ID C6E9A3_GEOSM Unreviewed; 382 AA.
AC C6E9A3;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Homocitrate synthase {ECO:0000256|RuleBase:RU367143};
DE EC=2.3.3.14 {ECO:0000256|RuleBase:RU367143};
GN OrderedLocusNames=GM21_2146 {ECO:0000313|EMBL:ACT18198.1};
OS Geobacter sp. (strain M21).
OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=443144 {ECO:0000313|EMBL:ACT18198.1};
RN [1] {ECO:0000313|EMBL:ACT18198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M21 {ECO:0000313|EMBL:ACT18198.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lovley D.;
RT "Complete sequence of Geobacter sp. M21.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This protein is a Fe-Mo-cofactor biosynthetic component.
CC {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|RuleBase:RU367143};
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. {ECO:0000256|RuleBase:RU003523}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001661; ACT18198.1; -; Genomic_DNA.
DR AlphaFoldDB; C6E9A3; -.
DR STRING; 443144.GM21_2146; -.
DR KEGG; gem:GM21_2146; -.
DR eggNOG; COG0119; Bacteria.
DR HOGENOM; CLU_022158_4_2_7; -.
DR OrthoDB; 9803573at2; -.
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 9..261
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 382 AA; 41025 MW; 1E6EC4E19B88B355 CRC64;
MAGFPKAQVF IADTTLRDGE QTAGVVFTAK EKISIARQLD AMGVHELECG IPAMGEEERD
SIRALVALGL SARLVTWNRA LVSDIEASIA CGIKAVDISL CVSDIMIEHK INKSRAFVKE
QLKRALCFAK DKGLYVCVGG EDASRADGDF LIELMQIAQA NGAERFRFCD TLGILDPFAM
FEKVGRLRAA VPGLDIEVHT HNDLGLATAN ALAGVRGGAS YISTTVNGLG ERAGNAALEE
VVMALKVACG IDAGIDTRRF KSVSRLVGRA SNREVPPWKA VVGERVFSHE SGLHADGVLK
DPRNYEGFTP EEVGLKRHIV AGKHSGTNGI VESYRQIGIP ISREEAQELM DKVRSTAQRI
KGALAPVDLL KLHQGRGVSL AA
//
