ID D1KS54_PANSA Unreviewed; 380 AA.
AC D1KS54;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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:ACU32744.1};
GN OrderedLocusNames=Pat9b_4710 {ECO:0000313|EMBL:ADU72679.1};
OS Pantoea sp. (strain At-9b).
OG Plasmid pPAT9B03 {ECO:0000313|EMBL:ADU72679.1,
OG ECO:0000313|Proteomes:UP000001624}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ACU32744.1};
RN [1] {ECO:0000313|EMBL:ACU32744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=At-9b {ECO:0000313|EMBL:ACU32744.1};
RA Pinto-Thomas A.A., Anderson M.A., Suen G., Stevenson D.M., Chu F.S.T.,
RA Cleland W.W., Weimer P.J., Currie C.R.;
RT "Symbiotic Nitrogen Fixation in the Fungus Gardens of Leaf-Cutter Ants.";
RL Science 326:1120-1123(2009).
RN [2] {ECO:0000313|EMBL:ADU72679.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|Proteomes:UP000001624};
RC PLASMID=At-9b {ECO:0000313|EMBL:ADU72679.1}, Plasmid pPAT9B03
RC {ECO:0000313|Proteomes:UP000001624}, and pPAT9B03
RC {ECO:0000313|EMBL:ADU72679.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence plasmid3 of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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; GQ342604; ACU32744.1; -; Genomic_DNA.
DR EMBL; CP002436; ADU72679.1; -; Genomic_DNA.
DR RefSeq; WP_013512504.1; NC_014840.1.
DR AlphaFoldDB; D1KS54; -.
DR KEGG; pao:Pat9b_4710; -.
DR HOGENOM; CLU_022158_4_0_6; -.
DR OrthoDB; 9803573at2; -.
DR Proteomes; UP000001624; Plasmid pPAT9B03.
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 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 Plasmid {ECO:0000313|EMBL:ADU72679.1};
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 380 AA; 41658 MW; 51057A24E9AFF973 CRC64;
MSTVLINDTT LRDGEQSPGV AFRASEKIAI AEALYDAGIT ALEVGTPAMG EEERARIQLV
RRHLPDATLM TWCRMNADEI RQSAELGMDW VDISLPTSEK LRQYKLREAL PVLLERLADL
IALSRSLGMK VCVGCEDASR SSDRDLRLVA QAAQEAGAQR LRFADTLGVL DPFTTAARIT
ALRNIWPFEI EMHAHDDLGL ATANTLAAVQ AGATSVNTTV LGLGERAGNA ALETVALGLS
RCLEQDCGVD FRLLPALCQQ VAEAAQRTID VQHPLVGDQV FTHESGVHVA ALLRDRESYQ
AIDPALVGRE YRLVLGKHSG RQAVDGVFSK MGYTLDTLQI DLLLPAIRRF AESWKRIPQD
YELIAIYDQL CGETVPTLRI
//
