GenomeNet

Database: UniProt
Entry: A0A3N2DPC3_9GAMM
LinkDB: A0A3N2DPC3_9GAMM
Original site: A0A3N2DPC3_9GAMM 
ID   A0A3N2DPC3_9GAMM        Unreviewed;       562 AA.
AC   A0A3N2DPC3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
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=EDC56_2108 {ECO:0000313|EMBL:ROS01664.1};
OS   Sinobacterium caligoides.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Sinobacterium.
OX   NCBI_TaxID=933926 {ECO:0000313|EMBL:ROS01664.1, ECO:0000313|Proteomes:UP000275394};
RN   [1] {ECO:0000313|EMBL:ROS01664.1, ECO:0000313|Proteomes:UP000275394}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100316 {ECO:0000313|EMBL:ROS01664.1,
RC   ECO:0000313|Proteomes:UP000275394};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (NOV-2018) 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}.
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:ROS01664.1}.
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; RKHR01000004; ROS01664.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2DPC3; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000275394; 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:UP000275394};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00572}.
FT   DOMAIN          30..304
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          439..562
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         243
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         245
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00572"
SQ   SEQUENCE   562 AA;  62178 MW;  AE10413E3D16F3C2 CRC64;
     MSFNHNKYRP FAPIKLADRQ WPSRTIDIAP DWCSVDLRDG NQALIKPMSV EQKLVMFKLL
     VEVGFKQIEV GFPAASQPDF DFVRCLIEQD LIPEDVTIQV LTQAREALIA RSYESLRGAR
     RAIVHVYNST STVQREQVFK QDRDAIKRIA TQGARWVQQY AAQQPETQWQ FQYSPESFTG
     TELDYAVEVC NAVIDIWQPS VEQPCIINLP ATVEVASPNV YADQIEWFCR HVDSRDAIIV
     SLHTHNDRGC GVAAAELGVM AGADRIEGTL LGNGERTGNM DIVTMAMNLY SQGVDPTLNF
     SDMKRIIEVV EYCTEIPVHP RHPYAGELVF TAFSGSHQDA IKKCLDLRQD DTDEAAWEVA
     YLPIDPADVG CSYEAVIRVN SQSGKGGVAH LLAADHGINL PRWAQVDFSP IVQAYAETQG
     GEVDSSTVLA LFRQHYQLDR ELQSEQYQIS SYQIEHGEHD TVAITLSNGN NEAIIKATAD
     GVLASFVQGL SRFSGHTIDI NNYVEHAIEG GSDARAIAFV QLCIEGSEII GAAEDGDIVT
     ASLTAVLAAF NRRQNSNIKA TA
//
DBGET integrated database retrieval system