ID   NIFV_FRASP              Reviewed;         401 AA.
AC   P54610;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Frankia sp. (strain FaC1).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia;
OC   unclassified Frankia.
OX   NCBI_TaxID=1857;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Oh B., Twigg P., Hong J., Mullin B., An C.S.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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; U53363; AAB36875.1; -; Genomic_DNA.
DR   AlphaFoldDB; P54610; -.
DR   SMR; P54610; -.
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..401
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140463"
FT   DOMAIN          22..271
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   REGION          367..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   401 AA;  43158 MW;  BF164D7EF0D85246 CRC64;
     MTVRETRFPS SSATATQPDA VVRFCDTTLR DGEQAPGVAF TAAEKLAIAG ALDAIGVHQI
     EAGIPGMGVT ERDVLREILA TDPKAEIVGW CRADHRDVEA AASCGLVTAH LTIPVSDLHL
     KSKLERDRAW ARRRVRDCVV DGTDRGMRVS VGFEDASRAD DAFVTDLAGE LRDVGVTRLR
     WADTVGLLDP VSAYDRLGRL VRAVPGPWEI HAHDDFGLAT ANTIAAVQAG FTWVSTTVLG
     LGERAGNAPI EEVAMALRHL LKLPIDLDTT SFRTLAQLVV GWPLPAGKKA VVGESVFAHE
     SGIHVHGILR HPATYEPFDP EVGGRRRLTV GKHSGRASLR HALEQCGITA EESELEPLVE
     QVRLAATRHK RGLDSRDLPG TSRAGRDAGP RAGTPTREEP V