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Database: UniProt
Entry: A0A0G9MQG0_9SPHN
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ID   A0A0G9MQG0_9SPHN        Unreviewed;       565 AA.
AC   A0A0G9MQG0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|HAMAP-Rule:MF_00572};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_00572};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_00572};
GN   ORFNames=AAW01_01870 {ECO:0000313|EMBL:KLE32804.1}, BMF35_a1794
GN   {ECO:0000313|EMBL:APE28623.1};
OS   Aurantiacibacter gangjinensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=502682 {ECO:0000313|EMBL:KLE32804.1, ECO:0000313|Proteomes:UP000053070};
RN   [1] {ECO:0000313|EMBL:KLE32804.1, ECO:0000313|Proteomes:UP000053070}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K7-2 {ECO:0000313|EMBL:KLE32804.1,
RC   ECO:0000313|Proteomes:UP000053070};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacr gangjinensis K7-2.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:APE28623.1, ECO:0000313|Proteomes:UP000183202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC1.15024 {ECO:0000313|EMBL:APE28623.1,
RC   ECO:0000313|Proteomes:UP000183202};
RA   Xu L., Wu Y.-H., Cheng H., Zhou Y.-G., Wu M., Cheng L., Xu X.-W.;
RT   "Complete genome sequence of two-chromosomal Erythrobacter gangjinensis
RT   CGMCC 1.15024T, isolated from seawater.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA
CC       with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-
CC       hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000256|HAMAP-
CC       Rule:MF_00572}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00572};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00572};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC       from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000256|ARBA:ARBA00004689,
CC       ECO:0000256|HAMAP-Rule:MF_00572}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00572}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 2 subfamily. {ECO:0000256|ARBA:ARBA00009767,
CC       ECO:0000256|HAMAP-Rule:MF_00572}.
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DR   EMBL; CP018097; APE28623.1; -; Genomic_DNA.
DR   EMBL; LBHC01000001; KLE32804.1; -; Genomic_DNA.
DR   RefSeq; WP_047005653.1; NZ_LBHC01000001.1.
DR   AlphaFoldDB; A0A0G9MQG0; -.
DR   STRING; 502682.BMF35_a1794; -.
DR   KEGG; egn:BMF35_a1794; -.
DR   PATRIC; fig|502682.8.peg.382; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000053070; Unassembled WGS sequence.
DR   Proteomes; UP000183202; Chromosome i.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003985; F:acetyl-CoA C-acetyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00572; LeuA_type2; 1.
DR   InterPro; IPR013709; 2-isopropylmalate_synth_dimer.
DR   InterPro; IPR002034; AIPM/Hcit_synth_CS.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR005668; IPM_Synthase.
DR   InterPro; IPR036230; LeuA_allosteric_dom_sf.
DR   InterPro; IPR039371; LeuA_N_DRE-TIM.
DR   InterPro; IPR000891; PYR_CT.
DR   NCBIfam; TIGR00970; leuA_yeast; 1.
DR   PANTHER; PTHR46911; -; 1.
DR   PANTHER; PTHR46911:SF1; 2-ISOPROPYLMALATE 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   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   Acyltransferase {ECO:0000313|EMBL:APE28623.1};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00572};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_00572};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00572};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_00572}; Magnesium {ECO:0000256|HAMAP-Rule:MF_00572};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00572}; Reference proteome {ECO:0000313|Proteomes:UP000053070};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00572}.
FT   DOMAIN          33..307
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          441..565
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         42
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ   SEQUENCE   565 AA;  62845 MW;  55254C79881DC871 CRC64;
     MPMHSDPKTK YRPFPQVDLP DRQWPTRSIT APPRWLSTDL RDGNQSIIDP MDRAKKTRFF
     DLLLEVGVKE IEVGFPAAGQ TEFDFISWLV QSGRVPEDVT VQVLTQSRED LIARSFESLE
     GAHRAIVHLY NALSPAWRDI VFRMSRDEVR DIAIRGAQQL VDEAAKRPGT DWHYQYSPET
     FSTAELDFSL EVCEAVMRTV GATKDRPLIL NLPATVEAAT PNIYADQIEY FCRNLPNREA
     AIISLHTHND RGTGVAAAEL GLMAGADRVE GCLFGNGERT GNCCLVTVAL NMYTQGVDPG
     LDFSDIDKVI ETVEYCNALP VHQRHPYGGE LVYTAFSGSH QDAIKKGFEA RGAQNDEHWR
     VPYLPIDPAD LGRNYEAVIR VNSQSGKGGF AWVLQQDQGL KLPKRLQADF SKHVQHMADG
     EGHELTAEDI WHCFRETYYV QSERRRFRLV DYDESRASDG TRIFTGTVEV DGEEQRVSGR
     GKGLISSVLS TIREAFDVDL EVADYSEHAL GTGVDSRAAA YIEWTTPDGR NGWGVGIDED
     VATASVRAIL SAANGAAHGP GTPRF
//
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