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Database: UniProt
Entry: A0YAU0_9GAMM
LinkDB: A0YAU0_9GAMM
Original site: A0YAU0_9GAMM 
ID   A0YAU0_9GAMM            Unreviewed;       570 AA.
AC   A0YAU0;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 87.
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=GP2143_04450 {ECO:0000313|EMBL:EAW31670.1};
OS   marine gamma proteobacterium HTCC2143.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; BD1-7 clade.
OX   NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW31670.1, ECO:0000313|Proteomes:UP000004931};
RN   [1] {ECO:0000313|EMBL:EAW31670.1, ECO:0000313|Proteomes:UP000004931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW31670.1,
RC   ECO:0000313|Proteomes:UP000004931};
RX   PubMed=20601481; DOI=10.1128/JB.00683-10;
RA   Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT   isolated from the Oregon Coast.";
RL   J. Bacteriol. 192:4530-4531(2010).
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}.
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:EAW31670.1}.
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DR   EMBL; AAVT01000002; EAW31670.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0YAU0; -.
DR   STRING; 247633.GP2143_04450; -.
DR   eggNOG; COG0119; Bacteria.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000004931; Unassembled WGS sequence.
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   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:UP000004931};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00572}.
FT   DOMAIN          42..316
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          448..570
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         257
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         291
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ   SEQUENCE   570 AA;  63403 MW;  43478CFDF309B90A CRC64;
     MLDNPLNSSA ISGDFNHRKY RPVATFNKSD RRWPDQVITK APRWCSVDLR DGNQALVEPM
     NPEQKLDLFK LLVEVGFKEI EVGFPAASQP DFDFVRKIIE ENLIPDDVSI QVLTQSREEL
     ISRSFEALTG AKKAIVHLYN STSTVQREHV FGMSREQIKA IAVEGAVWVK QCAQQQPDTD
     WTFEYSPESF TGTEMEYAVE VCDAVTDIWQ PTVEKPVIIN LPSTVEMTTP NVYADQIEWV
     SDNIARRDCL QISLHTHNDR GCGVAAAELG LMAGADRAEG TLLGNGERTG NMDVITAAMN
     MYSQGIDPML DFSNMDKIIK VVNQCTNITI HPRHPYAGEL VFTAFSGSHQ DAINKCLHRR
     QTNDVWDVAY LPIDPADLGR SYQEVIRINS QSGKGGIAYV LEQDYGVQMP RWLQVDFSRH
     VQHLAEQNEG EVSSKEIWQV FRETYIGSAQ AIQLDGYQLT RQDNRDQLNA TMILENKHVA
     LSGNGQGALD AFVGGLTQLI GADVVITDYS EHTLGNSEQS DAIAYIQLSI DGQRYCGVGQ
     SADIVEASLR AVLSACSRAQ LVMSPLPKKA
//
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