ID   NIFV2_NOSS1             Reviewed;         376 AA.
AC   P58637;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Homocitrate synthase 2;
DE            EC=2.3.3.14;
GN   Name=nifV2; OrderedLocusNames=alr2968;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB74667.1; -; Genomic_DNA.
DR   PIR; AI2176; AI2176.
DR   RefSeq; WP_010997119.1; NZ_RSCN01000003.1.
DR   AlphaFoldDB; P58637; -.
DR   SMR; P58637; -.
DR   STRING; 103690.17132062; -.
DR   EnsemblBacteria; BAB74667; BAB74667; BAB74667.
DR   KEGG; ana:alr2968; -.
DR   eggNOG; COG0119; Bacteria.
DR   OMA; GDNSCGA; -.
DR   OrthoDB; 840579at2; -.
DR   BRENDA; 2.3.3.14; 8113.
DR   Proteomes; UP000002483; Chromosome.
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; Reference proteome; Transferase.
FT   CHAIN           1..376
FT                   /note="Homocitrate synthase 2"
FT                   /id="PRO_0000140457"
FT   DOMAIN          4..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01151"
SQ   SEQUENCE   376 AA;  40937 MW;  343A804D990E4300 CRC64;
     MNKVLINDTT LRDGEQAAGV AFSVEEKIAI AKFLDAIGVH EIEVGIPAMG KAEQEAIANI
     VKLDLSANLL GWNRAVIADI QASIACGLQR VHISIPVSAI QIAVKFHGQW QVVLQKLHDS
     ISFAVDQGLF VSIGGEDSSR AEESFLLDVV LAAQEWGASR FRFCDTVGIL DPFTTHAKVK
     QLVASLTIPV EMHTHNDFGL ATANALAGTK AGALSVNTTV NGLGERAGNA ALEEVVMALK
     HLYHHDLGID TRRLLEISQL VASASGHPVP PWKAIVGENT FAHESGIHAH GVLQNPQTYE
     PFAPEEVGRE RRLVVGKHSG RHLLSSILQQ HDIILNHEET QFVLDAVRQE SVEKKRSLTD
     QELLHLVQTK QHFRAC