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Database: UniProt
Entry: I3VRC2_THESW
LinkDB: I3VRC2_THESW
Original site: I3VRC2_THESW 
ID   I3VRC2_THESW            Unreviewed;       383 AA.
AC   I3VRC2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143};
DE            EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143};
GN   OrderedLocusNames=Tsac_0029 {ECO:0000313|EMBL:AFK85067.1};
OS   Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485).
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacterium.
OX   NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK85067.1, ECO:0000313|Proteomes:UP000006178};
RN   [1] {ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RA   Brown S.D., Land M.L., Herring C.D.;
RT   "Thermoanaerobacterium saccharolyticum JW/SL-YS485.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AFK85067.1, ECO:0000313|Proteomes:UP000006178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178};
RX   PubMed=24907337; DOI=10.1128/AEM.00998-14;
RA   Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M.,
RA   Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.;
RT   "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in
RT   Thermoanaerobacterium saccharolyticum during the Degradation of
RT   Hemicellulose.";
RL   Appl. Environ. Microbiol. 80:5001-5011(2014).
CC   -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC       {ECO:0000256|RuleBase:RU367143}.
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:0000256|RuleBase:RU367143};
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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DR   EMBL; CP003184; AFK85067.1; -; Genomic_DNA.
DR   RefSeq; WP_014756991.1; NC_017992.1.
DR   AlphaFoldDB; I3VRC2; -.
DR   STRING; 1094508.Tsac_0029; -.
DR   KEGG; tsh:Tsac_0029; -.
DR   PATRIC; fig|1094508.3.peg.30; -.
DR   eggNOG; COG0119; Bacteria.
DR   BioCyc; TSAC1094508:GLMA-32-MONOMER; -.
DR   Proteomes; UP000006178; Chromosome.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07939; DRE_TIM_NifV; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013477; NifV/FrbC.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR02660; nifV_homocitr; 1.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1.
DR   PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   3: Inferred from homology;
KW   Nitrogen fixation {ECO:0000256|RuleBase:RU367143};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          10..261
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   383 AA;  42618 MW;  1AFF34E2BB7368F7 CRC64;
     MKFKKEDGKL YLVDTTLRDG EQTAGVVFAN SEKIRIAKML DEIGVHQLEV GIPTMGGDEK
     ETIAKIAKLG LNASIMAWNR AVVNDVKESL ECGVDAVAIS ISTSDIHIEH KLRTSRQWVL
     DHMTSAVEFA KKDGVYVSVN AEDASRTDMD FLIEFARCAK QAGADRLRFC DTVGILDPFK
     TYDIIKKIKE AIDIDIEMHT HNDFGMATAN ALAGFKAGAN FIGVTVNGLG ERAGNAALEE
     VVMALKHVYK YDINIDTKRF REISEYVSTA SGRQLPSWKA IVGTNVFAHE SGIHVDGALK
     DPHTYEIFDP DEVGLERQIV IGKHSGTAAL INKFKEYGRV LPEEEAKELL PYVRSLSIQL
     KRPLFDKELI YLYEEHISKI KAI
//
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