ID A0A1N7SX79_9BURK Unreviewed; 378 AA.
AC A0A1N7SX79;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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:SIT52096.1};
GN ORFNames=BN2476_1800030 {ECO:0000313|EMBL:SIT52096.1};
OS Paraburkholderia piptadeniae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1701573 {ECO:0000313|EMBL:SIT52096.1, ECO:0000313|Proteomes:UP000195569};
RN [1] {ECO:0000313|EMBL:SIT52096.1, ECO:0000313|Proteomes:UP000195569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=STM 7183 {ECO:0000313|EMBL:SIT52096.1,
RC ECO:0000313|Proteomes:UP000195569};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CYGY02000180; SIT52096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N7SX79; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000195569; Unassembled WGS sequence.
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 Acyltransferase {ECO:0000313|EMBL:SIT52096.1};
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 378 AA; 40767 MW; CB3838E9EA288C6D CRC64;
MLKPIINDTT LRDGEQAAGV AFRLEEKCAI AASLSRAGVA ELEIGIPAMG EDEIACIEAI
VGLKLDARLM VWGRLTDGDL TAALRCHADI VHLSIPVSDI HLQHKLRQSR SWVLAQVARV
VEEAAKNHSK ISLGMEDASR ADPSFLIEVA RCAQRYGAQR VRFADTVGML DPFKTFHAIA
ALRDAVDLEV EIHAHDDLGL ATANTLAALA AGATHANTTV NGLGERAGNA ALEEIVMGVR
HLLGRDTGVD TRALLDISSL VEQASGRTVS FNKSIVGRGV FTHESGIHTD GVAKHPTTYE
GFDPAELGRQ RSMILGKHSG SQSVREAYDA LGVRVGERLI PRLLARIRSF ATQYKQAPSA
RDLHQFLAQA RGTRMETS
//
