ID E8WM84_GEOS8 Unreviewed; 528 AA. AC E8WM84; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 62. DE RecName: Full=(R)-citramalate synthase {ECO:0000256|ARBA:ARBA00022325}; DE EC=2.3.3.21 {ECO:0000256|ARBA:ARBA00034330}; GN OrderedLocusNames=GM18_1123 {ECO:0000313|EMBL:ADW12598.1}; OS Geobacter sp. (strain M18). OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geobacter. OX NCBI_TaxID=443143 {ECO:0000313|EMBL:ADW12598.1, ECO:0000313|Proteomes:UP000001442}; RN [1] {ECO:0000313|EMBL:ADW12598.1, ECO:0000313|Proteomes:UP000001442} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M18 {ECO:0000313|EMBL:ADW12598.1, RC ECO:0000313|Proteomes:UP000001442}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Chertkov O., Munk C., Detter J.C., Han C., Tapia R., Land M., Hauser L., RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Holmes D., RA Aklujkar M., Lovley D., Woyke T.; RT "Complete sequence of Geobacter sp. M18."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + H2O + pyruvate = (3R)-citramalate + CoA + H(+); CC Xref=Rhea:RHEA:19045, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30934, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.21; CC Evidence={ECO:0000256|ARBA:ARBA00034270}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 1/3. {ECO:0000256|ARBA:ARBA00004743}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. {ECO:0000256|ARBA:ARBA00006154, 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; CP002479; ADW12598.1; -; Genomic_DNA. DR AlphaFoldDB; E8WM84; -. DR STRING; 443143.GM18_1123; -. DR KEGG; geb:GM18_1123; -. DR eggNOG; COG0119; Bacteria. DR HOGENOM; CLU_022158_7_0_7; -. DR OrthoDB; 9803573at2; -. DR UniPathway; UPA00047; UER00066. DR Proteomes; UP000001442; Chromosome. DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:RHEA. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro. DR CDD; cd07941; DRE_TIM_LeuA3; 1. DR Gene3D; 1.10.238.260; -; 1. DR Gene3D; 3.30.160.270; -; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005675; Citramal_synthase. DR InterPro; IPR036230; LeuA_allosteric_dom_sf. DR InterPro; IPR000891; PYR_CT. DR NCBIfam; TIGR00977; citramal_synth; 1. DR PANTHER; PTHR43538:SF1; (R)-CITRAMALATE SYNTHASE; 1. DR PANTHER; PTHR43538; ALPHA-IPM SYNTHASE/HOMOCITRATE SYNTHASE; 1. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ADW12598.1}; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304}; KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304}; KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}. FT DOMAIN 4..266 FT /note="Pyruvate carboxyltransferase" FT /evidence="ECO:0000259|PROSITE:PS50991" SQ SEQUENCE 528 AA; 58642 MW; DCC80117B9F71451 CRC64; MSLVKLYDTT LRDGTQAEDI SFLVEDKIRI AHKLDECGIH YIEGGWPGSN PKDVAFFKDI KKEKLSQAKI AAFGSTRRAK ITPDKDQNLR TLVDSKADAA TIFGKSWDFQ VHEALRIPLE ENLEMIFDSL EYLKGHMPEV FYDAEHFFDG YKSNPEYAIK TLQAAQQAGA DCIILCDTNG GSMPYEIARI VNEVKKSITT PLGVHAHNDG ECAVANTIIS VEQGIVHVQG TINGFGERCG NANLCSIIPA LKVKMKRDCI SDAQMRTLRE LSRYVYELAN LAPNKHQPYV GNSAFAHKGG VHVSAIQRHP ETYEHMRPEL VGNTTRVLVS DLSGRANILA KATEFNINLD SKDPVTLEIL EDIKSMENRG YQFEGAEASF ELLMKRALGT HRKFFSVIGF RVIDEKRSED DQPISEATIK VKVGGKIEHT ASEGHGPVNA LDNALRKALE KFYPRLKDVK LHDYKVRVLP AGQGTASSIR VLIESGDKEG RWGTVGVSSN VIEASYQALV DAIEFKLHKD EETAAPKK //