ID I3YGI2_THIV6 Unreviewed; 384 AA.
AC I3YGI2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 OrderedLocusNames=Thivi_4287 {ECO:0000313|EMBL:AFL76100.1};
OS Thiocystis violascens (strain ATCC 17096 / DSM 198 / 6111) (Chromatium
OS violascens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiocystis.
OX NCBI_TaxID=765911 {ECO:0000313|EMBL:AFL76100.1, ECO:0000313|Proteomes:UP000006062};
RN [1] {ECO:0000313|EMBL:AFL76100.1, ECO:0000313|Proteomes:UP000006062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17096 / DSM 198 / 6111
RC {ECO:0000313|Proteomes:UP000006062};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z.,
RA Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of Thiocystis violascens DSM 198.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003154; AFL76100.1; -; Genomic_DNA.
DR RefSeq; WP_014780480.1; NC_018012.1.
DR AlphaFoldDB; I3YGI2; -.
DR STRING; 765911.Thivi_4287; -.
DR KEGG; tvi:Thivi_4287; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_6; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000006062; 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 Reference proteome {ECO:0000313|Proteomes:UP000006062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 8..259
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 384 AA; 42052 MW; 74871C1D7C03FD74 CRC64;
MIDHRLKVTI NDTTLRDGEQ SAGVAFSLDE KLAIARGLDT LGVPELEIGI PAMGEDERAS
IRAVAALGLS ARLMVWTRML PDDIAQCRDL GVDLVDLSIP VSDQQIARKL RRDRAWVLGQ
IRRQVNAAQD LGLEVCVGAE DASRADPEFL WRAAEAAQEA GARRFRFADT VGLMDPFAVF
ERIRDLRAIV DLEIEMHAHD DLGLATANSL AAVRGGATHV NTTVHGLGER AGNAALEEVI
MGLRHIHRID CGVDLKDFDG LSRLVAKASG KPVAWHKSLV GAGAFTHEAG IHVDGLLKDP
LNYQGVDPAD VGRRHCMVLG KHSGTRAVRQ VYADQLRFEI DTDQAERVLP LVRRFVTETK
RSPEPLDLRR FLAEIGHPQA ALLQ
//
