ID A0A0L6TWS7_9FIRM Unreviewed; 517 AA.
AC A0A0L6TWS7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=AKG39_16090 {ECO:0000313|EMBL:KNZ40708.1};
OS Acetobacterium bakii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52689 {ECO:0000313|EMBL:KNZ40708.1, ECO:0000313|Proteomes:UP000036873};
RN [1] {ECO:0000313|Proteomes:UP000036873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8239 {ECO:0000313|Proteomes:UP000036873};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Acetobacterium bakii DSM 8293, a potential
RT psychrophilic chemical producer through syngas fermentation.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004689}.
CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNZ40708.1}.
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DR EMBL; LGYO01000045; KNZ40708.1; -; Genomic_DNA.
DR RefSeq; WP_050741429.1; NZ_UOGO01000001.1.
DR AlphaFoldDB; A0A0L6TWS7; -.
DR STRING; 52689.AKG39_16090; -.
DR PATRIC; fig|52689.4.peg.2751; -.
DR OrthoDB; 9804858at2; -.
DR UniPathway; UPA00048; UER00070.
DR Proteomes; UP000036873; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd07940; DRE_TIM_IPMS; 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; IPR036230; LeuA_allosteric_dom_sf.
DR InterPro; IPR005671; LeuA_bact_synth.
DR InterPro; IPR000891; PYR_CT.
DR NCBIfam; TIGR00973; leuA_bact; 1.
DR PANTHER; PTHR10277:SF9; 2-ISOPROPYLMALATE SYNTHASE 1, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR10277; HOMOCITRATE SYNTHASE-RELATED; 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; PS00816; AIPM_HOMOCIT_SYNTH_2; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000036873};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT DOMAIN 5..269
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 517 AA; 56661 MW; FCDA8244BE34F5E8 CRC64;
MSRKIYVFDT TLRDGEQVPG AKLNLAEKLA VAEQLAKMKV DMMEVGFPSS SQGDFEAVRA
ISRKIGKDVW IAALGRAVES DIDCIYESIR EAENPLIHIV LGSSEVHVSK KFRKTPQQVI
DMGVGAVKYA RRLLPQVQYS LEDASRSEFE YLWQTIEAVV KAGATIINVP DTVGFAIPDE
FGKLIYRIND RLKNLDPKVL LSVHCHNDTG LATANTLAAV KNGADKVECT INGIGERAGN
TALEEVVMGI SLHEAYYGGH TTVDTRQIYE TSRMVSATMG LDIQVNKAIT GENAFAHSSG
IHQDGLLKSK DVYEIMDPET IGAPAMEIVL TARSGRHAFM HITRQLGFDI PEESMGEIYQ
QFLAMADAKK EIYDNDVLTL LKNSTIPSSG NNPQLWQLIN YEMTVARGLP SATVTLAKGD
KEVVTRQTGS GVIDALYGAI MEAVDAPMEL IDYRINSLSR GKGSLGKVTT QIRCDDQLFA
GKAIEQDVMR ASALALINAI NKMVLEQAFG YQQEALH
//
