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
|
|---|---|---|---|---|---|---|
O54239
|
FLIF_RHIME
|
Flagellar M-ring protein
|
Sinorhizobium
|
MNLFDQFSTFTKNLSNLGQGKLIALAVAGVVAIGFVLGAGIYVNRPSFETLYVGLERSDVTQISIALAEANVDFEVGTDGGSIQVPVGMTGKARLLLAERGLPSSANAGYELFDNVGSLGLTSFMQEVTRVRALEGEIARTIQQISGIAAARVHIVMPERGSFRKAEQTPTASVMIRASATVGRSAASSIRHLVASSVPGLDVDDVTVLDSTGQLLASGDDPSNSALNQSLGVVQNVQSDLEKKIDNALAPFLGMDNFRTSVTARLNTDAQQIQETVFDPESRVERSTRVIKEEQKSSQQQPDNAATVQQNVPQAAPRGGAGQQSSDEAEKKEEQTNYEINSKTIATVKNSYSIERLSIAVVVNRGRLAAMAGEPADQAKIDAYLQEMQKIVSSAAGIDPGRGDVVTLNAMDFVETQLLDQAVPGPGIMEMLTRNLGGIINALAFVAVAFLVVWFGMRPLARQLGFGGQAGKLEGEAAGLELPDFSPAGAGAGGALMEGFGSDFGFDGGDDLLNLGDEAGFNRRVKEGPERRLARMVEISEERAAKILRKWAVDRAA
|
The M ring may be actively involved in energy transduction.
|
O54239
|
A7MMK4
|
MLIC_CROS8
|
Membrane-bound lysozyme inhibitor of C-type lysozyme
|
Cronobacter
|
MKKLLVVLLPTLLAGCSYYDAMVERMNTDTLEYRCDEKPLTVSLNKQREQVSFVLDDKMLHLNQGRAASGTRYTDGIYAFWSKGDEATVYHRDNIVLNHCQLQNPKR
|
Specifically inhibits C-type lysozymes.
|
A7MMK4
|
Q9XFM6
|
MSBP1_ARATH
|
Membrane-associated progesterone-binding protein 5
|
Arabidopsis
|
MALELWQTLKEAIHAYTGLSPVVFFTALALAFAIYQVISGWFASPFDDVNRHQRARSLAQEEEPPIPQPVQVGEITEEELKQYDGSDPQKPLLMAIKHQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEEKDLTWDVSGLGPFELDALQDWEYKFMSKYAKVGTVKVAGSEPETASVSEPTENVEQDAHVTTTPGKTVVDKSDDAPAETVLKKEE
|
MSBP1 can bind to multiple steroid compounds with different affinities. Negatively regulates cell elongation and brassinosteroid signaling. May act as a coreceptor with BAK1 and enhances its endocytosis.
|
Q9XFM6
|
C6E4N1
|
RS4_GEOSM
|
30S ribosomal protein S4
|
unclassified Geobacter
|
MARYTGPSCRLCRREGSELFLKGERCYTDKCAIKRRSYPPGQHGQGRIKVSDYGVQLREKQKVRRIYGILENQFRGYFETADRMKGVTGENLLFILERRLDNVAYRLGFATSRDEARQLVRHGHFTLNGRKVNIPSLQVKAGDVLQLREKSRKVAAISESLEGVVRRGIPQWLELEKDAFKGTVKAMPVREDITMPIQEQLIVELYSK
|
With S5 and S12 plays an important role in translational accuracy.
|
C6E4N1
|
B7K0U6
|
NDHI_RIPO1
|
NDH-1 subunit I
|
Rippkaea orientalis
|
MFNLLKQVSDYAKESIEAAKYIGQGLSVTFDHMRRRPVTVQYPYEKLIPSERFRGRIHFEFDKCIACEVCVRVCPINLPVVDWEFNKAVKKKELKHYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELATYDRHELNYDNVALGRLPYKVTEDPMVTPLRELGYLPKGVLDPHDLPSGNQRSGKRPEEIIAESD
|
NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic 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.
|
B7K0U6
|
B2HN69
|
CAR_MYCMM
|
Fatty acid reductase
|
Mycobacterium
|
MSPITREERLERRIQDLYANDPQFAAAKPATAITAAIERPGLPLPQIIETVMTGYADRPALAQRSVEFVTDAGTGHTTLRLLPHFETISYGELWDRISALADVLSTEQTVKPGDRVCLLGFNSVDYATIDMTLARLGAVAVPLQTSAAITQLQPIVAETQPTMIAASVDALADATELALSGQTATRVLVFDHHRQVDAHRAAVESARERLAGSAVVETLAEAIARGDVPRGASAGSAPGTDVSDDSLALLIYTSGSTGAPKGAMYPRRNVATFWRKRTWFEGGYEPSITLNFMPMSHVMGRQILYGTLCNGGTAYFVAKSDLSTLFEDLALVRPTELTFVPRVWDMVFDEFQSEVDRRLVDGADRVALEAQVKAEIRNDVLGGRYTSALTGSAPISDEMKAWVEELLDMHLVEGYGSTEAGMILIDGAIRRPAVLDYKLVDVPDLGYFLTDRPHPRGELLVKTDSLFPGYYQRAEVTADVFDADGFYRTGDIMAEVGPEQFVYLDRRNNVLKLSQGEFVTVSKLEAVFGDSPLVRQIYIYGNSARAYLLAVIVPTQEALDAVPVEELKARLGDSLQEVAKAAGLQSYEIPRDFIIETTPWTLENGLLTGIRKLARPQLKKHYGELLEQIYTDLAHGQADELRSLRQSGADAPVLVTVCRAAAALLGGSASDVQPDAHFTDLGGDSLSALSFTNLLHEIFDIEVPVGVIVSPANDLQALADYVEAARKPGSSRPTFASVHGASNGQVTEVHAGDLSLDKFIDAATLAEAPRLPAANTQVRTVLLTGATGFLGRYLALEWLERMDLVDGKLICLVRAKSDTEARARLDKTFDSGDPELLAHYRALAGDHLEVLAGDKGEADLGLDRQTWQRLADTVDLIVDPAALVNHVLPYSQLFGPNALGTAELLRLALTSKIKPYSYTSTIGVADQIPPSAFTEDADIRVISATRAVDDSYANGYSNSKWAGEVLLREAHDLCGLPVAVFRCDMILADTTWAGQLNVPDMFTRMILSLAATGIAPGSFYELAADGARQRAHYDGLPVEFIAEAISTLGAQSQDGFHTYHVMNPYDDGIGLDEFVDWLNESGCPIQRIADYGDWLQRFETALRALPDRQRHSSLLPLLHNYRQPERPVRGSIAPTDRFRAAVQEAKIGPDKDIPHVGAPIIVKYVSDLRLLGLL
|
Catalyzes the ATP- and NADPH-dependent reduction of carboxylic acids to the corresponding aldehydes . Catalyzes the reduction of a wide range of aliphatic fatty acids (C6-C18) into their corresponding aldehydes. Can also reduce benzoate to benzaldehyde. Has a preference for NADPH over NADH as the electron donor .
|
B2HN69
|
Q0TR53
|
OGA_CLOP1
|
N-acetyl-beta-D-glucosaminidase
|
Clostridium
|
MKRKMLKRLLTSAFACMFIANGLITTTVRAVGPKTGEENQVLVPNLNPTPENLEVVGDGFKITSSINLVGEEEADENAVNALREFLTANNIEINSENDPNSTTLIIGEVDDDIPELDEALNGTTAENLKEEGYALVSNDGKIAIEGKDGDGTFYGVQTFKQLVKESNIPEVNITDYPTVSARGIVEGFYGTPWTHQDRLDQIKFYGENKLNTYIYAPKDDPYHREKWREPYPESEMQRMQELINASAENKVDFVFGISPGIDIRFDGDAGEEDFNHLITKAESLYDMGVRSFAIYWDDIQDKSAAKHAQVLNRFNEEFVKAKGDVKPLITVPTEYDTGAMVSNGQPRAYTRIFAETVDPSIEVMWTGPGVVTNEIPLSDAQLISGIYNRNMAVWWNYPVTDYFKGKLALGPMHGLDKGLNQYVDFFTVNPMEHAELSKISIHTAADYSWNMDNYDYDKAWNRAIDMLYGDLAEDMKVFANHSTRMDNKTWAKSGREDAPELRAKMDELWNKLSSKEDASALIEELYGEFARMEEACNNLKANLPEVALEECSRQLDELITLAQGDKASLDMIVAQLNEDTEAYESAKEIAQNKLNTALSSFAVISEKVAQSFIQEALSFDLTLINPRTVKITASSEETSGENAPASFASDGDMNTFWHSKWSSPAHEGPHHLTLELDNVYEINKVKYAPRQDSKNGRITGYKVSVSLDGENFTEVKTGTLEDNAAIKFIEFDSVDAKYVRLDVTDSVSDQANGRGKFATAAEVNVHGKLKENAEVTGSVSLEALEEVQVGENLEVGVGIDELVNAEAFAYDFTLNYDENAFEYVEAISDDGVFVNAKKIEDGKVRVLVSSLTGEPLPAKEVLAKVVLRAEAKAEGSNLSVTNSSVGDGEGLVHEIAGTEKTVNIIEGTSPEIVVNPVRDFKASEINKKNVTVTWTEPETTEGLEGYILYKDGKKVAEIGKDETSYTFKKLNRHTIYNFKIAAKYSNGEVSSKESLTLRTAR
|
Binds carbohydrates . Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
|
Q0TR53
|
Q3K437
|
ATPF_PSEPF
|
F-type ATPase subunit b
|
Pseudomonas
|
MNINATLIGQSVAFLIFVLFCMKFVWPPVIAALHERQKKIADGLDAASRAARDLELAQEKAGQQLREAKAQAAEIIEQAKKRGNQIVEEAVEKARIDADRVKVQAQAEIEQELNSVKDKLRAQVGLLAVGGAEKILGATIDQNAHAELVNQLAAEI
|
Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).
|
Q3K437
|
A6V6L2
|
UPPP_PSEA7
|
Undecaprenyl pyrophosphate phosphatase
|
Pseudomonas
|
MEWWTAFQAFILGVVEGLTEFLPISSTGHQIIVADLIGFGGERAKAFNIIIQLAAILAVVWEFRGKIFQVVRDLPSQHQAQRFTVNLLIAFFPAVILGVLFADLIHEWLFNPITVALALVVGGVIMLWAERRQHVIRAEHVDDMTWKDALKIGCAQCLAMVPGTSRSGATIIGGLLFGLSRKAATEFSFFLAMPTMVGAAVYSGYKYRELFRPEDLPVFAVGFVTSFVFAMVAVRALLKFIGNHSYAAFAWYRIAFGLLILATWQFHLIDWSTAGDL
|
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
|
A6V6L2
|
H2FU77
|
BAMC_OCESG
|
Outer membrane protein assembly factor BamC
|
unclassified Oceanimonas
|
MISLLAVAVLAGCSNPETRSQANRGFDYEQETLRTAPLLIPEGLQAPRFNTEYVIPKGTAQGVTGKVLDIRPPTQVLPLVRGSEAMTEGSGLWFYQQRLDQPLERELNQALTVFFEQTDTDYDAVANGFESSGDAIGAPSQQFRWQLMPDAVRRAVAVQVQSTEGGGVLAQDRLRAEASMLNAFSLSYQRELSRQQELLDQGPIALTLDAGQGLLLAEQDYDRTWKRLITLLPRLGFDISNRQQALGYVDVEFDGLSKGDWQDLRLPALDIPEQEYRIQLGDLGSRTSLSLSNKDREPVAADVLSKLVNTLAPAFERTDLVR
|
Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane.
|
H2FU77
|
B5YL84
|
COBS_THEYD
|
Cobalamin-5'-phosphate synthase
|
Thermodesulfovibrio
|
MINRFLIALSFLTVLPLKFKEINEKELIRSIIFFPFIGFLEGVFCIFLVNIFKQIFSSSVISIILLVFLFSVRGIFHIDGLSDTFDALFYKGTGQKEKDLQQRLQIMKDSVIGVAGAVALVLDVLCRFAFVKELIDINQFLIFLFMFCFSRWIVIPLMYYGKPARTTGLGVLFIGKISSWQVIISTVLPIFLLVYFTIEKNFIFLPLIALFLFFISYILKKFFERKFNGITGDHLGATVEITEIVFLICFLLGEKLWLSY
|
Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5'-phosphate.
|
B5YL84
|
A9A0L9
|
DNLJ_DESOH
|
Polydeoxyribonucleotide synthase [NAD(+)]
|
Desulfosudis
|
MHNTLDKSEAKERVTFLRNELHRHNHLYYIKDAPEISDAEYDRLFRELAELEALHPDLADPASPTARVGAPPTGDLATVTRTIPMLSISNAFADEELFKFDERVRRSLQTGDPVTYLAEPKLDGTAVELVYEKGRLVMAATRGDGVTGEVITPNARTIGSVPLHLTGDAVPMPNLLEVRGEVVMTKEGFEKLNALRLERDEPLFANARNAAAGSLRQLDSRVTASRPLTLIAYGIGRFSEIDAISTQHEIVTRLADFGFKTNSHVRWDLDIKGVIDFYRFLEGIRPSLPYDIDGMVVKVDRLDFQRTLGATSRSPRWVIAYKFAASQETTRLVAIDVQVGRTGALTPVALLEPVTIGGVTVSRATLHNEDEIARKDIRVGDAVLVQRAGDVIPEVVQVITGRRTGNETPFQMPATCPVCGTPVVREPSEAVTRCVNAACPAQVKERIKHFAAKGAFDIDGLGDKLVDQLVDRGMIASYADLFTLRVEDLESLDRMGFKSAQNLVAAIEKSRHITFDAFLYGLGMRHVGAHVATLLARAFPGIDQLAEAALAGQLNSIDGIGGVIAESVKNFFSNPENRQTVDSLINHGVALQFPEKEAATGHEMPLAGKTFVLTGTLEKMTRDQARQRIEAAGGKVTGSVSSRTDYVVAGEAPGSKRDKAEALGVAILDEAGLLSLLEPGER
|
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.
|
A9A0L9
|
Q0AAG8
|
RNFB_ALKEH
|
Rnf electron transport complex subunit B
|
Alkalilimnicola
|
MLTPILALTALALIAGALLGFAAVRFRVEGNPIADQVDAVLPQTQCGQCGFGGCRPYAEAIAAGEAEINRCPPGGQDTVQTLADLLGVEPLPLDEERGEAPHTPQVAWVDEAVCIGCTRCIQACPVDAILGAAKQMHTVLKGECTGCGLCVDPCPVDCIHMVPVDLDLAEWHWPLPQNDTARREVA
|
Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.
|
Q0AAG8
|
B7MTJ3
|
PYRC_ECO81
|
Dihydroorotase
|
Escherichia
|
MTAPSQVLKIRRPDDWHLHLRDGDMLKTVVPYTSEIYGRAIVMPNLAPPVTTVEAAVAYRQRILDAVPAGHDFTPLMTCYLTDSLDPNELERGFNEGVFTAAKLYPANATTNSSHGVTSVDAIMPVLERMEKIGMPLLVHGEVTHADIDIFDREARFIESVMEPLRQRLTALKVVFEHITTKDAADYVRDGNERLAATITPQHLMFNRNHMLVGGVRPHLYCLPILKRNIHQQALRELVASGFNRVFLGTDSAPHARHRKESSCGCAGCFNAPTALGSYATVFEEMNALQHFEAFCSVNGPQFYGLPVNDTFIELVREEQQVAESIALTDDTLVPFLAGETVRWSVKQ
|
Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate.
|
B7MTJ3
|
Q9FX55
|
SOT9_ARATH
|
Sulfotransferase 4c
|
Arabidopsis
|
MDEKDILRNLREEEEEEEENQSEETKILISSLPWEIDYLGNKLFKYQGYWYYEDVLQSIPNIHSSFQPQETDIVVASFYKSGTTWLKALTFALVQRSKHSLEDHHHPLLSHNPHEIVPYLELDLYLNSSKPDLTKFLSSSSSSSSPRLFSTHMSLDALKLPLKKSPCKVVYVCRNVKDVLVSLWCFLNANKGVEWGDFSQNEKIIRAENYSFKAIFESFCNGVTLHGPFWDHAQSYWRGSLEDPKHFLFMRYEELKAEPRTQVKRLAEFLDCPFTKEEEDSGTVDKILELCSLSNLSSLEINKTGSLGGVDYKTYFRKGQVGDWKSYMTSEMVNKIDMIVEEKLKGSGLKF
|
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor. No activity with brassinosteroids.
|
Q9FX55
|
O28316
|
LEUC1_ARCFU
|
Isopropylmalate isomerase 1
|
Archaeoglobus
|
MAQTLVEKIFSKASGKEVKAGEFVMANIDLAMIHDITAPLAIKAFREILGSDAKVWDKSKVIMAFDHQVPADSVHAAENHKMLRKFAEEQGILNYDVKGGIAHQIMVENHVEPGMLIVGADSHTCMYGALGAFATGIGSTDMGFVLAMGKLWFKVPESIRFNVHGKLEKHVYGKDIVLKLIGMVGADGANYKACIYSGEVVEKLGMSDRLTMCNMAIEMGGKAGIVEPDKTTLEYLKAMGRPYEGELLKSDEDAEFQEVELDVTGMEPQVAAPHRVDNVVGISEVEGTRVDQVFIGSCTNGRYEDLKIAAEILKGEKVASNVRLIVIPASHREYRRALKEGLIEIFVDAGALVEAPCCGPCMGGSFGLIASGEVSVSTSNRNFIGRQGSPEGKIYLVNPAVAAATAIYGEITDPRKIK
|
Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.
|
O28316
|
O16202
|
LYS7_CAEEL
|
Lysozyme-like protein 7
|
Caenorhabditis
|
MAHKSIVIFSVLAVLCHSASVKVPPIVDSSLPVKFSEVIAEPAPNVPSNLASYAYALDIYVQTTLSQLQCIKQAGYCAVFVRAYNPAGQGSFDTSSCVTIQNAYKAGLGIEIYMTPQPVSNKQGYQQLDEIIQGLTARAITVRAIWIQVTSPTNWPNNANSNINFINSIVSRARQSGLTVGIYTSYYDWNQITTGWSNIGNDVLLWYWNVYSGGVTGETPANFNDFRKFGCWTAPSVKQFAQDETVCGITVNRDVYLAGNVLKAVEEDGKIYAGGFVQGSLKI
|
Plays a role in resistance to Gram-positive bacteria B.thuringiensis and M.nematophilum and Gram-negative bacteria S.boydii or S.flexneri infection and to fungus C.neoformans infection . Plays a role in susceptibility to Gram-negative bacterium S.typhimurium infection .
|
O16202
|
A5ETJ9
|
GLND_BRASB
|
[Protein-PII]-UMP uridylyl-removing enzyme
|
unclassified Bradyrhizobium
|
MDSVTPNSRPESFPEFDSAGLAAAVDALAAQHSGREDMFRAAVVQLLKAELVKARAVAQAQLLKDRHGRRCAERLCFVQDEIIRILYAAATQHLYRSQVPSGAERMAVVATGGYGRGLMAPESDIDLLFILPYKQTAWGEQVAEAILYSLWDMGLKVGHATRSVDESIRQARGDMTIRTAILETRYLAGDRPLYDELVERFDTEVVQGTAAEFVAAKLAEREERHRRGGQSRYLVEPNVKDGKGGLRDLHTLFWIAKYVYRVRETAELVERGVFDAHEYRTFRRCADFLWSVRCNLHFVSGRPEERLSFDLQREIAVRLGYTSHPGMQDVERFMKHYFLVAKEVGNLTAILCAKLEDQQAKPAPVLSRVISRLKTGNSWRRVPESDDFIVDNNRINLAAPDVFKHDPVNLIRIFRLAQKNNLAFHPDAMRAVTRSLNLINTELRDNPDANRLFMEILTSNDAETVLRRMNETGVLGHFIRAFGRIVSMMQFNMYHHYTVDEHLIRCIGFLQEIERGGIDEFALASDLMRKIRPEHRAVIYISVLLHDVAKGRPEDHSIAGAKVARRLCPRLGFNNADTELVAWLIEEHLTMSTVAQSRDLSDRRTIEKFAAVVQSVEQMKLLTILTTADIRGVGPGVWNGWKAQLLRTLYYETEPVLTGGFSEVNRAKRITAAQAEFRNAFTDWPEDELNTYIGRHYPAYWLKVELPRKIRHARFVRASEDAGHKLAINVGFDPARGVTELTIFAMDHPWLLSIIAGACASAGANIVDAQIYTTTDGRALDTIAISREYERDEDEGRRATRIGETIEQVLEGKLRLPDAVARRTTRGKQHKAFSVEPEVSINNQWSELYTVIEVSGLDRPGLLYELTTAISKLNLNIASAHVATFGERARDVFYVTDLLGAQINAPTRQAAIKSALLHLLASDDTAAQPAA
|
Modifies, by uridylylation and deuridylylation, the PII regulatory proteins (GlnB and homologs), in response to the nitrogen status of the cell that GlnD senses through the glutamine level. Under low glutamine levels, catalyzes the conversion of the PII proteins and UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls uridylylation state and activity of the PII proteins, and plays an important role in the regulation of nitrogen fixation and metabolism.
|
A5ETJ9
|
P0DQJ4
|
GEND1_ACAGO
|
Genicutoxin-D1-like protein
|
Acanthoscurria
|
SFRFFEEIIMRLATLLGLSVLHLALCVLTCTAHHPGLEKSRVSYENMGDEENAEERSCVHERETCSKVRGPLCCRGECICPIYGDCFCYGS
|
Putative ion channel inhibitor that may also act as a antimicrobial peptide.
|
P0DQJ4
|
Q1HN33
|
BDNF_LOXBI
|
Brain-derived neurotrophic factor
|
Loxocemus
|
SCMKAAPMKEVSIRGQGSLAYPGLRTQGNLETLSGPNDATRGLTSLADTFEHVIEELLDEQQVIQPSKENKDADLYSSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSTSEWVTAAEKKTAVDMSGATVTVLEKVPVPKGQLKQYFYETKCSSKGYAKEGCRGIDKRYWNSQCRTTQSYVRALTMDNKKRVGWRFIRI
|
Promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it.
|
Q1HN33
|
B5RB82
|
NAGK_SALG2
|
GlcNAc kinase
|
Salmonella
|
MYYGFDIGGTKIALGVFDSTRRLQWEKRVPTPHTSYSAFLDAVCELVAEADQRLGVKGSVGIGIPGMPETEDGTLYAANVPAASGKPLRADLSARLDRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKPITGQSYITGEFGHMRLPVDALTLMGFDFPLRRCGCGQMGCIENYLSGRGFAWLYQHYYDQSLQAPEIIALWEQGDEQAHAHVERYLDLLAVCLGNILTIVDPDLLVIGGGLSNFTAITTQLAERLPRHLLPVARAPRIERARHGDAGGMRGAAFLHLTD
|
Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
|
B5RB82
|
Q9ZD46
|
TRUB_RICPR
|
tRNA-uridine isomerase
|
typhus group
|
MGNYWLNFYKPRGISSAKLVNIVKKIIGKTKIGHAGTLDVEAEGILPLAVGEATKLIQLLIDARKTYIFSVKFGTQTDSGDYTGKVIASKDYIPSQEEVYTVCSKFIGNIRQVPPIFSAIKVNGVRAYKLAREGKIVELKPRNITIYDLKCLNFDKENAIATYYTECSKGLI
|
Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs.
|
Q9ZD46
|
O68324
|
CH60_LACHE
|
Chaperonin-60
|
Lactobacillus
|
MAKDIKFSENARRSLLKGVDKLADTVKTTIGPKGRNVVLEQSYGNPDITNDGVTIAKSIELKDRYENMGAKLVAEAAQKTNDIAGDGTTTATVLTQAIAREGMKNVTAGANPVGIRRGIEKATKAAVDELHKISHKVESKDQIANVAAVSSASKEIGALIADAMEKVGHDGVITIEDSRGINTELSVVEGMQFDRGYLSQYMVTDNDKMEADLDNPYILITDKKISNIQDILPLLQEIVQQGKSLLIIADDITGEALPTLVLNKIRGTFNVVAVKAPGFGDRRKAQLQDIAALTGGTVITEDLGLELKDTKIDQLGQARRITVTKDSTTIVGGAGSKEAIDERVDTIRKQIEDSTSDFDKKKLQERLAKLTGGVAVIHVGAATETELKERRYRIEDALNSTRAAVDEGYVAGGGTALVNVEKAVREVKGETTDEQTGINIVLRALSAPVRQIAENAGKDGSVILDKLEHQENEIGYNAATDKWENMVDAGIIDPTKVTRTALQNAASIAALLLTTEAVVAEIPEPKQAAPQGGAGAPMGM
|
Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
|
O68324
|
A1VZB4
|
KTHY_CAMJJ
|
dTMP kinase
|
Campylobacter
|
MYVVFEGIDCVGKSTQISLLKEIYKDAIFTLEPGGTELGKHLREILLNKTHPINKRAELLLFLADRAQHFEEILKINQNKLIISDRSFISGMAYAKDFENDLLFALNSFALENFFPQKIIFLKGDANLIQERLSQKELDSIEKRGIEYFLSVQDKLEKVLHFLKEKISIEILTLDAKESKEKLHQQIKEFLQ
|
Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
|
A1VZB4
|
A4YV68
|
SURE_BRASO
|
Nucleoside 5'-monophosphate phosphohydrolase
|
unclassified Bradyrhizobium
|
MRILCTNDDGIHAPGLKVIEEIARALSDDVWIVAPELDQSGVSHSLSLNDPLRLREVGPRHFAVRGTPTDCVIMGARHILGEKRPDLVLSGVNKGRNVAEDVVYSGTIAGALEGTILGLPSFALSQEFSIATRDKPSWDTALKFGPQIVRKVLDAGVPKNTVINVNFPSCAPDQVKGIVVTRQGKRNLGFLKVDERRDGRGNPYFWIGFDRAAALDVPEEGTDLAALAAHYVSVTPLRLDRTDEAFSGKLGSILA
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
A4YV68
|
P73440
|
Y1459_SYNY3
|
Nucleoside 5'-monophosphate phosphohydrolase
|
unclassified Synechocystis
|
MNFLLTNDDGIDAPGIEALYEALGKRGVWVAPKNQHSGCGHKVTTDQAIAVEQRGKNRYAVDGTPADCTRLGVVHFYPEVDWVIAGINAGGNMGIDSYLSGTVAAVREAAILGHKAIAISHWINKPRTINWAWASHWANAVFNTLWQQDLPPQHFWNVNLPHWQSGDPEPEVIFCEPSRDPLPVAFTIEGSNFFYRGEYSQRPRQPGSDIDVCFSGNIAITQLRV
|
Nucleotidase that shows phosphatase activity on nucleoside 5'-monophosphates.
|
P73440
|
Q55BI8
|
DUSP3_DICDI
|
Probable dual specificity protein phosphatase DDB_G0271350
|
Dictyostelium
|
MGISMILDNFLYLGAAKDTKDEKEMEKLKITHIFSCAGTVHSPEKYIIANEKFEDDETVDISEQIEKAYWFIERVRMKKGARVFIHCMAGKSRSASIVLSYLLKRDIHSLSDCLFYLHSKRLEIRPNDGFMNQLCDLELKLTNKQTLSKEIKEWRSLQSKALKTKIDVQTCHFIQPSLDSTKKANEQYLLHIQSISFTFFEIHLNQDKIIQLYQQQCQLLHSNNIDIKYFTSILQEELSNSTKKAFDFLLIHYYLDWQDIINNLLNYTNLKLNLN
|
Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
|
Q55BI8
|
Q5E715
|
METN_ALIF1
|
Methionine import ATP-binding protein MetN
|
Aliivibrio
|
MIEINRVNKIFYQGAKEINALKDINLHIAQGTIFGVIGSSGAGKSTLIRCVNMLERPTNGEVVVDGVDLTKLSSSELSKARRNIGMIFQHFNLLASRTVFDNVALPLELAGKSKHDIQKKVTELLDLVGLADKHHTYPANLSGGQKQRVAIARALSTDPKVLLCDEATSALDPATTKSILELIKDLNRKLSITILIITHEMEVVKNICHEVAIIGGGELVEKGAVSDIFAHPKTALAQEFIRATLDLSIPEDFKARLKDTYVEGSYPLIRLEFTGSTVDAPVISQISREFDIDISILSSDIDYAGGVKFGLMLAEVFGNQESTQKAIEFLRNHHVKVEVLGYVV
|
Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system.
|
Q5E715
|
Q6B906
|
RK1_GRATL
|
50S ribosomal protein L1, chloroplastic
|
Agarophyton tenuistipitatum
|
MKKRSRRFSTLLKQIEADKLYSPLDALNLMKNLSNVKFIETAEVHIVLGLDPKYADQQLRTTVMLPKGTGKIMRVAVITQNNKTHEAKSSGADIVGGEDLIDEIKKGRLDFDKLIATPDMMMSIAKLGKILGPKGLMPSPKAGTVTHNLITTIKEFKAGKLEYKIDRSGILHIPFGKLNFNVEDLHINLITLQESIDRNRPQGSKGKYWKSVHINSTMGPSIPLDIQLLRNNYVL
|
Binds directly to 23S rRNA. Might be involved in E site tRNA release (Potential).
|
Q6B906
|
Q0AN96
|
FLGH_MARMM
|
Basal body L-ring protein
|
Maricaulis
|
MIRKLAALIVAAAALQACAVSDRLSYVGQTPPMTPIQNPADLAGTGPSQLPMPMPRMPQQRYATNSTANNSLWTANSPTFFGDPRADQVGDIVTVNIAISDSAQLNNTTNRSRSSAEDSDLTSFLGADLTGFFNDNIDPTSMTSLGSTSSLAGSGSVNRTESISLTVAALVTQVLPNGNLVIAGRQEVRVNNEVRELLITGIARPQDIGSDNTIAHTQIAEARISYGGRGHLSDAQRPRYGQELYDILMPF
|
Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
|
Q0AN96
|
O25620
|
VAD2_HELPY
|
Virulence-associated protein D homolog
|
Helicobacter
|
MYAVTFDLDTNCLNENAVNLSKVYSDIRKFMEQHGFKWQQGSVYFGDETINAVTCVATVQILAKQIPSFAVCVKDVRMLKIEENNDLMPAIKIVL
|
Cleaves ssRNA, mostly between U:A.
|
O25620
|
Q8PJX2
|
MUTL_XANAC
|
DNA mismatch repair protein MutL
|
Xanthomonas
|
MAIRQLPEILINQIAAGEVVERPASVVKELVENALDAGATRVDIELEEGGVRLIRIRDNGGGITPDELPLAVSRHATSKIASLDDLETVATLGFRGEALPSIASVSRFTLTSRRHDAEHGSALEIDGGRLGEVVPRAHAPGTTVEVRELFFNVPARRKFLRAERTELGHIEEWLRSLALARPDVELRVSHNGKPSRRYKPGDLYSDARLGETLGDDFARQALRVDHSGAGLRLHGWVAQPHYSRASTDQQYLYVNGRSVRERSVAHAVKMAYGDVLFHGRQPAYVLFLELDPARVDVNVHPAKHEVRFREARLIHDFVYRTLQDALAHTRAGATPNSIGGDGTGYTAATSGGMGGIASGGVPGNGGASIGSGGAYSYASWTPSQTPLGLRVDEARAAYSALYAPPPSSAQQSAGMPNMAGTGLPATAQDSGVPPLGYAIAQLHGIYILAENAEGLIVVDMHAAHERIGYERLKHAHDSIGLHAQPLLVPMTLAVGEREADTAEREAETLATLGFEITRAGPQSLHVRSIPALLANAEPEALLRDVLSDLREHGQSRRIASARDELLSTMACHGAVRANRRLTVPEMNALLRDMEATERSGQCNHGRPTWARFTLSDIDRWFLRGR
|
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.
|
Q8PJX2
|
Q6MSM9
|
RS19_MYCMS
|
30S ribosomal protein S19
|
Mycoplasma
|
MARSLKKGPFVDESLFKKVTAAKDGEVIKTWSRRSTIFPEFIGKTFGVYNGKEFIPVYITEDMVGNKLGEFAPTRKFGGHGDDKGKKK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
Q6MSM9
|
A4RGT4
|
MEP1_MAGO7
|
Extracellular metalloprotease MGG_08041
|
Pyricularia
|
MQINVVKTFLFALAASSVSALAVDTEFRCGAPEPSEELIEASAIMAVAEAEAAANGTLAARQSALTIDTYVHVVATSTSASAGYLSDATIQQQLRVMNEDYAPSGIQFVLKGTDRTVNANWARDSGETAMKTALRKGTYKDLNLYFLSSIPGGILGYCYFPASATTSTVRLDGCTIASGTVPGGSISRFNLGKTAVHEVGHWFGLYHTFQGGCNGQGDLVDDTPAQASASSGCPIGRDSCPNQPGLDPIHNYMDYSDDSCYEEFTPGQNARMSSMFAQFRAGK
|
Secreted metalloproteinase that allows assimilation of proteinaceous substrates.
|
A4RGT4
|
Q9SZL7
|
FRS9_ARATH
|
Protein FAR1-RELATED SEQUENCE 9
|
Arabidopsis
|
MAIIAVAELVEEVSMSRVEHVLNYLKRRQLENPGFLYAIEDDCGNVFWADPTCRLNYTYFGDTLVFDTTYRRGKRYQVPFAAFTGFNHHGQPVLFGCALILNESESSFAWLFQTWLQAMSAPPPPSITVEPDRLIQVAVSRVFSQTRLRFSQPLIFEETEEKLAHVFQAHPTFESEFINCVTETETAAEFEASWDSIVRRYYMEDNDWLQSIYNARQQWVRVFIRDTFYGELSTNEGSSILNSFFQGFVDASTTMQMLIKQYEKAIDSWREKELKADYEATNSTPVMKTPSPMEKQAASLYTRAAFIKFQEEFVETLAIPANIISDSGTHTTYRVAKFGEVHKGHTVSFDSLEVKANCSCQMFEYSGIICRHILAVFSAKNVLALPSRYLLRRWTKEAKIRGTEEQPEFSNGCQESLNLCFNSLRQEATKYVEEGAKSIQIYKVAMDALDEAAKKVAAASNRTPGTRLPNGEAYPSEEARETANATNHPGGEKERTILELTAELERTGQRCEVYRANLLSILRDMEEQKFQLSLKVQNARLSLKE
|
Putative transcription activator involved in regulating light control of development. May act as a negative regulator specific to phyB signaling.
|
Q9SZL7
|
C1DHV0
|
GLPK_AZOVD
|
Glycerokinase
|
Azotobacter
|
MTQTNNKHYIVALDQGTTSSRAIVLDRDANVVSVAQHEFTQIYPQSGWVEHDPMEIWATQSATLVEALAQAGIDHRQVAAIGITNQRETTVIWDKQSGRPIHNAIVWQCRRSAAICEELKRDSLEEHVRERTGLVIDPYFSATKIKWVLDHVEGSRERARRGELLFGTVDSWLIWKMTQGRVHVTDFTNAARTMLFDIHALDWDARLLEALDIPREMLPQVRSSSEVYGHACIAGGDEDDGIPIAGIAGDQQAALFGHMCVEPGQGKNTYGTGCFLLMNTGAKAVRSGHGLLTTIACGPRGEVAYALEGAIFNAGSTVQWLRDELKLIDDSFDSEYFATKVQDSNGVYLVPAFTGLGAPYWDPYARGAVFGLTRGVKADHLIRAALESIAYQTCDVLDAMQRDAGERLKALRVDGGAVSNNFLMQFQADLLGTPVERPAVKEVTALGAAYLAGLATGFWSGLDELRDKARIERVFEPACSEEKRRSLSAGWKKAVLRSQRWAEDD
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
C1DHV0
|
A8GXV3
|
XERC_RICB8
|
Tyrosine recombinase XerC
|
belli group
|
MLDTQIQELIIKWQKYLSLQKNYSNHTLISYNNDLKHFLEFMNYYNSDIVTMDYIKAADIRLMRSWLAKRKCDNFVTSSIARGLSAIKNFYKFLEKTAELHNHVVFSIKSPKKSKLLPKALSEEEVNISLDHIEEYGNSQWIEIRNKALLVLIYASGLRISEALSITKLHLQNLEFIKIMGKGSKERVIPWLAIARNLITEYLEKLPYELKDDEPIFRGKQGKKLQPPVFNRELIKLKRFYGLPEHLSAHSFRHSFASHLLENGADLRSIQELLGHKSLSTTQSYTKTSIKHLETAYVTAHPIKK
|
Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC-XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids.
|
A8GXV3
|
Q9R0K8
|
STC2_RAT
|
Stanniocalcin-2
|
Rattus
|
MCAERLGQFVTLALVFATLDPARGTDSTNPPEGPQDRGSQQKGRLSLQNTAEIQHCLVNAGDVGCGVFECFENNSCEIQGLHGICMTFLHNAGKFDAQGKSFIKDALRCKAHALRHKFGCISRKCPAIREMVYQLQRECYLKHDLCSAAQENVVVIVEMIHFKDLLLHEPYVDLVNLLLTCGEDVREAVTRSVQAQCEQSWGGLCSILSFCTSNIQRPPTAAPEHQPLADRAQLSRPYHRDTDHHLTANRGAKGERGSKSHLHAHARGGAGGQSAQGPSGSSEWEDEQSEYSDIRR
|
Has an anti-hypocalcemic action on calcium and phosphate homeostasis.
|
Q9R0K8
|
Q4QMS5
|
GLMU_HAEI8
|
Glucosamine-1-phosphate N-acetyltransferase
|
Haemophilus
|
MTKKALSAVILAAGKGTRMYSDLPKVLHTIAGKPMVKHVIDIAHQLGSENIHLIYGHGGDLMRTHLANEQVNWVLQTEQLGTAHAVQQAAPFFKDNENIVVLYGDAPLITKETLEKLIEAKPENGIALLTVNLDNPTGYGRIIRENGNVVAIVEQKDANAEQLNIKEVNTGVMVSDGASFKKWLARVGNNNAQGEYYLTDLIALANQDNCQVVAVQATDVMEVEGANNRLQLAALERYFQNKQASKLLLEGVMIYDPARFDLRGTLEHGKDVEIDVNVIIEGNVKLGDCVKIGAGCVLKNVVIGNDVEIKPYSVLEDSIVGEKAAIGPFSRLRPGAELAAETHVGNFVEIKKSTVGKGSKVNHLTYVGDSEIGSNCNIGAGVITCNYDGANKFKTIIGDDVFVGSDTQLVAPVKVANGATIGAGTTITRDVGENELVITRVAQRHIQGWQRPIKKK
|
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.
|
Q4QMS5
|
Q47Q20
|
MEND_THEFY
|
Menaquinone biosynthesis protein MenD
|
Thermobifida
|
MNPSTALARVLVDELARLGLTEAVIAPGSRSTPLALALVADTRIRTHVRIDERSASFLAVGLARASRRPVALVCTSGTAAANFHPAVLEADQSGVSLIVLTADRPPELRGTGANQTVNQIGLYGSAVRFFAEVGVPEREAGMVAYWRSLVCRAWAAAQANKPGPVHLNLAFREPLVPEPGGQPWPEPVTGRPDGKPWITVDLQRNEPEPVELPWVERGVIVCGDGDYDPIPLLALSAQTGWPLLAEPTSNARRAEALSSYRQLLAVPEFVAAHEPELVVSVGRPGLSRQLLAYLRRAPRHVVVGDPVAFADPVRTATDVVGAVTAPPSATPDTAWAASWAAAEAAARAAADRLLDSDETLSELRLARDLAAHLPAGSLLFAGASMPIRDLDAVMRPRCGLRLIGNRGVSGIDGTVSTAVGAALAHQADGGGEAFALLGDLALLHDQNGLLLGPDEPRPNLTIVVVNNDGGGIFSELEQAGHPDFERVFGTPHGVAVEQVAATAGLPYTRVEWATDLPKALIGDGLRLVEVRTDRAASARLRRALQEAVAAAVR
|
Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
|
Q47Q20
|
A1SNC7
|
NRDR_NOCSJ
|
Transcriptional repressor NrdR
|
Nocardioides
|
MHCPYCRNTDTRVLDSRVADDGGSIRRRRTCSACAKRFTTVELMQLTVLKRSGASEPFTREKAVAGVRKACKGRPVTEDQLACLGQAVEDALRLDGAAEVPAHEVGLAILGPLRELDEVAYLRFASVYRAFESADDFEDEIAMLRAERPAVAIEPVTVPATEPAPPQPVATG
|
Negatively regulates transcription of bacterial ribonucleotide reductase nrd genes and operons by binding to NrdR-boxes.
|
A1SNC7
|
B8FXS7
|
GLPK_DESHD
|
Glycerokinase
|
Desulfitobacterium
|
MKKYVLALDQGTTSCRAILFDRESQIVGVAQKEFTQIYPQPGWVEHDPEEVWSTQYGVIAELLARYQVTSEEIAGIGITNQRETTVVWDKHTGKSVTNAIVWQCRRTAPLCDELKMKGLEPLFKEKTGLVLDAYFSGTKIRWILDRVPGAQEKAEKGELLFGTMDTWLVWNLTKGRIHVTDYSNASRTLLYNIKTLAWDPDLLQVLNIPLAMLPEVKPSSTIYGETAAEGLFGHPIPIAGIAGDQQAALFGQACFAPGMAKNTYGTGCFMLLNTGEELYESRHGLISTIAWGLDEKVIYALEGSVFMAGAVMQWLRDELKLIETAGDSEYFAGKVADNGGVYLVPAFTGLGAPYWDMDARGAIVGLTRGSNKNHIIRAALESMAYQTRDILEAMEADSQLPLQLLKVDGGAVVNNLLMQFQADILGVEVERPHCIETTALGAAYLAGLAIGFWSSKEELRDKAKMERSFKPQMAEERKEKYYQGWHKAVRQIME
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
B8FXS7
|
P31326
|
OTC_LITCT
|
Ornithine transcarbamylase
|
Lithobates
|
MLHHMRTIINASWRYGNKCIVRQFGFSQTYSQLKGRDLLTLKNYSAEEIKYLLWVAADLKYRIKEKGEYLPLLQGKSLAMIFEKRSTRTRLSTETGFALLGGHPSFLTTQDIHLGVNESLKDTARVLSGMTDAVLARVYHQSDLEVLAEEASIPIVNGLSDDYHPIQILADYLTIQEHYGHLKGLTISWIGDGNNVLHSIMMSAAKFGMHLHIATPKGYEPNSSLTEAAKQFSKECGTKLLMTNDPLEAANGANVLVTDTWVSMGQEEEKKKRLLDFKGYQITMKTAKLAAPNWIFLHCLPRKPEEVDDEVFYCPKSLVFQEAENRKWTIMGVMVSLLTDYSPQLLRPTF
|
OTC is necessary for the tadpoles transition from an ammonotelic, aquatic larva to a ureotelic, terrestrial adult.
|
P31326
|
Q8KDS8
|
AAPAT_CHLTE
|
Aspartate/prephenate aminotransferase
|
Chlorobaculum
|
MSVESFERFLSRRVLSMQESQTMKITGLAKKMQAEGKDVVSLSAGEPDFPTPENVCEAGIEAIRKGFTRYTANSGIPELKKAIIRKLQRDNGLEYAEDEIIVSNGGKQALANTFLALCDEGDEVIVPAPYWVSFPEMARLAEATPVIVETSIETGYKMTPEQLAAAITPKTRILVLNSPSNPSGAVYNEAEVRALMQVIEGKEIFVLSDEMYDMICYGGVRPFSPARIPEMKPWVIVSNGTSKSYSMTGWRIGYLAAPKWIINACDKIQSQTTSNANSIAQKAAVAALDGDQSIVEQRRAEFEKRRDFMFRELNTISGIECTLPEGAFYIFPSIKGLLGKTFGGKVMKDSTDVAEYLLTEHYVATVPGDAFGAPENLRLSYAASIEELAEAVNRIRKAFS
|
Catalyzes the reversible conversion of aspartate and 2-oxoglutarate to glutamate and oxaloacetate . Can also transaminate prephenate in the presence of aspartate .
|
Q8KDS8
|
P13812
|
E2AB_ECOLX
|
Heat-labile enterotoxin IIA, B chain
|
Escherichia
|
MSSKKIIGAFVLMTGILSGQVYAGVSEHFRNICNQTTADIVAGVQLKKYIADVNTNTRGIYVVSNTGGVWYIPGGRDYPDNFLSGEIRKTAMAAILSDTKVNLCAKTSSSPNHIWAMELDRES
|
The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
|
P13812
|
Q7VZ79
|
UPP_BORPE
|
UPRTase
|
Bordetella
|
MPVHEIRHPLIRHKLGIMRRADLSTKSFRELSQEVAALLTYEATKDMPLAPASVEGWCGTVEVDKITGKKVTVVPILRAGIGMLDGVLSLIPGAKVSVVGVARNEETLQAHTYLERLVGELDQRLALIVDPMLATGGSMVAAIDMLKRAGCREIRALTLVSAPEGIDAVLKAHPDVQIYTASIDQGLNENGYIMPGLGDAGDRIFGTTQKHAE
|
Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
|
Q7VZ79
|
B8E6K8
|
YBEY_SHEB2
|
Endoribonuclease YbeY
|
Shewanella
|
MSLDLALDIQHATTCDWLPTDEQFALWATTAIGNSMDEAELTIRIVDSRESQMLNSTYRGKDKPTNVLSFPFEAPPEIELPLLGDLVICAAVVENEAREQQKTLEAHWAHMVVHGCLHLLGYDHIEDEEAEEMESLETQLIEGLGFTDPYKEQ
|
Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA.
|
B8E6K8
|
Q89AP5
|
DEGPL_BUCBP
|
Protease Do
|
Buchnera
|
MKKITMIFNTVLIFLVFLLISGFSWHKSEIPTQEKFFESKSFSLSTVLEKVIPSVVSITVEGNVTQSTRIPRQFQSSFNKKVLDCFGISRCMTRQGKFHALGSGVILDSKNGYIVTNSHVVDRANKIQVQLSNGCKHEAVVIGKDARFDIAIIKLKKVKNLHEIKMSNSDILKVGDYVIAIGNPYGLGETVTSGIISALHRSGLNIENYENFIQTDAAINRGNSGGALVNLKGELIGINTAILTPDGGNIGIGFAIPINMVNNLTTQILEYGQVKQNELGIVGMELNSDLAKVLKINVHRGAFISQVLSKSPADVSGIKPGDVIILLNRKPIASFATLRAEIASFPIKTKIELGILRNKKVKFIIVELKQKIQSKIDSSVLCKLISGASLSNFRIHGQNKGICVNYVNNGTPAYRTGLRKNDIIFEVNKYQVSSLSNFQKVLKTKPLILVLHVKRGNDVLYLVTH
|
Might be efficient in the degradation of transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions.
|
Q89AP5
|
B7GYS7
|
LEPA_ACIB3
|
Ribosomal back-translocase LepA
|
Acinetobacter calcoaceticus/baumannii complex
|
MAQAKKSVDIKNIRNFSIIAHIDHGKSTLADRFIQMCGGLQDREMQAQVLDSMELERERGITIKAASVTLYYTHPNGQEYQLNFIDTPGHVDFSYEVSRSLAACEGALLVVDAAQGVEAQSVANCYTAIEQGLEVLPILNKIDLPQAEPERVIHEIEEIIGIEATNAPTCSAKTGLGVEGVLETLVDVIPAPTGDREAPLQALIIDSWFDNYLGVVSLVRIKDGRIRKGDKMLVKSTGQTHIVTSVGVFNPKHTETGVLEAGEVGFVIAGIKDIFGAPVGDTITLSTTPEVASLPGFKKVKPQVYAGLFPIDASDFEPFREALQKLQINDSALFFEPESSDALGFGFRCGFLGMLHMEIVQERLEREYDLDLISSAPTVVYEAVTKKGDTIYIDSPSKMPDGSVVEDLREPIAECHILVPQEYLGNVMTLCIERRGVQKDMKFLGNQVSITFEIPMAEVVMDFFDKLKSCSRGFASLDYNFIRFESSSLVKVDVLINGEKVDALAMICHRNDARHRGIALVEKMKDLIPRQMFDVAIQAAIGAQIIARSTVKAMRKNVLAKCYGGDVSRKKKLLAKQKEGKKRMKQVGSVEIPQEAFLAVLKVER
|
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.
|
B7GYS7
|
Q9WYZ2
|
HSLU_THEMA
|
Unfoldase HslU
|
Thermotoga
|
MKSFDEMTPKEIVQELDKYIVGQYEAKKAVAIAVRNRIRRQKLPEEWRKEVLPKNILMIGPTGVGKTEIARRLAQLSGSPFLKVEATRFTEVGYVGKNVDSMIRDLVEISVNMVKQEKIKEVERQAEELVEERILDALVPESKAMPVVTNPFINLITGGQQQQYTPEDRRRFRAKREEMREKLRKGELEDEEIEIELEETVSPFMGIFGPGMEDLGIEITNMFSGMLPKRKKKRKMKVSEARKVLLPLEAEKLIDMDKVVQEALDRAQNRGIIFIDEIDKIAGKESAVGPDVSRQGVQRDLLPIVEGTTIMTKYGPVRTDFILFIAAGAFHVSRPSDLIPELQGRFPIRVELSPLTEEDFVRILKEPENAIIKQYQALLSTEGVELVFTEDGIREMARIAYQLNQRLENIGARRLYTVAEKVLEEISFEAPDIPEKRVVVDAEYVRRRLEKIVQDEDLSAYIL
|
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
|
Q9WYZ2
|
Q5F678
|
QUEF_NEIG1
|
PreQ(0) reductase
|
Neisseria
|
MSRNNEELQGISLLGNQKTQYPTGYAPEILEAFDNKHPDNDYFVKFVCPEFTSLCPMTGQPDFATIVIRYIPHIKMVESKSLKLYLFSFRNHGDFHEDCVNIIMKDLIALMDPKYIEVFGEFTPRGGIAVHPFANYGKAGTEFEALARKRLFEHDAQ
|
Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
|
Q5F678
|
B5ZSU2
|
PDXH_RHILW
|
Pyridoxal 5'-phosphate synthase
|
Rhizobium
|
MSANELTSGDFTESGEPFKLFAEWLGEAEASEPNDPNAVALATVDEDGLPNVRMVLLKGFDDNGFVFYTNFESQKGREILGQKKAAMCFHWKSLRRQVRLRGPVEIVTDAEADAYFKTRARGSRIGAWASKQSRPLESRFALEKAVAEYTARYAIGEIPRPAHWSGFRIRPTSIEFWKDQNFRLHDRIEFRRPLPEGAWDKVRMYP
|
Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP).
|
B5ZSU2
|
Q8CNC7
|
UREF_STAES
| null |
Staphylococcus
|
MIDHQHLRLFQFCDSQFPTGAFSHSFGLETYIQRETVHDTETFIKWLHLFINEQLTYSDGIAMRIVYHALINNDKDKILDINQKLFVQNLPKETRIGAKQMGTRMVKLALDLYDSEWIQWYYNQMKNNKIKLHPAVCFTMLGHFLGVDVESIIDYYLYQNISSLTQNAVRAIPLGQTAGQQVVTEMIAHIEKTRNHILELDEIDFGMTAPGLELNQMEHENVHVRIFIS
|
Required for maturation of urease via the functional incorporation of the urease nickel metallocenter.
|
Q8CNC7
|
Q864H9
|
MSHR_MICAD
|
Melanocortin receptor 1
|
Mico
|
MPMQGAQRKLLGSLNSTPTATSNLGLAANHTGAPCLEVSIPDGLFLSLGLVSLVENVLVVAAIAKNRNLHSSMYCFICCLALSDLLVSGSNMLETAIILLLEAGTLATRASVVQQLHNTIDVLTCSSMLCSLCFLGAIAVDRYISIFYALRYHSIMTLPRAQRAIAAIWVTSVLSSTLFITYYDHAAVLLCLVVFFLAMLVLMAVLYVHMLARACQHAQGIIRLHNRQLPAHKGFGLRGAATLTILLGIFFLCWGPFFLHLTLVVFCPQHLTCNCIFKNFKVFLTLIICNTIIDPLIYAFRSQELRRTLKEVLLCSWWPGCGAEGGGDSVWPGSCVTLRGPLPP
|
Receptor for MSH (alpha, beta and gamma) and ACTH. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. Mediates melanogenesis, the production of eumelanin (black/brown) and phaeomelanin (red/yellow), via regulation of cAMP signaling in melanocytes.
|
Q864H9
|
Q9L7S0
|
SQUU_SALTY
|
3-sulfolactaldehyde reductase
|
Salmonella
|
MAVIAFIGLGQMGSPMASNLLKQGHQLSVFDVNPDAVQRLVDKGAQPASSPAQATIGAEFVITMLPNGDLVRSVLFGEQGVCETLSREALVIDMSTIHPLQTDNLIADMQSKGFSMMDVPIGRTSDNAITGTLLLLAGGTAEQVERATPVLMAMGNELVNTGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAGKGHFTTTWPNKVMKGDLSPAFMIDLAHKDLGIALDVANQLHVPMPLGAASREVYNLARAAGRGREDWSAILEQVRISAGLTANVKK
|
Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS).
|
Q9L7S0
|
Q64FU1
|
IL23A_HORSE
|
Interleukin-23 subunit p19
|
Equus
|
MLGSRAVLLLLLLLWPRTAQARAVPGGSSPAWAQCQQLSQKLCTLAWSAHPPMGHVDLPREEGDAETTNDVPHIQCEDGCDPEGLRDNSQPCLQRIHQGLVFYEKLLGSDIFTGEPSLLPNGPVDQLHASLLGLRQLLQPEGHHWETEQIPSPSPSQPWQRLLLRPKILRSLQAFVAVAARVFAHGAATLTP
|
Associates with IL12B to form the pro-inflammatory cytokine IL-23 that plays different roles in innate and adaptive immunity. Released by antigen-presenting cells such as dendritic cells or macrophages, binds to a heterodimeric receptor complex composed of IL12RB1 and IL23R to activate JAK2 and TYK2 which then phosphorylate the receptor to form a docking site leading to the phosphorylation of STAT3 and STAT4. This process leads to activation of several pathways including p38 MAPK or NF-kappa-B and promotes the production of pro-inflammatory cytokines such as interleukin-17A/IL17A. In turn, participates in the early and effective intracellular bacterial clearance. Promotes the expansion and survival of T-helper 17 cells, a CD4-positive helper T-cell subset that produces IL-17, as well as other IL-17-producing cells.
|
Q64FU1
|
Q30KK1
|
DB127_PANTR
|
Defensin, beta 127
|
Pan
|
MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGHCRKICRVNEVPEALCENGRYCCLNIKELEACKKITKPSHPKPATLALTLQDYVTIIENFPSLKTQST
|
Has antibacterial activity.
|
Q30KK1
|
Q0I5A5
|
IOLE_HAES1
|
2-keto-myo-inositol dehydratase
|
Histophilus
|
MKAENVKLGIAPIGWTNDDLPEIGKENTFEQCVSEMALAGFTGSEVGSKYPRDIDVLKRKLDLRGIQICNAWFSTFFVDGKKEETIKGFIEHRDFLHAMGAKVIGCSEQSRSIQGQKKAIFKEKTIFTEAEWQLLAEGYNELAKLAAEKGMKVCLHHHMGTGIQTPAEIDKYMEITNDDVYLLFDSGHLYYSEGSQQVMLEVLEKYIHRVVHVHLKDVRDEVVAEVKANDLSFLEGVVKGTFTVPGDGVIDFKPIFDILEKYDYKGWMVVEAEQDPAIANPLEYAIKGRQYIREVAGV
|
Catalyzes the dehydration of inosose (2-keto-myo-inositol, 2KMI or 2,4,6/3,5-pentahydroxycyclohexanone) to 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione (D-2,3-diketo-4-deoxy-epi-inositol).
|
Q0I5A5
|
Q58868
|
METE_METJA
|
Methylcobalamin:homocysteine methyltransferase
|
Methanocaldococcus
|
MITTVVGSYPVVKKEETFLDKVKKVFGLYDEYKYAIERAVKDQVKAGVNIISDGQVRGDMVEIFTNNMYGFDGKRVVGRVEFIKPITLKDILYAKSIAKKLNPNVEIKGIITGPCTIASSVRVESCYSDNRDENLIYDIAKALRKEVEALKKHVPIIQIDEPILSTGMYDFDVARKAIDIIVDGLNIKFAMHVCGNVYNIIDELNKFNVDILDHEFASNKKNLVILESMEKKVGFGCVNTKVKKVESVEEIKSLIEEGIEILKNNEKLNKNLSDNILIDPDCGMRLLPIDVAFNKLKNMVEATKLIKI
|
Catalyzes the transfer of a methyl group to L-homocysteine resulting in methionine formation. Can use methylcobalamin and methylcobinamide as methyl donors, but methylcobalamin is not considered to be the physiological substrate.
|
Q58868
|
A7FGU1
|
RLMF_YERP3
|
rRNA adenine N-6-methyltransferase
|
Yersinia
|
MLSYAPENAYQRASTMENKKVFPKEKSGLHPRNRHRSRYDFDALSVSCPELIPFLAPTAYGDISVDFADPLAVKMLNKALLKHFYGIEYWDIPADSLCPPIPGRADYVHHLADLLASCNGEVIPKGKNIALLDIGVGANCIYPIIGQREYGWRFTGTDIDSHALSAAKMVVSMNPTLKNTLRLKQQKDPHAIFEGVWAVNERYDATLCNPPFHGSAEEAAATTRRKLHKLGKNEVAAKPVQNFGGKNSELWCEGGEEGFVSRMVAESVAKAQNCFWFTSLISKKTTLPAIYHALRYVKAVEVRTIEMAQGQKVSRFVAWTFLTPEQQAAWVAERWA
|
Specifically methylates the adenine in position 1618 of 23S rRNA.
|
A7FGU1
|
Q0AE34
|
RNH_NITEC
|
Ribonuclease H
|
Nitrosomonas
|
MQLKSDMKRVEIFTDGACKGNPGPGGWGVCLHFNGETREFFGGEPVTTNNRMELLAAIRALQELESLEDNGQQHLQVQLHTDSQYVQKGISEWIHGWKKRGWRTADKKPVKNEALWRELDDLSQRHQVEWFWVRGHNGHAGNERADRLANQGVESVLSKKAD
|
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
|
Q0AE34
|
Q9NZC9
|
SMAL1_HUMAN
|
Sucrose nonfermenting protein 2-like 1
|
Homo
|
MSLPLTEEQRKKIEENRQKALARRAEKLLAEQHQRTSSGTSIAGNPFQAKQGPSQNFPRESCKPVSHGVIFKQQNLSSSSNADQRPHDSHSFQAKGIWKKPEEMPTACPGHSPRSQMALTGISPPLAQSPPEVPKQQLLSYELGQGHAQASPEIRFTPFANPTHKPLAKPKSSQETPAHSSGQPPRDAKLEAKTAKASPSGQNISYIHSSSESVTPRTEGRLQQKSGSSVQKGVNSQKGKCVRNGDRFQVLIGYNAELIAVFKTLPSKNYDPDTKTWNFSMNDYSALMKAAQSLPTVNLQPLEWAYGSSESPSTSSEGQAGLPSAPSLSFVKGRCMLISRAYFEADISYSQDLIALFKQMDSRRYDVKTRKWSFLLEEHSKLIAKVRCLPQVQLDPLPTTLTLAFASQLKKTSLSLTPDVPEADLSEVDPKLVSNLMPFQRAGVNFAIAKGGRLLLADDMGLGKTIQAICIAAFYRKEWPLLVVVPSSVRFTWEQAFLRWLPSLSPDCINVVVTGKDRLTAGLINIVSFDLLSKLEKQLKTPFKVVIIDESHFLKNSRTARCRAAMPVLKVAKRVILLSGTPAMSRPAELYTQIIAVKPTFFPQFHAFGLRYCDAKRMPWGWDYSGSSNLGELKLLLEEAVMLRRLKSDVLSQLPAKQRKIVVIAPGRINARTRAALDAAAKEMTTKDKTKQQQKDALILFFNRTAEAKIPSVIEYILDLLESGREKFLVFAHHKVVLDAITQELERKHVQHIRIDGSTSSAEREDLCQQFQLSERHAVAVLSITAANMGLTFSSADLVVFAELFWNPGVLIQAEDRVHRIGQTSSVGIHYLVAKGTADDYLWPLIQEKIKVLAEAGLSETNFSEMTESTDYLYKDPKQQKIYDLFQKSFEKEGSDMELLEAAESFDPGSASGTSGSSSQNMGDTLDESSLTASPQKKRRFEFFDNWDSFTSPL
|
ATP-dependent annealing helicase that binds selectively to fork DNA relative to ssDNA or dsDNA and catalyzes the rewinding of the stably unwound DNA. Rewinds single-stranded DNA bubbles that are stably bound by replication protein A (RPA). Acts throughout the genome to reanneal stably unwound DNA, performing the opposite reaction of many enzymes, such as helicases and polymerases, that unwind DNA. May play an important role in DNA damage response by acting at stalled replication forks.
|
Q9NZC9
|
A8GMB6
|
DAPB_RICAH
|
4-hydroxy-tetrahydrodipicolinate reductase
|
spotted fever group
|
MINIGLSGSTGKMGKTILARIDKFKDCKISAKFNSTDDLDDLNNFCKNSDVIIDFSTPEILEKLINYALKHNTKLVIGTTGLQPKHFKLLEKAAKTLPILYSANMSTGANLLSYLAKKATKILDDYDIEILETHHRNKKDSPSGTAIMLAETIAREKGLNIVFNRGNRPRSEKEIGISSLRGGNVHSIHEISLLGDDEIITLKHEALNKNSFVIGAIKSAIWLQDKSPALYSMQDIYNYSLQKQL
|
Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate.
|
A8GMB6
|
B3QH88
|
GLPK_RHOPT
|
Glycerokinase
|
Rhodopseudomonas
|
MPFVMAIDQGTTSSRAILFRSDISIAASAQQEFPQHFPASGWVEHEPEDIWATTIATCRAAMDKAGATAADIAAIGITNQRETVVVWDAVSGQAIHRAIVWQDRRTAEFCTRLKAEGLEPMVTAKTGLIIDPYFSGTKVAWLLDNVPGARARAERGELKFGTVDCYLLWRLTGGKVHATDATNASRTLLFNIHDGAWDDELLKLLGVPRSMLPEVKDSSAHFGDSVPELFGGSITIRGIAGDQQAATIGQACFTPGMIKSTYGTGCFALLNTGATPVKSNNKLLTTVAYQLGGKRTYALEGSIFVAGSAVQWLRDGLGVIKHASETGPLADKSDSAQSVYLVPAFVGMGAPYWNPRVRGALFGLTRNTGPAELAHAALESVCYQTFDLWAAMRADWPDADAATTVLRVDGGMTASDWTMQRLADLLDAPVDRPVIQETTALGAAYLAGLSAGVFPEPQKFADNWRLDHRFRPAMSAATRERKLAGWARAVRGLLATDEGE
|
Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
|
B3QH88
|
A0T0B7
|
PETD_PHATC
|
17 kDa polypeptide
|
Phaeodactylum
|
MSVIKKPDLTDPKLRAKLAKGMGHNYYGEPAWPNDLLYVFPLTMLGTLTCIVGLSVLAPTQLGEPADPFNTPLEILPEWYFFPTFNLLRVLPNKLLGVLAMAAVPLGLITVPFIENVNKFQNPFRRPLASLTFIFGFFTAVWLGIGACVPIDKAISLGFW
|
Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
|
A0T0B7
|
Q7VI82
|
ACCA_HELHP
|
Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha
|
Helicobacter
|
MATYLDFEQKIKNLQDDIESAIISGDNDAISILEKELEKEVSSVYSNISDYQKLQLARHPDRPYAMDYIESILKNPYEINGDRHFKDDKAIVCFLGKIGEQTTMIIGEEKGRGTKNKLARNFGMPSPEGYRKALRAAKLAEKFHIPILMLVDTQGAYPGLGAEERGQSEAIARNLQEFAKLKTPTIAVVIGEGGSGGALAIAVADKLAMMQYSIFSVISPEGCAAILWNDPSKIESATKALKITPIELKKCGLIDDVINEPLIGAHRDKESAAKAIESYFLKAFEEISQDDNYLNKRYQKLMNYGAFS
|
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.
|
Q7VI82
|
A0A0S1TP26
|
C76H2_SALPM
|
Ferruginol monooxygenase
|
Salvia incertae sedis
|
MLQLGSQPHETFAKLSKKYGPLMSIHLGSLYTVIVSSPEMAKEIMHKYGQVFSGRTIAQAVHACDHDKISMGFLPVGAEWRDMRKICKEQMFSHQSMEDSQNLRKQKLQQLLDYTQKCSEEGRGIDIREAAFITTLNLMSATLFSMQATEFDSKVTMEFKEIIEGVASIVGVPNFADYFPILRPFDPQGVKRRADVYFGRLLGLIEGYLNERIEFRKANPNAPKKDDFLETLVDALDAKDYKLKTEHLTHLMLDLFVGGSETSTTEIEWIMWELVASPEKMAKVKAELKSVMGGEKVVDESMMPRLPYLQAVVKESMRLHPPGPLLLPRKAESDQVVNGYLIPKGTQVLINAWAMGRDSSLWKNPDSFEPERFLDQKIDFKGTDYELIPFGSGRRVCPGMPLANRILHTVTATLVHNFDWKLERPEANDAHKGVLFGFAVRRAVPLKIVPIKA
|
Monooxygenase involved in the biosynthesis of labdane-related diterpenes natural products . Catalyzes the oxidation of abietatriene to produce ferruginol . Ferruginol is an intermediate in the biosynthesis of carnosate, a potent antioxidant . May also convert miltiradiene into 11-oxomiltiradiene .
|
A0A0S1TP26
|
B3PUN6
|
ACPS_RHIE6
|
4'-phosphopantetheinyl transferase AcpS
|
Rhizobium
|
MIIGIGSDLIDIRRVEKSIERFGERFTHRCFTEIERARSDRRANRAESYAKRFAAKEACSKALGTGLAQGVFWKDMGVVNLPSGKPTMVLSGGAAVILESMLPAGHRAAIHLTITDDYPLAQAFVIIEALPESL
|
Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein.
|
B3PUN6
|
F4KAK5
|
PSD2_ARATH
|
Phosphatidylserine decarboxylase 2 alpha chain
|
Arabidopsis
|
MGNGNSREAKESRRSRLRHKLQKFRIHRRHLRSSRNSAGMVIQRTVSAEDFSGIALLTLIGAEMKFKDKWLACVSFGEQTFRTEISDTTQKPIWNSEKKLLLEKNGPSLARVSVFETNRVARNKIIGYCELDIFDFVVQEPESTCKSFNLLDPTSSNVVGSIFLSCAIEDPVETERRFAKRILSIVDYNEDGQLSFSEFSDLIKAFGNLVAANKKEELFKAADLNGDGVVTIDELAALLALQQEQEPIINNCPVCGEALQVSDKLNAMIHMTLCFDEGTGNQVMTGGFLTDRQASYGWMFKLSEWTHLSTYDVGLNTGSSASYIVVIDRKSKRLVEELIDSKIVLSMRAIYQSKIGLRLMDQGAKEILQRLSEKQGKKMSSVESAQKIPRFLEFFKDQINMAEVKYPLQHFKTFNEFFIRELKPGARPIACMNRNDVAVCAADCRLMAFQSVEDSTRFWIKGKKFSIRGLLGKNVNPNAFLDGSLVIFRLAPQDYHRFHVPVSGVIEQFVDVSGSLYTVNPIAVNSKYCNVFTENKRTVAIISTAEFGKVAFVAIGATMVGSINFVRKEGEHVKKGDELGYFSFGGSTVICVFEKDAIGIDNDLLVNSGRSLETLVSVGMQLGVSTRTFARSTLI
|
Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. Contributes only to a minor proportion of PtdEtn production.
|
F4KAK5
|
Q3SLN3
|
RL18_THIDA
|
50S ribosomal protein L18
|
Thiobacillus
|
MNTKQSRIRRARKTRAKIAAVKAIRLAIHRTNSHIYAQIISADGGTVMASASSNDKDLRGQLANGGTTAAAAAVGKRLAEKAKGLGIEKVAFDRAGFKFHGRVKALAEAAREGGLAF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
Q3SLN3
|
A1USL8
|
RS19_BARBK
|
30S ribosomal protein S19
|
Bartonella
|
MVRSVWKGPFVDGYLLGKAEKVRASGRNEVIKIWSRRSTILPQFVGLTFGVHNGNKHIPVFVSEEMVGHKFGEFAPTRTYYGHGADKKAKRK
|
Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
|
A1USL8
|
Q91WN4
|
KMO_MOUSE
|
Kynurenine 3-hydroxylase
|
Mus
|
MASSDTQGKRVAVIGGGLVGALNACFLAKRNFQVDVYEAREDIRVAKSARGRSINLALSYRGRQALKAIGLEDQIVSKGVPMKARMIHSLSGKKSAIPYGNKSQYILSISRENLNKDLLTAVESYANAKVHFGHKLSKCIPEEGVLTVLGPDKVPRDVTCDLVVGCDGAYSTVRAHLMKKPRFDYTQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRNAYMMIALPNMDKSFTCTLFMPFEEFERLPTRSDVLDFFQKNFPDAIPLMGEQALMRDFFLLPAQPMISVKCSPFHLKSHCVLMGDAAHAIVPFFGQGMNAGFEDCLVFDELMDKFNNNLSMCLPEFSRFRIPDDHAISDLSMYNYIEMRAHVNSRWFLFQKLLDKFLHAIMPSTFIPLYTMVAFTRIRYHEAVLRWHWQKKVINRGLFVLGSLIAIGGTYLLVHHLSLRPLEFLRRPAWMGTTGYWTRSTDISLQVPWSY
|
Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid, a neurotoxic NMDA receptor antagonist and potential endogenous inhibitor of NMDA receptor signaling in axonal targeting, synaptogenesis and apoptosis during brain development. Quinolinic acid may also affect NMDA receptor signaling in pancreatic beta cells, osteoblasts, myocardial cells, and the gastrointestinal tract.
|
Q91WN4
|
Q07PK4
|
MIAA_RHOP5
|
Isopentenyl-diphosphate:tRNA isopentenyltransferase
|
Rhodopseudomonas
|
MSVATSDMSGAGPEQAKAVLIAGPTASGKSALALRLAEARGGVVINTDSMQVYRDLRVLTARPTPDEEARAPHRLYGTVDAAQNFSAGAWLDAAAGALAEARRAGAMPIFIGGSGLYFKALTRGLSAVPPIAPEVREAVRERLARDGVAALHAELARCDSEAAARLNVADRSRVARALEVIIATGKPQAAWHAEALPPLLPPSEVLAAVFLAPQREALYARIDARFATMLAEGALDEVAALRARQLDPLLPAMKAHGVPALIRHLDGALSLDEAAAIGCADTRHYAKRQFTWFRHQLPEFCWVAPEEAGNYLGDVIPGRERSERARNP
|
Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A).
|
Q07PK4
|
B9E748
|
TIG_MACCJ
|
PPIase
|
Macrococcus
|
MSVKWEKQEGNEGVLTVTVPAEEVNAGLDKAFKKVVKQVNVPGFRKGKMPRPMFEQRFGVEALYQDALDFILPDAYAAAVEEAGINPVDRPEIDIEQMEKGKELIFTAKVTVEPEVELGDYKGLEVEKEDTEVTEEDLNKAIEADLARKAELVVKEEGEVAEGDVVNLDFDGYVNEEAFEGGKAEGYDLEIGSGQFIPGFEEQLVGTKVGDEKDVTVTFPEEYHAEELAGKEAVFKVKINEVKSKEVPELDDEMAKELDESVDSVDAYKEKYKKDLQEQKTLQAENNMKESLIAQAVENAKVDIPEAMINTELDRMMQEFEQRIAQQGLNLELYYQFSGQTEEQLKESMKADAEARVKTNLTLAAIAKAENIEISDTDVDAELSKMSEQFGLSVDDIKAALGNGEVLKDDLRIQKAIDVLVKESKEK
|
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.
|
B9E748
|
B0SZ20
|
EFTS_CAUSK
|
Elongation factor Ts
|
unclassified Caulobacter
|
MAEVTAALVKELREKSGVGMMDCKKALVENNGDIDASIDWLRAKGLSKAAKKADRVAAEGLVGIVVRAEGAGMIAAAVEVNAETDFLSRNELFQTAVRKIARAGLDNEGVEAISAAKTPDGEVVSDLLTHLIATIGENMVLRRSARFAVAHGAVASYIHNATAPDLGRIGVLVAIEGAGDQTKILELGRKIAMHVAATAPLSLSPDDLDQAAIEKERQIFTEQALESGKPPAVVEKMVEGRIRKFLEEVVLLKQAFVMNPDQTVEQLVAEAGKELGSPLTVKGFVRLALGEGVEKGPEGDFAAEVAAMTGQA
|
Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
|
B0SZ20
|
Q44015
|
YGB4_CUPNE
|
Glyoxylate-induced protein
|
Cupriavidus
|
MPRFAANLSMMYNEHAFLDRFAAAAADGFRAVEFLFPYEHAAAELRARLDANGLTQALFNAAPGDWAAGERGLAALPGREADFRGTIGRALEYAGVIGNDRIHVMAGLIPADADRARCRATYLENLAFAANAAAAQGVTVLIEPINTRDMPGYFLNRQDDGQAICKEVGAANLKVQFDCYHCQIVEGDVAMKLKRDIAGIGHIQIAGVPERHEPDVGELNYPYLFEVMDTLGYDGWIGCEYRPRAGTSAGLGWLKPYLGR
|
Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
|
Q44015
|
Q03KS5
|
PYRE_STRTD
|
Orotate phosphoribosyltransferase
|
Streptococcus
|
MTLASQIASDLLDIKAVYLKPEEPFTWASGIKSPIYTDNRITLSYPETRTLIENGFVKKIKEEFPEVEVIAGTATAGIPHGAIIADKMNLPFAYIRSKPKDHGAGNQIEGRVVKGEKMVVVEDLISTGGSVLDAVAAAEREGADVIGVVAIFTYELPKAEKNFAEAGVKLVTLSNYTELIKVAKVKGYITADGLQLLKKFKENQETWQD
|
Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
|
Q03KS5
|
A5EXW8
|
RPOZ_DICNV
|
Transcriptase subunit omega
|
Dichelobacter
|
MARVTVEDCLIHENSRFRLVLAASKRARQLTLGHQPLVAPENDKPTVLALREIEEGKVTVQGLLDGQDVSEHLARQA
|
Promotes RNA polymerase assembly. Latches the N- and C-terminal regions of the beta' subunit thereby facilitating its interaction with the beta and alpha subunits.
|
A5EXW8
|
Q27896
|
TRF_DROME
|
TBP-related factor
|
Sophophora
|
MQFHFKVADAERDRDNVAATSNAAANPHAALQPQQPVALVEPKDAQHEIRLQNIVATFSVNCELDLKAINSRTRNSEYSPKRFRGVIMRMHSPRCTALIFRTGKVICTGARNEIEADIGSRKFARILQKLGFPVKFMEYKLQNIVATVDLRFPIRLENLNHVHGQFSSYEPEMFPGLIYRMVKPRIVLLIFVNGKVVFTGAKSRKDIMDCLEAISPILLSFRKT
|
May be essential for embryonic development.
|
Q27896
|
Q12J93
|
MUTL_SHEDO
|
DNA mismatch repair protein MutL
|
Shewanella
|
MPIHILPPQLANQIAAGEVVERPASVVKELVENSLDAGATRVDIDIDKGGSKLIRIRDNGSGIPKDELALALSRHATSKVHSLDDLEAILSFGFRGEALASISSVARLTLTSKTAEQTEAWQAHAEGSQMDVSLMPAAHPQGSTIEVVDLFFNTPARRRFLKSDKTEFTHIDEWLKRIAIVRTDIHFSLTHNGKLVRQYRAANTDIQMQQRLSQICGRAFAEQAITLACEHDGLSLEGYIQSPHDNSVTDTNYFYVNGRLVRDKLVNHAVRQAFAEHQWHQQPSYVLKLTLDPHQVDVNVHPAKHEVRFHQSRYVHDFILQALQSALAQFPAKGSQAEYDFEQDNGSLEATAASNPDNGLSPSRGHAEEGDFSNSVAYAANAASVHRGSTSSERKASAGVSQFGRIPSSQGDYQPQDNSRYTPKRYSTNAASTNTASNYSHSTSAPVSRQALEGYAQLLATPEIVSSSNQYVADKNQEFKDVNESGSTPKVAAMPAVLAGQYWVITQGECLRLLPLQAVRLWLRQKEISHKLPTGLVSQPLLMPVAVKADKHWGEILLERESLLRQLGLELTIRYQQLIIKKVPPYLRESQLAVLIPELLQWVEHQVPAIPALSAWLAKHGQKHEQSLTDTWEGFCLLSEPEQQVLLEKAKVLPWQAWLEESQSE
|
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.
|
Q12J93
|
P0CT93
|
ORDA_ASPFL
|
Cytochrome P450 64
|
Aspergillus subgen. Circumdati
|
MIYSIIICAGALLGLWILEKLLAPKDTRPPLPPGPWRKPIIGNLTDFPPKGTPEWLFWAKHQERYGPMSSLEVMGQTIIMINDAQLGIEIMHKKSALSQMIPDAPFAHMAGWGMSLATERNRQAWKTIRANMKQEIGTRRAISTFHPKMEIGIRRFLLRTLDNPDDLRFHIRKEANAFMMDVAYGYTIAPHGKDELYDLTQQSVRQFSHIFSPGEWSVNFFPILRYVPSWFPGASFQIKAAEYKRTIERMTMVPYLWIKDQVARGCSRPSILLRLLQKGHYESGSHQEQVLVWTNAEFVMGGSDTTVSAVSSFFVAMALYPEVQRKAREELDRVVGPTTLATFEHRSQLPFIDALVKEVFRWHPASPLGAPHITQEDQIWDGYLLPKGALLLPNIWTFTHDPSVYHDPMVFKPERFLEGKDSPPETDPMKFVFGFGRRICPGRFVTDEKLFLIACHAVSCFFISPKDPGAPEPDWLPGVISQPGAFDLNVVPRSPAHEELIRSIETDHPWKNADATDISRFMARNQMI
|
Converts O-methylsterigmatocystin (OMST) to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway.
|
P0CT93
|
Q48544
|
PEPR_LACDL
|
HTH-type transcriptional regulator pepR1
|
Lactobacillus
|
MNKQDVTIYDVAREAKVSMATVSRVVNGNNNVRKETRDRVMEVIKRLHYQPNAVAQGLASKRTTTVGLIVPDLTNLYFAELSKGIDDIAVLYKYNIIISSVENRLMKEDAVIQGLLNKQVDGVIYMSNKLSEEAAEAFKRTDTPVVLAGTVSDNLEFPSVNIDYKKADTEALNLLLNDGKKKLALIVGDKEASINRNYRIPAFEKFVADNELEGCEIFDNIKDYSDGYNLYPELAKKGINGAIITKDVSSVGLLNSALDRGAKVPEDFEIITASATQIASVVRPALTTIKQPLYDLGAVAMRMLTKLMNDESLEDKHIILPYELIKKQSTLNK
|
Transcriptional regulator of the pepQ gene for prolidase.
|
Q48544
|
P07143
|
CY1_YEAST
|
Ubiquinol-cytochrome c oxidoreductase cytochrome c1 subunit
|
Saccharomyces
|
MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAEAMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFVFNPPKPRK
|
Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c (Probable). Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c .
|
P07143
|
B4F766
|
DYM_RAT
|
Dymeclin
|
Rattus
|
MGSNSSKISDLPKNEYLKRLSGPEAISENDPFWNQLFSFSFSAPTSSTELKLLEEATISVCKSLVENNPRTGNLAALTKVFLARTRELRLSAECQNHIFIWQTHNALFIICCLLKVFICEMSEEELQLHFTYEEKLPGTYTLCVLLGSDSEDLLEELLCSLIQLITDTPLLDITYEISVEAISAMIVFLSCQLFHKEVLRQSISHKYLMQGPCLPYTSKLVKTLLYNFIRQEKPPPPGTHVFPQQSDGGGLLYGLASGVATGLWTVFTLGGVGSKAASPELTSPLANQSLLLLLVLVNLTDAPDIPNPYRQAVTSFKNTQDSSPFPSSVPHTFQINFNSLYTTLCEQQTSDQATLLLYTLLHQNANVRTYMLARTDMENLVLPILEILYHVEERNSHHVYMALIILLILTEDDGFNRSIHEVILKNITWYSERVLTEISLGSLLILVVIRTIQYNMTRTRDKYLHTNCLAALANMSAQFRSLHQYAAQRIISLFSLLSKKHNKVLEQATQSLRGSLSSSDVPLPDYAQDLSVIEEVIRMMLEIINSCLTNSLHHNPNLVYALLYKRDLFEQFRTHPSFQDIMQNIDLVISFFSSRLLQSGAELSVERVLEIIKQGVVALPKDRLKKFPELKFKYVEEEQPEEFFIPYVWSLVYNSAVGLYWNPQDIQLFAMDSD
|
Necessary for correct organization of Golgi apparatus. Involved in bone development.
|
B4F766
|
Q5RDV8
|
METL6_PONAB
|
Methyltransferase-like protein 6
|
Pongo
|
MASLQRKGLQARILTSEEEEKLKRDQTLVSDFKQQKLEQEAQKNWDLFYKRNSTNFFKDRHWTTREFEELRSCREFEDQKLTMLEAGRGVGNCLFPLLEEDPNIFAYACDFSPRAVEYVKQNPLYDTERCKVFQCDLTKDDLLDHVPPESVDVVMLIFVLSAVHPDKMHLVLQNIYKVLKPGKSVLFRDYGLYDHAMLRFKAGSKLGENFYVRQDGTRSYFFTDEFLAQLFMDTGYEEVVNEYVFRETVNKKEGLCVPRVFLQSKFLKPPKNPSPVVPGPGS
|
S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Ser), including tRNA(Ser)(UGA) and tRNA(Ser)(GCU). Interaction with SARS1/SerRS is required for N(3)-methylcytidine methylation.
|
Q5RDV8
|
Q9CW73
|
B3GA1_MOUSE
|
UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
|
Mus
|
MPKRRDILAIVLIVLPWTLLITVWHQSSLAPLLAVHKDEGSDPRHEAPPGADPREYCMSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSTQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
|
Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group.
|
Q9CW73
|
P46182
|
RL18_BUCAK
|
50S ribosomal protein L18
|
unclassified Buchnera (in: Bacteria)
|
MDKKSARIRRATRARRKLKELGATRLVVHRSPRHMYAQVIAPNGSEVLVAASTLEKAITEQLKYSGNKDAAAAVGKALAERALEKGIAKVSFARSGFQYHGRVQALADAAREAGLQF
|
This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
|
P46182
|
Q32B99
|
AAEB_SHIDS
|
p-hydroxybenzoic acid efflux pump subunit AaeB
|
Shigella
|
MGIFSIANQHIRFAVKLATAIVLALFVGFHFQLETPRWAVLTAAIVAAGPAFAAGGEPYSGAIRYRGFLRIIGTFIGCIAGLVIIIAMIRAPLLMILVCCIWAGFCTWISSLVRIENSYAWGLAGYTALIIVITIQPEPLLTPQFAVERCSEIVIGIVCAIMADLLFSPRSIKQEVDRELESLLVAQYQLMQLCIKHGDGEVVDKAWGDLVRRTTALQGMRSNLNMESSRWARANRRLKAINTLSLTLITQSCETYLIQNTRPELITDTFREFFDTPVETAQDVHKQLKRLRRVIAWTGERETPVTIYSWVAAATRYQLLKRGVISNTKINATEEEILQGELEVKVESAERHHAMVNFWRTTLSCILGTLFWLWTGWTSGSGVMVMIAVVTSLAMRLPNPRMVAIDFIYGTLAALPLGLLYFLVIIPNTQQSMLLLCISLAVLGFFLGIEVQKRRLGSMGALASTINIIVPDNPMTFHFSQFLDSALGQIVGCVLAFTVILLVRDKSRDRTGRVLLNQFVSAAVSAMTTNVARRKENHLPALYQQLFLLINKFPGDLPKFRLALTMIIAHQRLRDAPIPVNEDLSAFHRQMRRTADHVISARSDDKRRRYFGQLLEELEIYQEKLRIWQAPPQVTEPVHRLAGMLHKYQHALTDS
|
Forms an efflux pump with AaeA. Could function as a metabolic relief valve, allowing to eliminate certain compounds when they accumulate to high levels in the cell.
|
Q32B99
|
Q2RJT7
|
NUON_MOOTA
|
NDH-1 subunit N
|
Moorella
|
MANLHLLTVEILTAALGLGLLALGLLVPHSDRRGIAYVATAGLAGILAAAFGMREASGVVLGGYVIDPFGTYFKILFLVAAMLTAACSYDYVEKMGLNQGEYYALLVLATLGMMVLASSGELVSLYLGLELMTITFCILAAFHLGDAKSAEAGIKYVLLGAMSSAIFLYGLSLVYGSSGTTVIREIGQAVATRGASPALLLGTIFILAGFAFKVTAVPFHMWSPDVYEGAPTPVTGFLSVASKAAAFAALVRVFFGALPDLHSFWVQLFIALAVLTIVLGNLVAIPQTNIKRLLAYSSIAQAGYLLLGIVSFSVLGVGAVMYYAMLYVFGNMGAFMAATAFYNNDGSDEIKDYAGLARRSPLVAALMLFSLLSLAGIPPMAGFVGKFYLFMSIISRQYIWLAILGILMSMVSVYYYLLVAKAMYLGNPPEGSKPLRVAPGLQVAMVVSLLILFILGIYPTPLTNYAMNSAVTFFMP
|
NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
|
Q2RJT7
|
B2RHB7
|
GPMA_PORG3
|
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase
|
Porphyromonas
|
MKRIVLIRHGESLWNKENRFTGWTDVDLSEKGIEEAKKAGELMKKEGFQFTKAYTSYLKRAVKTLNGVLDVMDLDWIPVEKTWRLNEKHYGMLQGLNKAETAEKYGDEQVLIWRRSYDVPPTPMEKEDPRSPFMDPRYKGVCEKDLPLTEALCDTVNRILPYWNETIFPTLKEHDEVLVAAHGNSLRGIIKVLKNISDEDIISLNLPTAVPYVFEFDDNLRLVKDYFLGDPEEIKKLMEAVANQGKKK
|
Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.
|
B2RHB7
|
Q9VEU6
|
GCYDA_DROME
|
Soluble guanylate cyclase 89Da
|
Sophophora
|
MYGMLYESVQHYVQEEYGVDIWRKVCHIIDCKHNSFKTHQIYPDKLMPDIAEALSACTGESFDFCMNFFGRCFVRFFSNFGYDKMIRSTGRYFCDFLQSIDNIHLIMRFTYPKMKSPSMQLTNMDDNGAVILYRSSRTGMSKYLIGQMTEVAREFYGLEIKAYVIESQNDISGGTAGPIKLTDGPLTVIVKYRLDFDNREYMAKRVNTEAHPSQLKMPTVKLDVFLDLFPFTFVLNHDMKITHAGEKIVETWIMHNPGANPKSFIGTHVMDLFQCRRPKDTTIDWDTLIQMRAVLFEFELIRTGHNRAAYDAVLNMDFENYDEMDLNEAQTMALAKAQEFSESHPVDDDESAREDEIDPATGERRSSQGLRSILLKGQMFYIKDVDSLIFLCSPLIENLDELHGIGLYLNDLNPHGLSRELVMAGWQHCSKLEIMFEKEEQRSDELEKSLELADSWKRQGDELLYSMIPRPIAERMRLSEEQVCQSFEEVSVIFLEVMNVYDEGLNSIQGAMQTVNTLNKVFSALDEEIISPFVYKVETVGMVYMAVSGAPDVNPLHAEHACDLALRVMKKFKAHDMGDVAIRVGINSGPVVAGVVGQKVPRYCLFGDTVNTASRMESSSDPWKIQLSKYTGDKVRQVGYKVESRGTVQVKGKGDMETYWLLEGPEG
|
Heterodimers with Gyc-89Da and Gyc-89Db are activated in response to changing oxygen concentrations, alerting flies to hypoxic environments. Under normal oxygen concentrations, oxygen binds to the heme group and results in low levels of guanylyl cyclase activity. When exposed to reduced oxygen concentrations, the oxygen dissociates from the heme group resulting in activation of the enzyme.
|
Q9VEU6
|
P50433
|
GLYM_SOLTU
|
Serine methylase
|
Solanum
|
MAMAIALRRLSATVDKPVKSLYNGGSLYYMSSLPNEAVYDKEKSGVAWPKQLNAPLEVVDPEIADIIEHEKARQWKGLELIPSENFTSVSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFRLDPAKWGVNVQPLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDESTGYIDYDQLEKSATLFRPKLIVAGASAYARLYDYDRIRKVCNKQKAILLADMAHISGLVAAGVIPSPFDYADVVTTTTHKSLRGPRGAMIFYRKGVKEVNKQGKEVFYDYEDKINQAVFPGLQGGPHNHTITGLAVALKQATTPEYRAYQEQVLSNSSKFAQALGEKGYELVSGGTDNHLVLVNMKNKGIDGSRVEKVLEAVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFLEEDFVKVADFFDAAVKIAVKVKAETQGTKLKDFVATLESSAPIKSEIAKLRHDVEEYAKQFPTIGFEKETMKYKN
|
Catalyzes the interconversion of serine and glycine.
|
P50433
|
O34295
|
TTUC5_AGRVI
|
D-malate dehydrogenase [decarboxylating]
|
Agrobacterium
|
MREYKIAAIPADGIGPEVIAAGLQVLEALEQRSGDFKIHTETFDWGSDYYKKHGVMMPADGLDKLKKFDAIFFGAVGAPDVPDHITLWGLRLPICQGFDQYANVRPTKILPGITPPLRNCGPGDLDWVIVRENSEGEYSGHGGRAHRGLPEEVGTEVAIFTRVGVTRIMRYAFKLAQARPRKLLTVVTKSNAQRHGMVMWDEIAAEVATEFPDVTWDKMLVDAMTVRMTLKPETLDTIVATNLHADILSDLAGALAGSLGVAPTANIDPERRFPSMFEPIHGSAFDITGKGIANPIATFWTAAQMLEHLGERDAAARLMGAVERVTEAGILTPDVGGTANTSQVTEAVCNAIAGSNII
|
Has multiple catalytic activities. Apart from catalyzing the oxidation of (+)-tartrate to oxaloglycolate, also converts meso-tartrate to D-glycerate and catalyzes the oxidative decarboxylation of D-malate to pyruvate.
|
O34295
|
B0SEH8
|
DAPAT_LEPBA
|
LL-diaminopimelate aminotransferase
|
Leptospira
|
MTQINENYLKLKAGYLFPEIGRRVKAYSDANQNAKIIRLGIGDVTLPLAPTIVNAMVDAAKEMGSAGGFHGYGPEQGYSFLIQKIIAHDYTARGVQIAEDEVFVSDGSKCDCGNIQEIFSLDSKIAVVDPVYPVYVDTNVMAGRTGEVGPDGRYANIVYMPATEENNFEPDFPKEKADIIYLCYPNNPTGMVATKARLTEWVNYAKKMGSIILYDSAYESFIQDPEIPKSIYEIPGAKEVAMEFRSFSKTAGFTGTRCAYLVIPKDLKGKTKSGEEVSFNSLWNRRHTTKFNGVSYITQKGAEAVFSAQGQVEIKEQISYYMENAKLIREGLVKAGYTVFGGTNAPYIWLKTPRGLKSWEFFDELLGTAQVVGTPGSGFGPAGEGYFRLSAFGKREDVISAIERIQKM
|
Involved in the synthesis of meso-diaminopimelate (m-DAP or DL-DAP), required for both lysine and peptidoglycan biosynthesis. Catalyzes the direct conversion of tetrahydrodipicolinate to LL-diaminopimelate.
|
B0SEH8
|
B2UL21
|
RL25_AKKM8
|
General stress protein CTC
|
Akkermansia
|
MATSHSLKAETRACGSGNLKQLRSQGLVPGVVYGPGFDNVNIQVDAREFARMLASAVSEHILVALDINGKIVKVLLKEVQHNPITNACLHVDFQAVTDTTVIHSIVPVILEGDSAGVALGGVLDQTIHELAIICQVKDLPEAITADISGLKLGESLRITDLKLPSGVTTELAGDVIVAIVEAPRVSGEEAAPAAEEAVAEK
|
This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance.
|
B2UL21
|
C6D8X1
|
GCSP_PECCP
|
Glycine dehydrogenase (aminomethyl-transferring)
|
Pectobacterium
|
MTQTLSQLEHDGAFIERHIGPSVSQQQHMLSVVGATSLDALIRQIVPQDIQLPSPPAVGEAATEHEALSELKAIAGRNQRYKSYIGMGYSAVLMPPVILRNVLENPGWYTAYTPYQPEVSQGRLEALLNFQQVTQDLTGLDLASASLLDEATAAAEAMAMAKRISKLKQAERFFVADDVHPQTLDVVRTRAETFGFEIVVGKAEDALKDDAVFGVLLQQVGTTGELHDYSDLMAALKARKVVSCVASDIMALVLLTAPGKQGADIVFGSAQRFGVPMGYGGPHAAFFACRDEHKRAMPGRIIGVSRDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIAGMYAVFHGPEGLKRIAGRIHRLTDILAAGLTQGGLLLRHRSWFDTLTIEVADKDAVLSRALSFGINLRSDLASAVGITLDEATTREDVLALFAVLLGDDHGLDIGALDAAISQQAATIPAGLLRQDAILSHPVFNRYHSETEMMRYLHRLARKDLALNQAMIPLGSCTMKLNAAAEMLPITWPEFAELHPFCPPEQALGYRQMIEQLSGWLVQLTGYDAICMQPNSGAQGEYAGLLAIRRYHESRNEAGRHLCLIPSSAHGTNPASAQMAGMDVVVVACDKQGNIDLHDLREKAQAAGEQLSCIMVTYPSTHGVYEETIREVCQIVHQYGGQVYLDGANMNAQVGITTPGYIGADVSHLNLHKTFCIPHGGGGPGMGPIGVKAHLAPFVPGHQVVKIDGVLTEQGAVSAAPFGSASILPISWMYIRMMGAEGLKQASQMAILNANYIATRLQQAYPVLYTGRDGRVAHECILDIRPLKESTGISEMDIAKRLIDYGFHAPTMSFPVAGTLMVEPTESESQVEIDRFVDAMLAIRAEINRVAQGEWPLDDNPLVNAPHTQAELVADWAHPYSRELAVFPAGSEHKYWPSVKRLDDVYGDRNLFCSCVPMSDY
|
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.
|
C6D8X1
|
Q3AMT7
|
RS10_SYNSC
|
30S ribosomal protein S10
|
unclassified Synechococcus
|
MSTAIAQQKIRIRLKAFDRRMLDLSCEKIIETADNTAATAIGPIPLPTKRKIYCVLRSPHVDKDSREHFETRTHRRIIDIYSPSAKTIDALMKLDLPSGVDIEVKL
|
Involved in the binding of tRNA to the ribosomes.
|
Q3AMT7
|
A1W0P5
|
DNAJ_CAMJJ
|
Chaperone protein DnaJ
|
Campylobacter
|
MEISYYELLEITQNADKETIKKAYRKMALKYHPDRNQGDKEAEDKFKLVNEAYEVLSNDEKRAIYDRYGKDALKGGGFGSNSSGFGGFEDLGDIFSSFFGEGFGSSSRRRKSSNDEKIPSDFIFNLKLSFKEAVFGCKKNIDFTYKCSCKTCNGTGAKDGKLQTCPKCQGRGQVGVSQGFITFAQTCPDCQGSGEKASEKCSDCKGLGYNESKDSVELNIPEGVDTGMKLRVNAKGNILKNGTRGDMYVKIIAAEDDTFIRDDDDIYIEFPVFFTQAILGESIKVPTIRGEATLNLPKGAKDGQRFVLEKEGVKDVHSSRMGNQIVQISIKFPTSLNDEQKELLEKLSESFGIKDGMHQEQKGLFEKITNWFKS
|
Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
|
A1W0P5
|
Q0IHM1
|
NLS1_XENTR
|
Major facilitator superfamily domain-containing protein 2A
|
Silurana
|
MEKESENASCAGLLGQKNEPGSPTQSRSGKHKLSVCSKICFAIGGAPYQITGCALGFFLQIFLLDIAQVPPFYASIILFSGRVWDAITDPLVGFFVSKSSWTRLGRLLPWVVFSTPFAVVSYLLIWFVPGFSGVSMVIWYLVFYCLFQTLVTCFHVPYSALTMFISKEQSDRDSATGYRMTVEVLGTVLGTAIQGQIVGRENTPCVEHIRETHLYNTSVIMEDLNITHDVESLSSTRDAYMIAAGVICAIYVLCAIILTLGVREKRDAYELLSDQPFSFWQGLKLVMSHKPYIKLITGFLFTSLAFMLLEGNFALFLTYTMGFRRDFQNILLVVMLSATLTVPFWQWFLTRFGKKTAVYFGISSVIPFLILVVLMESNLILAYVVAVAAGLSVAAAFLLPWSMLPDVIDDFILKNPDSHGHEPIFFSFYVFFTKFASGVSLGISTLSLDFAGYQTRACSQPEQVNLTLKMLICVAPVILILLGLLLFILYPINEEKRKQNKKALQLIRESNRDSDSDSLELASNV
|
Sodium-dependent lysophosphatidylcholine (LPC) symporter, which plays an essential role for blood-brain barrier formation and function. Specifically expressed in endothelium of the blood-brain barrier of micro-vessels and transports LPC into the brain. Transport of LPC is essential because it constitutes the major mechanism by which docosahexaenoic acid (DHA), an omega-3 fatty acid that is essential for normal brain growth and cognitive function, enters the brain. Transports LPC carrying long-chain fatty acids such LPC oleate and LPC palmitate with a minimum acyl chain length of 14 carbons. Does not transport docosahexaenoic acid in unesterified fatty acid.
|
Q0IHM1
|
A1R8T8
|
RL16_PAEAT
|
50S ribosomal protein L16
|
Paenarthrobacter
|
MLIPRRVKHRKQHHPGRSGAATGGTKVSFGEYGIQALSPAYVTNRQIESARIAMTRHIKRGGKVWINIYPDRPLTKKPAETRMGSGKGSPEWWVANVKPGRVLFELSGVNEEVAREALRLAIHKLPLKARIVRREGGE
|
Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs.
|
A1R8T8
|
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