPATVSNNVPGSDFSIGADTALNTITDTCDRIKQSASGTKRRVFIIETMGGYCGYLANMGGLAAGADAAYIFEEPFDIRDLQSNVEHLTEKMKTTIQRGLVLRNESCSENYTTDFIYQLYSEEGRGVFDCRKNVLGHMQQGGAPSPFDRNFGTKISARAMQWITTKLKESPGKGKRFVSDDSICVLGISKRNVLFQPVAELKNETDFEHRIPKEQWWLKLRPLMKILAKYKTSYDVSDSGQLVPVRHRGGPEEPAAI
|
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
|
P47859
|
Q5LYH7
|
Y1598_STRT1
|
Nucleoid-associated protein str1598
|
Streptococcus
|
MMNMQNMMKQAQKLQKQMEKSQAELAATTFTGKSAQDLVVAELTGDKKVVNITFADAVVDPDDVETLQDMTVQALNDALGQIDEATKKSMGAFAGKLPF
|
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
|
Q5LYH7
|
B1KIW2
|
FETP_SHEWM
|
Probable Fe(2+)-trafficking protein
|
Shewanella
|
MARTVNCVYLKKEAEGLGFQLYPGPLGKRIFDNVSKEAWGLWQAKQTMLINEKKLNMMNVEDRGFLETQMVNFLFEGKDVEIEGYVPQKDDD
|
Could be a mediator in iron transactions between iron acquisition and iron-requiring processes, such as synthesis and/or repair of Fe-S clusters in biosynthetic enzymes.
|
B1KIW2
|
A4Y493
|
G6PI_SHEPC
| null |
Shewanella
|
MTLLTQSSTWQALSAHTQNLPHMRELFATDAARFKNMSLSACGLFLDYSKNRATAETLELLFSLAKDSQLEAKIKAMFAGEIINTTEKRAVLHTALRSKASQSIIAEGQDIVLEVQQTLSKMQEFVETVTSGQWKGYTGKAITDIVSIGIGGSFLGPKVVSQALRPYWNQGLNCHFVANVDGTSISEKLKLLDSETTLFIMSSKSFGTQETLTNTLTAKAWFLAKGGLQSDVAKHFVAVTSNVTKATEFGIDANNIFPMWDWVGGRYSLWSAIGLPIALLVGMDNFRALLNGAHQMDEHFASAPLAENMPVIMGLLSLWYGNFFNAQSHVVLTYDHYLRGLPAYFQQLDMESNGKSVTLDGTDVDYSTGPVIWGGEGTNGQHAYHQLIHQGTALIPADFIMPLQSHNPIGVHHDQLASNCFGQTQALMQGRTFEEALAELANSSLTDEEKQLIAKHKVMPGNKPSNTLLMNKLTPETLGALIALYEHRTFVQGAIWDINSFDQWGVELGKNLGNDVLARISAEQDSSALDASSNGLINLYRQGAI
|
Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate.
|
A4Y493
|
A8Z5Q4
|
MNMG_SULMW
|
Glucose-inhibited division protein A
|
Candidatus Sulcia
|
MFVKQYDVIVVGGGHSGSEAALAASNLGSNTLLITTNLYNIGQMSCNPAMGGIAKGQMIKEIDALGGYSGIITDKSMIQFRMLNKSKGPAMWSPRAQCDRLKFSKEWRLTLEKKKNLSFFQSTVVDLIIKNYKVIGVKTILGIYIKSKSVILTNGTFLNGIIHIGDKKNSGGRISENSVKGLTEKLKKIGFFSGRMKTGTSPRLDGRSLDFSKMIEQLGDFPIEPFSYLSNLNILKQKKCYITHTNLETHNLLSKEFNRSPIFNGKIKCVGPRYCPSIEEKVYRFSNKENHQIFVEPEGVNTIEVYINGFSTSMPEEVQYKALLTIPGFEHAKMVRPGYAIEYDYFPPTQLKNNLETKLIENLFFAGQINGTTGYEEAAAQGLIAGINANLKINEKDPFILKRNEAYIGVLIDDLIYKGTEEPYRMFTSRAEYRILLRQDNADERLTHMGINLGLVSYDRIKKLKNKNKNKKQCFLFFKINKANNLILKENIKICDLLSRPEISIYDIIKLSLIKNFIKKNNIDKKILEQISLYIKYKGYLLKEEENVKKMYRLETIRIPNDFDYNQVKSISIEAREKLLNYKPNSIGEASRISGVSPSDIRILILFLIKK
|
NAD-binding protein involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
|
A8Z5Q4
|
A4TBJ9
|
LIPB_MYCGI
|
Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase
|
Mycolicibacterium
|
MSSVEGMAQSIRSGTEPVRVQWLGRIDYQAAWDLQRELAEERIAGGPDSLLLLEHPEVYTAGRRTLAHERPVDGTPVIDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVNFVRRLEESLISVCASFGVQTGRVEGRSGVWVAGDGGRPDRKIAAIGIRVARATTLHGFAINCDCDLGAFGSIVPCGIADAGVTSLTAELGRTVGVAEVIDRVSEAVLDALDGRIALGVASSPGVDSAQ
|
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.
|
A4TBJ9
|
Q138Z3
|
BIOB_RHOPS
|
Biotin synthase
|
Rhodopseudomonas
|
MNSIDLPSLAQALADSTPTIRHNWTREEAAAIYHAPFADLIFRAQTIHRQSFDANAVQCNQLLNVKTGGCAEDCGYCSQSSHHDTALPASKLMDPAKVIEGAKAARDAGATRYCMGAAWRSPKDRDMAPVIEMVKGVKALGMEACMTLGMLTDDQAKQLADAGLDYYNHNIDTSEEFYSSVVKTRSFGDRLETLEKVQDAGIKVCCGGILGLGEKPTDRVEMLRTLANLPQHPESVPINMLIPIEGTPIAATATPVDPFEFVRTIALARIMMPKSDVRLAAGRTAMSDEMQALCFLAGANSIFIGDTLLTTPNPGDSKDRALFARLGITPRDDLGVHAHGNA
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
Q138Z3
|
O33807
|
BLC4_SALTM
|
Cefotaximase 4
|
Salmonella
|
MMTQSIRRSMLTVMATLPLLFSSATLHAQANSVQQQLEALEKSSGGRLGVAQINTADNSQILYVADERFAMCSTSKVMAAAAVLKQSESDKHLLNQRVEIRASDLVNYNPIAEKHVNGTMTLAELGAGALQYSDNTAMNKLIAHLGGPDKVTAFARSLGDETFRLDRTEPTLNSAIPGDPRDTTTPLAMAQTLKNLTLGKALAETQRAQLVTWLKGNTTGSASIRAGMPKSWGVGDKTGSGDYGTTNDIAVIWPENHAPLVLVTYFTQPEQKAESRRDILAAAAKIVTHGF
|
Has cefotaxime-hydrolyzing activity.
|
O33807
|
B2VK57
|
RL16_ERWT9
|
50S ribosomal protein L16
|
Erwinia
|
MLQPKRTKFRKVHKGRNRGLAQGTDVSFGTFGLKAVGRGRLTARQIEAARRAMTRAVKRQGKIWIRVFPDKPITEKPLEVRMGKGKGNVEYWVALIQPGKVLYEMDGVPEELAREAFKLAAAKLPIKTTFVTKTVM
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
B2VK57
|
C6DHS8
|
NUDC_PECCP
|
NADH pyrophosphatase
|
Pectobacterium
|
MEQTLKGDETGWWVVSDAVQIWLPQGELPCGTATKWSLQGKTARQIGEWQEQPVWLVCQGRDTDMASVRQLLDQDVGLFQLAGRGVQLAEFYRSHRFCGYCGHEMVRSKTELACLCHHCKERYYPQIAPCIIVAIRRGEEILLAQHNRHRGNMYTVLAGFVEVGETLEQTVVREVMEESQVQIKNLRYVSSQPWPFPHSLMMAFMAEYAGGEIKHDPKELRDAGWFRYDQLPQLPPPGTVARRLIEDTVVLCRAYHENEG
|
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some mRNAs and stabilizes RNA against 5'-processing. Has preference for mRNAs with a 5'-end purine. Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates.
|
C6DHS8
|
B5FBS8
|
FRDD_ALIFM
|
Quinol-fumarate reductase subunit D
|
Aliivibrio
|
MVNRNPKRSDEPVWWGLFGAGGTWFAMLTPVTILVLGILVPLGVIGPESMNYLRVAGFVTSIIGALFVIGSISMPMWHAMHRLHHGMHDLKFHTGTAGKIACYAAAALATVLSVVFIFMI
|
Anchors the catalytic components of the fumarate reductase complex to the cell membrane, binds quinones.
|
B5FBS8
|
A6LUQ4
|
BIOB_CLOB8
|
Biotin synthase
|
Clostridium
|
MEKLAEEIINGRRLTRSDDLEFLLTCDLKKICDGANKIRKTLCGESVDLCTIINGRSGKCSENCKFCAQSNHHKTEIKKYDFLDPNVILKDCKKNEANGVHRYSIVTAGRALVGSDFDKAVQAYKMMNKECSINLCASHGFLSEEQFVLLKEAGVTMYHANIETSKRNFHNICTTHSYDDKIKEIKLAQNAGLKVCSGGIIGMGETWYDRIDMAISLSELGVISIPINVLMPIKGTPLENLKRISNYDILRTIAIFRYINPTAYIRMAAGRTYFEDGGIEIFQSGSNATITGDMLTTVGNNTCQDKIMLQTLGFSI
|
Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism.
|
A6LUQ4
|
B7IHV5
|
RS17_THEAB
|
30S ribosomal protein S17
|
Thermosipho
|
MPKKKLIGEVVSDKMDKTVVVAVSTLVKHPRVGKYIKRTKKYYAHDENNECRDGDIVEIIESRPLSKLKRWRVLRIVERSVFADETLDEELEGGSSDDN
|
One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA.
|
B7IHV5
|
Q32DZ9
|
MACB_SHIDS
|
Macrolide export ATP-binding/permease protein MacB
|
Shigella
|
MTPLLELKDIRRSYPAGDEQVEVLKGITLDIYAGEMVAIVGASGSGKSTLMNILGCLDKATSGTYRVAGQDVATLDADALAQLHREHFGFIFQRYHLLSHLTAEQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRTEYYPAQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAIDKVNVAGGTEPVVNTVSGWRQFVSGFNEALTMAWRALAANKMRTLLTMLGIIIGIASVVSIVVVGDAAKQMVLADIRSIGTNTIDVYPGKDFGDDDPQYQQALKYDDLIAIQKQPWVASATPAVSQNLRLRYNNVDVAASANGVSGDYFNVYGMTFSEGNTFNQEQLNGRAQVVVLDSNIRRQLFPHKADVVGEVILVGNMPARVIGVAEEKQSMLGSSKVLRVWLPYSTMSGRVMGQSWLNSITVRVKEGFDSAEAEQQLTRLLSLRHGKKDFFTWNMDGVLKTVEKTTRTLQLFLTLVAVISLVVGGIGVMNIMLVSVTERTSANDIPMDVGAGASYVLYHLFFRYPCKVLPAVGGALGITLSLLIAFTLQLFLPGWEIGFSPLALLLAFLCSTVTGILFGWLPARNAARLDPVDVLARE
|
Part of the tripartite efflux system MacAB-TolC. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.
|
Q32DZ9
|
A8MLJ8
|
DNLJ_ALKOO
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Alkaliphilus
|
MGSMERLRQLVDILNEYSYQYYVLDEPVVSDKEYDQLYDELVLLEKELNTVLEDSPTIRVGGDVLKNFKAHNHLAPLWSLDKCKTPEELISWDLRVRRLLEGSGVPIEYVMEYKFDGLTLNLTYNNGQLVQAATRGNGTTGEGILEQVKTIKTIPLTIPHKGRIEVQGEGLMGLSVLAAYNKTALEPLKNPRNAAAGALRNLDPKVTAKRKLSAFCYNVGFYEGIDFNTHMEILAFLKANKFPVSNYTKKFHTIHQVIEEIETIGEQVKSLDFLTDGLVIKVNHMEARRLLGYTQKFPRWAMAFKFEAEEMTTELKDVIWQVGRTGKLTPAAVLEPIDIGGVTVSRATLNNWEDIQRKKVKIGCRVWIRRSNDVIPEIMGSIEETLEGAMDIEKPQHCPACHSEVVERGAHIFCPNSLSCKPQLVSRIVHYASRDAMDIVGFSEKTAEQLFEELNLRDLADLYEIKYEDLIKLPRFGDKKARNLLEAIENSKNCKLDSFVYALGIPNVGRKTATDLAKHYKSFQAIQEAEFQELITLPDVGDIVAQSIIDFFEDEEIKKSVNRLINEGIRPLFKEVEQQENIFLGKTVVVTGTLEKYGRKEIKELLEKLGAKVTGSVSKNTDFLLAGEAAGSKLEKAMEIIASGVETSLRIISEAEFEAML
|
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.
|
A8MLJ8
|
Q28WQ1
|
KIF1A_DROPS
|
Kinesin-like protein unc-104
|
Sophophora
|
MSSVKVAVRVRPFNSREIGRESKCIIEMTGATTAITNPKVPPNTSEAVKRFNFDYSYWSHDPRDSDFSTQTMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICQDLFTRIHDTETDELKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDTMTDLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKHNKKADFIPYRDSALTWLLRENLGGNSKTAMIAAISPADINYDETLSTLRYADRAKQIVCKAVVNEDANAKLIRELKEEIQKLRDLLKAEGIEVQEEDELNKSTTGIKSPSKSRNRNGSTTEMAVDQLQASEKLIAELNETWEEKLKRTEEIRLQREAVFAEMGVAVKEDGITVGVFSPKKTPHLVNLNEDPNLSECLLYYIKDGLTRLGTHEANVPQDIQLSGSHILKEHCTFENRNSTVTLLPHKDAIIFVNGRQLVEPEVLKTGSRVILGKNHVFRFTNPEQARELREKITENEAENEVEKADAPQVDWNFAQCELLEKQGIDLKAEMKKRLDNLEEQYKREKMQADQQFEEQRKTYEARIDALQKQVEEQSMTMSMYSSYSPEDFHQEEDVYNNPMYESCWTAREAGLAAWAFRKWRYHQFTSLRDDLWGNAIFLKEANAISVELKKKVQFQFTLLTDTLYSPLPPELASSVAPLQQEDEFGAPPVSKTLVAVEVTDTKNGATHYWSLEKLRQRLELMREMYHNEAEMSPTSPDYNVESLTGGDPFYDRFPWFRMVGRSFIYLSNLLYPVPLVHKVAIVNERGDVRGYLRIAVQPVLDEESIDFNNGVKQSARLVFNEDDAKPKYRALNEKDDVQRYIDNGGHDSKLEELEDVDSGRGIDSNSASDCPENAEEPGEHLQVGKEFTFRVTVLQATGIGAEYADIFCQFNFLHRHEEAFSTEPVKNSASGAPLGFYHVQNITVPVTKSFIEYLKTQPIMFKIFGHYQTHPLHKDAKQDFVSRPPPRRMLPPSIPISQPVRSPKFGPLPCPPSSTVLAKHDVLVWFEICELAPNGEYVPSVVEHSDDLPCRGLFLLHQGIQRRIRITIVHEPTPEVKWKDINELVVGRIRNTPESSDEQDEDACVLSLGLFPGEVLDVPGDDRSFYRFEAAWDSSLHNSALLNRVSQGGETIYITLSAYLELENCARPAIVTKDLSMVIYGRDARTGPRSLKHLFSGQYRNPEANRLSGVYELSLRRASEAGSPGVQRRQRRVLDTSSTYVRGEENLHGWRPRGDSLIFDHQWELEKLTRLEEVGRMRHLLLLRERLGMDTNPNPTTKTEKDVCNLAARAATSPVHMVIPQSPQTPVKDPQQIMPEREYNQREQDLMLKCLKLVQAGRYAKNEANDTQTQSDVSPSDEGCADMTVSCISSNSMEDNKFVIRRRLCSPDRADAPNGWEAPAPATQPALPLRLYVPELEEIRVSPVVARKGLLNVLEHGGSGWKKRWVTVRRPYVFIYRSEKDPVERAVLNLATAQVECSEDQAAMVKIPNTFSVVTKHRGYLLQTLGDKEVHDWLYAINPLLAGQIKSRLARRTLEPASQTASQIQASSAANANSANK
|
Required for presynaptic maturation, has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors, components required for the morphological transformation of axonal growth cones to mature boutons.
|
Q28WQ1
|
Q5X112
|
GLMU_LEGPA
|
Glucosamine-1-phosphate N-acetyltransferase
|
Legionella
|
MNLQIIILAAGQGKRMYSDTPKVLHHLAGKPLLTHVVETAQQLNPDAIHVIYGHGGEQIKSSLPNLPVHWVHQAEQLGTGHAVLQAMPHIPDDAYVLVLSADVPLIQVGTLQSLIECSQRQNPDHSVLALLVAELENPSGLGRIIRNNQGEIYSIVEEKDANEQVKNIKEIYSGVCCTLANNLKKWLPQLSNSNAQGEYYLTEIISLAVQNKTPITSLTAKNSFEVQGINNRQQLQQLERTWQQRAANQLMEKGATLADANRFDLRGELYCGKDVYIDINCIFTGKVVLGNGCKIGPNCSLTNVTLGDGCEVYANSVLEGCHIANDCHIGPFARLRSGTQLASHCKIGNFVETKKAIFDEGTKASHLSYLGDVLLGKNVNVGAGTITCNYDGVNKHQTIIEDGVFIGSDTQLVAPVTVGANATIGAGSTIRRNVPPDELTLTESRQKTIYGWKRPVKRERD
|
Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain.
|
Q5X112
|
C5CDH9
|
RL21_KOSOT
|
50S ribosomal protein L21
|
Kosmotoga
|
MYAIIEASGKQYKVEEGITLFTEKLKDFAEGDQVVFDRVLLLKDDSGVKVGKPYLENVKIVGKVVRHGRGKKIRVVKFRPRKNYHRVKGHKQWFSEVLIEKIEY
|
This protein binds to 23S rRNA in the presence of protein L20.
|
C5CDH9
|
P33749
|
MSN4_YEAST
|
Multicopy suppressor of SNF1 protein 4
|
Saccharomyces
|
MLVFGPNSSFVRHANKKQEDSSIMNEPNGLMDPVLSTTNVSATSSNDNSANNSISSPEYTFGQFSMDSPHRTDATNTPILTATTNTTANNSLMNLKDTASLATNWKWKNSNNAQFVNDGEKQSSNANGKKNGGDKIYSSVATPQALNDELKNLEQLEKVFSPMNPINDSHFNENIELSPHQHATSPKTNLLEAEPSIYSNLFLDARLPNNANSTTGLNDNDYNLDDTNNDNTNSMQSILEDFVSSEEALKFMPDAGRDARRYSEVVTSSFPSMTDSRNSISHSIEFWNLNHKNSSNSKPTQQIIPEGTATTERRGSTISPTTTINNSNPNFKLLDHDVSQALSGYSMDFSKDSGITKPKSISSSLNRISHSSSTTRQQRASLPLIHDIESFANDSVMANPLSDSASFLSEENEDDAFGALNYNSLDATTMSAFDNNVDPFNILKSSPAQDQQFIKPSMMLSDNASAAAKLATSGVDNITPTPAFQRRSYDISMNSSFKILPTSQAHHAAQHHQQQPTKQATVSPNTRRRKSSSVTLSPTISHNNNNGKVPVQPRKRKSITTIDPNNYDKNKPFKCKDCEKAFRRSEHLKRHIRSVHSTERPFACMFCEKKFSRSDNLSQHLKTHKKHGDF
|
Positive transcriptional factor that acts as a component of the stress responsive system. Recognizes and binds to the stress response element (STRE) which is involved in the response to various forms of stress (heat, oxidative, osmotic, etc.). Involved in the regulation of the CTT1, DDR2, HSP12 genes.
|
P33749
|
Q9XI47
|
SHH1_ARATH
|
DNA-binding transcription factor 1
|
Arabidopsis
|
MAASDDSSHYFTEFTLSEIVDMENLYKELGDQSLHKDFCQTVASTFSCSVNRNGKSSITWKQVQIWFQEKLKHQSQPKSKTLPSPPLQIHDLSNPSSYASNASNATFVGNSTFVQTRKGKASDLADLAFEAKSARDYAWYDVSSFLTYRVLRTGELEVRVRFSGFDNRHDEWVNVKTSVRERSIPVEPSECGRVNVGDLLLCFQEREDQALYCDGHVLNIKRGIHDHARCNCVFLVRYELDNTEESLGLERICRRPEE
|
Involved in RNA-directed DNA methylation (RdDM). Required for the silencing of some endogenous RdDM targets and accumulation of 24-nt siRNAs, but not for the production of Pol V-dependent transcripts. Functions in transcriptional silencing through both DNA methylation-dependent and -independent pathways. Required for both maintenance and de-novo DNA methylation. Plays a role in the recruitment of Pol IV to genomic regions associated with K9 methylated histone H3 that are targets for RdDM.
|
Q9XI47
|
P24586
|
KPST5_ECOLX
|
Polysialic acid transport ATP-binding protein KpsT
|
Escherichia
|
MIKIENLTKSYRTPTGRHYVFKDLNIEIPSGKSVAFIGRNGAGKSTLLRMIGGIDRPDSGKIITNKTISWPVGLAGGFQGSLTGRENVKFVARLYAKQEELKEKIEFVEEFAELGKYFDMPIKTYSSGMRSRLGFGLSMAFKFDYYIVDEVTAVGDARFKEKCAQLFKERHKESSFLMVSHSLNSLKEFCDVAIVFKNSYIIGYYENVQSGIDEYKMYQDLDIE
|
Putative ATP-binding protein, and an energy coupling component for the transport of polysialic acid across the cytoplasmic membrane.
|
P24586
|
Q5L6H0
|
TPIS_CHLAB
|
Triose-phosphate isomerase
|
Chlamydia
|
MERKRYIFGNWKMHKTAKEAKDYLSVFCPLLEEVAPVSCVGITPAFTALHACCESIKFFHSPLWLGAQNVHQDTSGAFTGEISLPMLKEFDVNFVLLGHSECRHIFHEEDTTIALKVGAAAREGIIPVLCIGETLEVREKGATEAMLSNQLMLGLAQLPETASVIIAYEPVWAIGTGKVASAVDVQEAHAFCREVLANIFSKEKAEEISILYGGSVKADNAEGFARCPDVDGLLVGGASLDPKVFADVVANFHR
|
Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P).
|
Q5L6H0
|
B9K7B8
|
MUTL_THENN
|
DNA mismatch repair protein MutL
|
Thermotoga
|
MRIRRLPESLIRKIAAGEVIHNPSFVVKELVENSLDAQANRVVVEVENGGKNLVRVSDNGTGMTKEEVLVAIEPHTTSKIESEEDLRRIRTYGFRGEALASIVQVSRTRIVTKTKEDALATQVLITGGKVEEISETHRDTGTTVEVKDLFFNLPVRRKSLKSSSIELRMCREMFERFALVKNNVDFTFISDGKIIHSFPATSDLFERALLILEDLRKGYITFEEELSDLKIKGIVSAREITRPNRTGEYFYVNERFVISEELHEVLMKVYDLPKRRYPIAVLFIETDPEKLDINIHPSKIVVRFLEEEKVKEALEEVLTKNLARKWYRSVTYEEISSRALSVAEPSSYRWFLVKKKYAVVETEDALFFIDLHALHERVIYEEILAKRVWRSKNLKRRVITSLPDEKLEKLEKLGFSFQFEGESLVVRKVPEFLTEDAVEEFFKEIIHGSTEMLREKIALAACKLATRSGEFDEKTASKLVDLYFQKKYERCPHGRPVSFRISYEDLDRFFER
|
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
|
B9K7B8
|
C1L082
|
SYS_LISMC
|
Seryl-tRNA(Ser/Sec) synthetase
|
Listeria
|
MLDVKLLRNNFDEVKQKLQNRGEDLGEFEKFGELDKRRRTLIVETEALKSQRNEVSQEIAKLKREKQDADAKIEEMRVVGDRIKTLDIELREIDEKLDMILMSIPNIPHESTPVGESEDDNVEIRKWGEVREFDFEPKAHWDLGTDLDILDFENAAKVTGSRFVFYKKLGARLERALINFMMDLHSNEHGYEEMLPPYMVNRASMTGTGQLPKFEEDAFLIEAEDYFLIPTAEVPVTNYHREDILKAEDLPRKYTAFSACFRSEAGSAGRDTRGLIRQHQFNKVELVQFVKPEDSYAALEKLTGNAEEVLRRLELPYRVLSMCTADLGFTAAKKYDLEVWIPSYNSYREISSCSNFESFQARRANIRFRREPGSKPEYVHTLNGSGLALGRTVAAILENYQDADGSVRIPKVLQGYMGGIEKIELPK
|
Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
|
C1L082
|
P19959
|
3S12_AIPLA
|
Short neurotoxin B
|
Aipysurus
|
MKTLLLTLVVVTIVCLDLGYTLTCCNQQSSQPKTTTDCADNSCYKMTWRDHRGTRIERGCGCPQVKPGIKLECCKTNECNN
|
Binds to muscle nicotinic acetylcholine receptor (nAChR) and inhibit acetylcholine from binding to the receptor, thereby impairing neuromuscular transmission.
|
P19959
|
B8D0S4
|
CYSC_HALOH
|
Adenosine-5'-phosphosulfate kinase
|
Halothermothrix
|
MRNQKGVTVWFTGLSGAGKTTVAREVERQLKEKGYYVQRLDGDIVRQHLTRDLGFTKEDRDENIRRNSFVAKLLTQNDIITLCSFISPYRKARQTAREIIGEFIEVYVNAPLEVCEDRDVKGLYAKARAGEIDNFTGISDPYEPPQNPDLELRTDKETVEESASKVIEYLEEKGYINLPEDVLAG
|
Catalyzes the synthesis of activated sulfate.
|
B8D0S4
|
P36499
|
LAN4_LACLL
|
Lactococcin-DR
|
Lactococcus
|
MKEQNSFNLLQEVTESELDLILGAKGGSGVIHTISHECNMNSWQFVFTCCS
|
Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Lacticin 481 is a broad spectrum bacteriocin exhibiting activity against a wide range of lactic acid bacteria and C.tyrobutyricum.
|
P36499
|
Q2KD47
|
DAPE_RHIEC
|
N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
|
Rhizobium
|
MTATDPVANLQTLIRCPSVTPAEGGALTALDAMLTPLGFTVDRVTAREEGTAAIENLYARLGRDGPHLMFAGHTDVVPVGDEAAWTHPPFAAEISNGELFGRGAVDMKGGIACFVAAVARHIEKSGPPAGSISFLVTGDEEGPAINGTIKLLQWAAERGERWDACLVGEPTNPDRLGDMIKIGRRGSLSGKITVHGVQGHAAYPHLADNPVRGLLQLTQALMDPPFDGGTDDFQPSNLEVTTVDVGNPATNVIPAKASASFNIRFNDSWTVETLRAEILRRLEAAAGNGQLRPGRPPAKYDIVWADRPSHVFLTRNNALIASLSSAIESVAGRSPALSTTGGTSDARFIKDYCPVVEFGLVGQTMHMVDERVAVADLETLTAIYQTFIDRWFAHAGS
|
Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls.
|
Q2KD47
|
Q8MBQ3
|
ATPB_IPOQU
|
F-ATPase subunit beta
|
Ipomoea
|
MRINPTTSGSEVSAVEKKNLGRIVKIIGPVLDVAFPPGKMPNIYNALVVQGRDNEQTNVTCEVQQLLGNNRVRAVAMSDTDGLMRGMEVIDTGAPISVPVGGSTLGRIFNVLGQPVDNLGPVDTNTTSPIHRSAPAFIQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYLEMKESGVINEENIPESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQPRIVGEEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEATAKAMNLKT
|
Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
|
Q8MBQ3
|
Q4X1D2
|
EIF3L_ASPFU
|
Eukaryotic translation initiation factor 3 subunit L
|
Aspergillus subgen. Fumigati
|
MSYEERVNAHPNLGDESDVEEEALVNDYREQVNFDDGMSELDRTTSLGTGSQTQDLQAQLAAAATPLEYQATLETKFASYDNYCSLFHYILNSEGPVELEVPSYYWAWDVIDEFIYQFESFCRYRNRVARSGSNEEEAQLLRENPNTWGCYSVLNVLYSLIQKSQINEQLAAIKRGEDPLAFAGEYGSRPLYKMLGYFSIIGLLRVHCLLGDFSLALKTLDDIEMNKKAMFARVMAAHFTTYYYVGFSYMMMRRYGDAIRMFSHILVYVSRTKNFQKGGNSYDAIAKKNDQMYALIAICVALHPTRLDDTIHSALREKYGEQLLRLQHGGPDALPLFEELFRSACPKFISPTPPDFDNPALNIDPVDHHTAIFMDEVKNTLYNPTIRSYLKLYTTMDLKKLAGFLEVQPEVLRSWLLVNKQRSRQVRWVEGGLLEGEVVSANDLDYALENDLIHVSETKAGRRLVDWYLRNLARVY
|
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
|
Q4X1D2
|
Q5WBF8
|
PXPA_ALKCK
|
5-oxoprolinase (ATP-hydrolyzing) subunit A
|
Alkalihalobacillus
|
MNAIDLNSDVGESYGAYTIGNDEKIMPYISSANIACGFHAGDAHVMRETVARALEHSVAIGAHPGLPDIGGFGRRNIDISPQEGYELVVYQIGALWAIAKAQGGKLHHVKPHGALYNMAAADQALAEAIANAVYDVDPNLVFYGLAGSALIAAGKKAGLKTASEVFADRTYQADGSLTSRRAPNALITDAKEASAQVLRMIQEGKVRTQQGTDVKIDAQTVCIHGDGAQAVAFAEQLKGELERHGITVKAGNC
|
Catalyzes the cleavage of 5-oxoproline to form L-glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate.
|
Q5WBF8
|
A4IM26
|
LSPA_GEOTN
|
Signal peptidase II
|
Geobacillus
|
MGGFRAVIYYLLAAAVIALDQWTKWLVVRYMQLGESIPMIDNVLYITSHRNRGAAWGMLQGQFWLFYLVTVIVVAGIIIYIRRLRPSERLAGIGLGLMLGGAIGNFIDRVFRKEVVDFIHTYIGTYSFPVFNIADSALTVGVILLFIHMFFFATPEKGNE
|
This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
|
A4IM26
|
A0QF47
|
MURE_MYCA1
|
UDP-N-acetylmuramyl-tripeptide synthetase
|
Mycobacterium avium complex (MAC)
|
MVSVPTGLRPSAVPGVRLPALADQVGAVMAGPDRRAAVPDVTVTGVTLRAQDVLPGDLFAALPGATTHGARHAAEAIERGAVAVLTDAAGVAQLTGGRTTPTLLHPRPRSVLGELAAAVYAHPSERLTVIGITGTSGKTTTTYLVESGLRAAGRTAGLIGTVGIRIDGADIPSALTTPEAPALQALLAAMAEQRVDTVVMEVSSHALALGRVDGTRFAVGGFTNLSRDHLDFHPTMADYFEAKALLFDPNSPLRAHRAVVCIDDEAGREMAARAGDAVTVSAEGQPAHWRAVEVAPLGTGGQQFTVIDPAGVQHRAGIRLPGHYNVANCLVALALLDAVGVSPEQAAPGLLQTRVPGRMEEIDAGQDFLALVDYAHKPGALRAVLSSLKRPDRRLAVVFGAGGERDPGKRAPMGATAAELADLVVVTDDNPRGEDPAAIRREILAGATESGCAAEVIEIGDRRAAIRHAVAWAGPGDVVLVAGKGHETGQRTGEHTRPFDDRVELAEALREAVGPRKAQG
|
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.
|
A0QF47
|
C5BCN2
|
END4_EDWI9
|
Endonuclease IV
|
Edwardsiella
|
MKYIGAHVSAAGGLDQAPARAHALEATAFALFTKNQRQWKAAPLTDDAIDAFRAACTRYGYQSQQILPHDSYLINLGHPVTEALEKSRGAFIDEMQRCADLGLTLLNFHPGSHLLQIDERDCLSRIAESINLALSQTQGVCAVIENTAGQGSNLGFRFEQLAAIIEQVEDKSRVGVCIDTCHAFAAGYDLRDEAACGETFAQFSRTVGFSYLRGMHLNDAKSAFNSRVDRHQSLGEGNIGDAAFRWIMRDPRFDGIPLILETTDPGRWQDEIAWLKAQQTAE
|
Endonuclease IV plays a role in DNA repair. It cleaves phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating a 3'-hydroxyl group and a 5'-terminal sugar phosphate.
|
C5BCN2
|
Q88MG4
|
ACCA_PSEPK
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Pseudomonas
|
MNPNFLDFEQPIADLQAKIEGLRLVGNDNSLNISDEIARLQDKSNTLTESIFGNLTSWQIARLARHPRRPYTLDYLEHIFTEFEELHGDRHFSDDAAIVGGTARLDGKPVMVIGHQKGREVREKVRRNFGMPRPEGYRKACRLMEMAERFKMPILTFIDTPGAYPGIDAEERNQSEAIAWNLRVMARLKTPIIATVIGEGGSGGALAIGVCDQLNMLQYSTYSVISPEGCASILWKTADKAADAAEAMGITAERLKSLNIVDKVIQEPLGGAHRDPAKMSESIRADLVQQLDMLGKFDNDALLARRYERLMSYGL
|
Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA.
|
Q88MG4
|
A9KBT1
|
YIDC_COXBN
|
Membrane protein YidC
|
Coxiella
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MDIKRIILYVIVALLAIALFNAWQRDYPPTPKPTPTVEQPTANGDHPTAYTPPAFTPGAAEKTKKAGTIALTSKVPEARLITVRTDVLDVEIDTQGGNIVSAKLPKYPVSLEEKQTPVQILSGEPNELYVAQSGLTNGNGQPTTVQFESAKKQYVLENGQNQLIVQLTGRAPDGLLVTKTYTFHRDDYAIHLAYQVKNNTSKPWQGSLYTQITRRQPPTEHHHFYVRSYNGASMGSPQTPYEKLSYESLDKQNIDRTSQSGWIAMQQHYFLSAWVPGNPELTYHYYSHVIPASGEPNVYVVGFVSPQMNVAAGSEAATHATLYVGPEIAKRLKGLAPGLERTIDYGWLWPISMLLFWILSSVHAVVKNWGWSIIITTILIKIVFYWFSAKSFRSMARMREMQPRIQALKERHGDDRQALSRATMELYRKEKINPLGGCLPMLIQVPVFIAFYYVIIESVQLRQAPFIFWIHDLSVKDPYYILPIIMGLSMLAQQWLSPTSPDPTQQKMMWILPVIFTVFFINFPAGLVLYWITNNVVQTLQQWYVNKTYESHKAKLKARRARKRKR
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Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins.
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A9KBT1
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