ID   NIFV_RHOCA              Reviewed;         382 AA.
AC   Q07179;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33303 / B10;
RX   PubMed=8492805; DOI=10.1007/bf00291996;
RA   Masepohl B., Angermueller S., Hennecke S., Huebner P., Moreno-Vivian C.,
RA   Klipp W.;
RT   "Nucleotide sequence and genetic analysis of the Rhodobacter capsulatus
RT   ORF6-nifUI SVW gene region: possible role of NifW in homocitrate
RT   processing.";
RL   Mol. Gen. Genet. 238:369-382(1993).
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; X68444; CAA48488.1; -; Genomic_DNA.
DR   PIR; S34817; S34817.
DR   AlphaFoldDB; Q07179; -.
DR   SMR; Q07179; -.
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_0000140465"
FT   DOMAIN          7..257
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   382 AA;  40618 MW;  E2A0DEBC1E79062A CRC64;
     MTPDRTLALC DTTLRDGEQT AGVAFSLAEK KAIARALDRA GVAEIEVGIA AMGWAEVAEI
     RAVVAEIAHA TPVVWCRLRM HDLDMAQKTG VKRVHFAVPT STAQLEGKLR VDRDWILRET
     AALVFCASDR GLQVSVGAED ASRTDPDFLI RLAEVAAAAG AIRFRIADTL GLLDPLGAFR
     LVAELSARIS LPIEMHAHND FGMATANTIM AAHAGATHLS VTVNGLGERA GNAACEEVGA
     ALEAGGIDTG LDLCALPELS AVVAKASGRA FRAQKPITGD DWLFAHESGI HVDAILKRAD
     TYEDPRCAPA RFGRERQIVI GKHSGSAGLR AALLEAGLPA DDAVLDRLKP LLRAHAVRVK
     RPVEAGDLRR MVARLARPSP RT