ID   NIFV_AZOVI              Reviewed;         385 AA.
AC   P05342;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3040672; DOI=10.1128/jb.169.9.4024-4029.1987;
RA   Beynon J., Ally A., Cannon M., Cannon F., Jacobson M.R., Cash V.L.,
RA   Dean D.R.;
RT   "Comparative organization of nitrogen fixation-specific genes from
RT   Azotobacter vinelandii and Klebsiella pneumoniae: DNA sequence of the
RT   nifUSV genes.";
RL   J. Bacteriol. 169:4024-4029(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX   PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA   Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA   Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT   "Physical and genetic map of the major nif gene cluster from Azotobacter
RT   vinelandii.";
RL   J. Bacteriol. 171:1017-1027(1989).
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   -!- DISRUPTION PHENOTYPE: Fixes nitrogen very poorly; has very slow
CC       diazotrophic growth on nitrogen-free agar plates. A double nifS-nifV
CC       deletion no longer fixes nitrogen. {ECO:0000269|PubMed:2644218}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; M17349; AAA22169.1; -; Genomic_DNA.
DR   EMBL; M20568; AAA64727.1; -; Genomic_DNA.
DR   PIR; S29758; S29758.
DR   AlphaFoldDB; P05342; -.
DR   SMR; P05342; -.
DR   BioCyc; MetaCyc:MON-19489; -.
DR   SABIO-RK; P05342; -.
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..385
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140460"
FT   DOMAIN          4..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   CONFLICT        160
FT                   /note="R -> P (in Ref. 1; AAA22169)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   385 AA;  41653 MW;  1A5147B431B10984 CRC64;
     MASVIIDDTT LRDGEQSAGV AFNADEKIAI ARALAELGVP ELEIGIPSMG EEEREVMHAI
     AGLGLSSRLL AWCRLCDVDL AAARSTGVTM VDLSLPVSDL MLHHKLNRDR DWALREVARL
     VGEARMAGLE VCLGCEDASR ADLEFVVQVG EVAQAAGARR LRFADTVGVM EPFGMLDRFR
     FLSRRLDMEL EVHAHDDFGL ATANTLAAVM GGATHINTTV NGLGERAGNA ALEECVLALK
     NLHGIDTGID TRGIPAISAL VERASGRQVA WQKSVVGAGV FTHEAGIHVD GLLKHRRNYE
     GLNPDELGRS HSLVLGKHSG AHMVRNTYRD LGIELADWQS QALLGRIRAF STRTKRRSPQ
     PAELQDFYRQ LCEQGNPELA AGGMA