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HOSA_PYRAB
ID   HOSA_PYRAB              Reviewed;         361 AA.
AC   Q9V1J1; G8ZGD8;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Homocitrate synthase {ECO:0000255|HAMAP-Rule:MF_02222};
DE            Short=HCS {ECO:0000255|HAMAP-Rule:MF_02222};
DE            EC=2.3.3.14 {ECO:0000250|UniProtKB:O87198, ECO:0000255|HAMAP-Rule:MF_02222};
GN   OrderedLocusNames=PYRAB04360; ORFNames=PAB0286;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
CC   -!- FUNCTION: Catalyzes the aldol-type condensation of 2-oxoglutarate with
CC       acetyl-CoA to yield homocitrate. Carries out the first step of the
CC       alpha-aminoadipate (AAA) lysine biosynthesis pathway.
CC       {ECO:0000250|UniProtKB:O87198}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + acetyl-CoA + H2O = (2R)-homocitrate + CoA +
CC         H(+); Xref=Rhea:RHEA:12929, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:58884; EC=2.3.3.14;
CC         Evidence={ECO:0000250|UniProtKB:O87198};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12930;
CC         Evidence={ECO:0000250|UniProtKB:O87198};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O87198};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O87198};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC       pathway; L-alpha-aminoadipate from 2-oxoglutarate: step 1/5.
CC       {ECO:0000250|UniProtKB:O87198}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. Homocitrate synthase LYS20/LYS21 subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_02222}.
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DR   EMBL; AJ248284; CAB49358.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69817.1; -; Genomic_DNA.
DR   PIR; G75159; G75159.
DR   AlphaFoldDB; Q9V1J1; -.
DR   SMR; Q9V1J1; -.
DR   STRING; 272844.PAB0286; -.
DR   EnsemblBacteria; CAB49358; CAB49358; PAB0286.
DR   KEGG; pab:PAB0286; -.
DR   PATRIC; fig|272844.11.peg.461; -.
DR   eggNOG; arCOG02092; Archaea.
DR   HOGENOM; CLU_022158_4_2_2; -.
DR   OMA; DWSNGMR; -.
DR   PhylomeDB; Q9V1J1; -.
DR   UniPathway; UPA00033; UER00028.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_02222; Homocitr_synth_fung_arch; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011872; Homocitrate_synth_fun/arc.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02146; LysS_fung_arch; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Lysine biosynthesis; Magnesium; Manganese;
KW   Metal-binding; Transferase.
FT   CHAIN           1..361
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140419"
FT   DOMAIN          1..251
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   ACT_SITE        282
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         8
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         9
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         68
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         128
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         162
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         188
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O87198"
SQ   SEQUENCE   361 AA;  40827 MW;  C8667A7459954476 CRC64;
     MVLDSTLREG EQTPGVNYTP EQRLEIAIAL DEVGVDFIEI GHPAVSEDVF RGMKLIAEQG
     LNVELLAHSR ALIEDIDYVL KTGVDWVGIF FCLSEACLRK RFRITLDHAL EKISRAIEYA
     KDHGLKVRFT PEDTTRTEWA NLKRAIRLAK ELKVDRISVA DTTGSTHPLR FYTLVKKIVN
     FGIPVNVHCH NDLGLALANA IMGIEAGATL VDATVNGLGE RAGIVDLAQI ITVLYYHYGI
     KKYRLDLLYR VSNLVSEITG ISPQPNYPIV GENAFTHKAG LHVSAVLKDP RFYEFLPAEV
     FGRERTIYVD RYAGKDTIRY YLEKFGIRDH GIVTSLLRKV KSSREPFTWE KLLEEARRVK
     E
 
 
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