ID   NIFV_CERSP              Reviewed;         391 AA.
AC   Q01181;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1317839; DOI=10.1128/jb.174.12.3855-3866.1992;
RA   Meijer W.G., Tabita F.R.;
RT   "Isolation and characterization of the nifUSVW-rpoN gene cluster from
RT   Rhodobacter sphaeroides.";
RL   J. Bacteriol. 174:3855-3866(1992).
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; M86823; AAA26138.1; -; Genomic_DNA.
DR   PIR; D41880; D41880.
DR   RefSeq; WP_017139924.1; NZ_WSNV01000246.1.
DR   AlphaFoldDB; Q01181; -.
DR   SMR; Q01181; -.
DR   OrthoDB; 840579at2; -.
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..391
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140466"
FT   DOMAIN          19..269
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   391 AA;  40666 MW;  C58AC010086E498B CRC64;
     MSRQQPRASF LPESPLAPVA LCDTTLRDGE QTAGVAFTRA EKRAIAEALQ AAGVAEVEVG
     VPAMGEEERA DIRAVAAVLK TAAPVVWCRL RAEDLAAAQR TGVVRLHIGV PVSERQISAK
     LGKDAAWVRD KVEKLVRAAS WAGHKVSVGA EDASRADPFF LAEIAHVAAE AGAIRFRISD
     TLGVLDPFAA HELVGRVVTR CPLPVEFHGH NDLGMATANS LAAARAGASH LSVTVNGLGE
     RAGNAALEEV AAALEAAGRA TGVALGQLCA LSELVARASG RPLSPQKPIV GEGVFTHECG
     IHVDGLMKDR ATYESADLRP ERFGRSHRIA IGKHSSAAGL ARALAEAGLP ADAATLAALM
     PALRDWAAIT KRAAAPEDLA ALLAAQTETA R