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Database: UniProt
Entry: C1DH20_AZOVD
LinkDB: C1DH20_AZOVD
Original site: C1DH20_AZOVD 
ID   C1DH20_AZOVD            Unreviewed;       384 AA.
AC   C1DH20;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Homocitrate synthase {ECO:0000256|ARBA:ARBA00020735, ECO:0000256|RuleBase:RU367143};
DE            EC=2.3.3.14 {ECO:0000256|ARBA:ARBA00012974, ECO:0000256|RuleBase:RU367143};
GN   Name=nifV {ECO:0000313|EMBL:ACO76427.1};
GN   OrderedLocusNames=Avin_01640 {ECO:0000313|EMBL:ACO76427.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76427.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO76427.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC       {ECO:0000256|ARBA:ARBA00003050, ECO:0000256|RuleBase:RU367143}.
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         Evidence={ECO:0000256|ARBA:ARBA00000596,
CC         ECO:0000256|RuleBase:RU367143};
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. {ECO:0000256|RuleBase:RU003523}.
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DR   EMBL; CP001157; ACO76427.1; -; Genomic_DNA.
DR   RefSeq; WP_012698855.1; NC_012560.1.
DR   AlphaFoldDB; C1DH20; -.
DR   SMR; C1DH20; -.
DR   STRING; 322710.Avin_01640; -.
DR   EnsemblBacteria; ACO76427; ACO76427; Avin_01640.
DR   KEGG; avn:Avin_01640; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_022158_4_2_6; -.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000002424; Chromosome.
DR   GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd07939; DRE_TIM_NifV; 1.
DR   Gene3D; 1.10.238.260; -; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR013477; NifV/FrbC.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR02660; nifV_homocitr; 1.
DR   PANTHER; PTHR42880; HOMOCITRATE SYNTHASE; 1.
DR   PANTHER; PTHR42880:SF1; ISOPROPYLMALATE_HOMOCITRATE_CITRAMALATE SYNTHASE FAMILY PROTEIN; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 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 {ECO:0000256|RuleBase:RU367143};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          4..255
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   384 AA;  41497 MW;  E7C457B685E5A6D7 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 STRTKRSPQP
     AELQDFYRQL CEQGNPELAA GGMA
//
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