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Database: UniProt
Entry: Q2IDZ9_ANADE
LinkDB: Q2IDZ9_ANADE
Original site: Q2IDZ9_ANADE 
ID   Q2IDZ9_ANADE            Unreviewed;       447 AA.
AC   Q2IDZ9;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   OrderedLocusNames=Adeh_3037 {ECO:0000313|EMBL:ABC82806.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC82806.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Kiss H., Schmutz J., Larimer F., Land M., Kyrpides N.,
RA   Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R.,
RA   Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-
CC         isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178,
CC         ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13;
CC         Evidence={ECO:0000256|ARBA:ARBA00000064};
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
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DR   EMBL; CP000251; ABC82806.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2IDZ9; -.
DR   STRING; 290397.Adeh_3037; -.
DR   KEGG; ade:Adeh_3037; -.
DR   eggNOG; COG0119; Bacteria.
DR   HOGENOM; CLU_004588_3_2_7; -.
DR   OMA; WPDKVID; -.
DR   OrthoDB; 9803573at2; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd07942; DRE_TIM_LeuA; 1.
DR   Gene3D; 3.30.160.270; -; 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; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   PANTHER; PTHR46911; -; 1.
DR   PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE SYNTHASE; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   SUPFAM; SSF89000; post-HMGL domain-like; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyruvate {ECO:0000313|EMBL:ABC82806.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          31..304
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   447 AA;  49323 MW;  1AA75F7156D6A0B7 CRC64;
     MPRMPVHKYR PFPQVALADR RWPSRRIERA PRWCSVDLRD GNQALEDPMG PERKRLLFDA
     LVRAGFREIE VGFPSASRPE REFVRELVER GIPDGVTIQV LTQAREHLVR ATFDAIRGAP
     RAVVHLYNST SELQRRVVFG KDRAGIRQIA VDGTRLARQL AEELPETEVI LEYTPESFTG
     TELDFAAEVC EAVMDAWGAS AERPVILNLP ATVEMSTPNV YADQVEWFGR HVRGRERYVL
     SVHPHNDRGT AVAAAELAVM AGADRVEGTL FGNGERTGNV DLVTLALNLH TQGVDPGLDL
     ADLDALVEVA ERATRMPVHP RHPYAGALVY TAFSGSHQDA IKKGFAALRR TDGERWEMPY
     LPMDPADVGR TYQAVIRVNS QSGKGGVGWV LEEHGGIRLG REELVRFAAV IQGMAEARGT
     DLTPAEILEV YARTHGGAPG ARAVAQG
//
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