ID   NIFVA_CLOPA             Reviewed;         269 AA.
AC   Q00853; Q6J2L4;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Homocitrate synthase subunit alpha;
DE            EC=2.3.3.14;
GN   Name=nifV-ALPHA;
OS   Clostridium pasteurianum.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1501;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2022611; DOI=10.1128/jb.173.10.3041-3046.1991;
RA   Wang S.-Z., Dean D.R., Chen J.-S., Johnson J.L.;
RT   "The N-terminal and C-terminal portions of NifV are encoded by two
RT   different genes in Clostridium pasteurianum.";
RL   J. Bacteriol. 173:3041-3046(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   -!- SUBUNIT: Heterodimer of an alpha and an omega chain.
CC   -!- MISCELLANEOUS: In Clostridium pasteurianum the N-terminal and C-
CC       terminal portions of NifV are encoded by two different genes, nifV-
CC       alpha and nifV-omega.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000305}.
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DR   EMBL; AY603957; AAT37650.1; -; Genomic_DNA.
DR   PIR; B39403; B39403.
DR   RefSeq; WP_003447856.1; NZ_CP013019.1.
DR   AlphaFoldDB; Q00853; -.
DR   SMR; Q00853; -.
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   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   Pfam; PF00682; HMGL-like; 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..269
FT                   /note="Homocitrate synthase subunit alpha"
FT                   /id="PRO_0000140467"
FT   DOMAIN          3..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   269 AA;  29865 MW;  782C60A6595A3979 CRC64;
     MGINIVDTTL RDGEQKAGIA LSVQDKVEIA KIISEMGVHQ IEAGIPAMGG DEKISVSKIA
     ALGLPSKIAA WNRMSTKDID TSIECGVDIV HISSPVSDLQ IKTKLEKDRK WVAENLKRTV
     IYALEKDCEV TVGLEDSSRA DLNFLIQLCE MIFALGVKRV RYADTVGIME PKELYSQIKK
     IRDKVPIDIE IHVHNDFGMA ISNSFAAFKA GAKFADCTIT GMGERAGNCD FLKFVKVIQE
     LTGEKIYTGD FEDIIEKENE IKKILRLNW