ID   NIFV_AZOCH              Reviewed;         382 AA.
AC   P23122;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1885524; DOI=10.1128/jb.173.17.5457-5469.1991;
RA   Evans D.J., Jones R., Woodley P.R., Wilborn J.R., Robson R.L.;
RT   "Nucleotide sequence and genetic analysis of the Azotobacter chroococcum
RT   nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine
RT   acetyltransferase.";
RL   J. Bacteriol. 173:5457-5469(1991).
CC   -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
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   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; M60090; AAA22161.1; -; Genomic_DNA.
DR   PIR; C43706; C43706.
DR   AlphaFoldDB; P23122; -.
DR   SMR; P23122; -.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07939; DRE_TIM_NifV; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013477; NifV/FrbC.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 1.
DR   TIGRFAMs; TIGR02660; nifV_homocitr; 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; Transferase.
FT   CHAIN           1..382
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140459"
FT   DOMAIN          4..254
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   382 AA;  41490 MW;  0518B7315F567DF4 CRC64;
     MASVIIDDTT LRDGEQSAGV AFNADEKIAI RRALAELGVP ELEIGIPSMG EEEREVMRAI
     AGLGLSSRLL AWCRLCDFDL SAARSTGVTM VDLSLPISDL MLRHKLNRDR DWALGEVARL
     VSEARMAGLE VCLGCEDASR ADQDFIVRVG AVAQAARPPP AFADTVGVME PFGMLDRFRF
     LRQRLDVELE VHAHDDFGLA TANTLAAVMG GATHINTTVN GLGERAANAA LEECVLALKN
     LHGIDTGIDT RGIPAISALV ERASGRQWPG RRAWLAPVFT HEAGIHVDGL LKHRRNYEGL
     NPDELGRSHS LVLGKHSGAH MVRNSYRELG IELADWQSQA LLGRIRAFST RTKRSPQAAE
     LEDFYRQLCE QGTAELAAGG MA