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Database: UniProt
Entry: A0A372JV24_9BURK
LinkDB: A0A372JV24_9BURK
Original site: A0A372JV24_9BURK 
ID   A0A372JV24_9BURK        Unreviewed;       516 AA.
AC   A0A372JV24;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00018198, ECO:0000256|HAMAP-Rule:MF_01025};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973, ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-IPM synthase {ECO:0000256|ARBA:ARBA00029993, ECO:0000256|HAMAP-Rule:MF_01025};
DE   AltName: Full=Alpha-isopropylmalate synthase {ECO:0000256|HAMAP-Rule:MF_01025};
GN   Name=leuA {ECO:0000256|HAMAP-Rule:MF_01025};
GN   ORFNames=D0B32_31240 {ECO:0000313|EMBL:RFU43810.1};
OS   Paraburkholderia sp. DHOC27.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU43810.1, ECO:0000313|Proteomes:UP000263097};
RN   [1] {ECO:0000313|EMBL:RFU43810.1, ECO:0000313|Proteomes:UP000263097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHOC27 {ECO:0000313|EMBL:RFU43810.1,
RC   ECO:0000313|Proteomes:UP000263097};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL   Submitted (AUG-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_01025}.
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|HAMAP-Rule:MF_01025};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01025};
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_01025}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01025}.
CC   -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase
CC       family. LeuA type 1 subfamily. {ECO:0000256|ARBA:ARBA00009396,
CC       ECO:0000256|HAMAP-Rule:MF_01025}.
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:RFU43810.1}.
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DR   EMBL; QVQV01000014; RFU43810.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372JV24; -.
DR   OrthoDB; 9803573at2; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000263097; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
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:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniRule.
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   HAMAP; MF_01025; LeuA_type1; 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   Acyltransferase {ECO:0000313|EMBL:RFU43810.1};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01025};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_01025};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01025};
KW   Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430, ECO:0000256|HAMAP-
KW   Rule:MF_01025};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01025};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01025}; Reference proteome {ECO:0000313|Proteomes:UP000263097};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01025}.
FT   DOMAIN          5..268
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
FT   REGION          395..516
FT                   /note="Regulatory domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         14
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         204
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
FT   BINDING         239
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01025"
SQ   SEQUENCE   516 AA;  55874 MW;  7B1DD03F88635D92 CRC64;
     MADKLIIFDT TLRDGEQSPG ASMTKEEKIR IAKQLERMKV DVIEAGFAAS SNGDFDAIHT
     IASMVKDSTV CSLARANDKD IQRAADALKP ADHFRIHTFI ATSPLHMEKK LRMTPDQVFE
     QAKLAVRFAR KFTNDVEFSP EDGSRSDMDF LCRVLEAVIA EGATTINIAD TVGYGVPELY
     GQLVKTLRER IPNSDKAVFS VHCHNDLGMA VANSLAGVQI GGARQVECTI NGLGERAGNT
     SLEEIVMAVK TRKDYFGLEV GLDTTQIVPA SKLVSQVTGF VVQPNKAVVG ANAFAHASGI
     HQDGVLKARD TYEIMRAEDV GWSANKIVLG KLSGRNAFKQ RLQELGVALD SEAALNTAFA
     RFKELADRKA EIFDEDIMSI VTEESEEAQQ KEHYKFVSLA QRSETGEQPQ ARIVFSMEGK
     EVTGEARGNG PVDATLNAIE SEVGSGSELL LYSVNAITTG TQAQGEVTVR LSKSGRIVNG
     VGTDPDIVAA SAKAYISALN KLYSNDKLNP QRSEGP
//
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