ID   NIFV_KLEPN              Reviewed;         381 AA.
AC   P05345;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Homocitrate synthase;
DE            EC=2.3.3.14;
GN   Name=nifV;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3054814; DOI=10.1093/nar/16.20.9860;
RA   Beynon J., Cannon M., Banan-Wollaston V., Ally A., Sutterquist R.,
RA   Cannon F.;
RT   "The nucleotide sequence of the nifT, nifY, nifX and nifW genes of K.
RT   pneumoniae.";
RL   Nucleic Acids Res. 16:9860-9860(1988).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA   Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT   "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT   nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL   J. Mol. Biol. 203:715-738(1988).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 344-381.
RC   STRAIN=UN;
RA   Collet T.A., White T., Howard K., Orme-Johnson W.H.;
RL   Submitted (JUL-1989) 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; X12600; CAA31119.1; -; Genomic_DNA.
DR   EMBL; M17350; AAA25157.1; -; Genomic_DNA.
DR   EMBL; X13303; CAA31676.1; -; Genomic_DNA.
DR   EMBL; M24106; AAA25102.1; -; Genomic_DNA.
DR   PIR; S34848; S34848.
DR   PIR; S37297; S37297.
DR   AlphaFoldDB; P05345; -.
DR   SMR; P05345; -.
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; 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..381
FT                   /note="Homocitrate synthase"
FT                   /id="PRO_0000140464"
FT   DOMAIN          4..256
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
FT   CONFLICT        102
FT                   /note="R -> P (in Ref. 2; AAA25157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        155..157
FT                   /note="NAP -> QCA (in Ref. 3; CAA31676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        232..236
FT                   /note="AWKPS -> LETV (in Ref. 3; CAA31676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        258
FT                   /note="L -> S (in Ref. 3; CAA31676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        296
FT                   /note="D -> H (in Ref. 3; CAA31676)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        363
FT                   /note="E -> Q (in Ref. 2; AAA25157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        381
FT                   /note="G -> A (in Ref. 2; AAA25157)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   381 AA;  41190 MW;  3135F8E0A39216D1 CRC64;
     MERVLINDTT LRDGEQSPGV AFRTSEKVAI AEALYAAGIT AMEVGTPAMG DEEIARIQLV
     RRQLPDATLM TWCRMNALEI RQSADLGIDW VDISIPASDK LRQYKLREPL AVLLERLAMF
     IHLAHTLGLK VCIGCEDASR ASGQTLRAIA EVAQNAPAAR LRYADTVGLL DPFTTAAQIS
     ALRDVWSGEI EMHAHNDLGM ATANTLAAVS AGATSVNTTV LGLGERAGNA AAWKPSALGL
     ERCLGVETGV HFSALPALCQ RVAEAAQRAI DPQQPLVGEL VFTHESGVHV AALLRDSESY
     QSIAPSLMGR SYRLVLGKHS GRQAVNGVFD QMGYHLNAAQ INQLLPAIRR FAENWKRSPK
     DYELVAIYDE LCGESALRAR G