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Database: UniProt
Entry: A0A498I0D3_MALDO
LinkDB: A0A498I0D3_MALDO
Original site: A0A498I0D3_MALDO 
ID   A0A498I0D3_MALDO        Unreviewed;       642 AA.
AC   A0A498I0D3;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE            EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN   ORFNames=DVH24_039401 {ECO:0000313|EMBL:RXH75702.1};
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH75702.1, ECO:0000313|Proteomes:UP000290289};
RN   [1] {ECO:0000313|EMBL:RXH75702.1, ECO:0000313|Proteomes:UP000290289}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC   TISSUE=Young leaf {ECO:0000313|EMBL:RXH75702.1};
RA   Hu J.;
RT   "A high-quality apple genome assembly.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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};
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:RXH75702.1}.
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DR   EMBL; RDQH01000341; RXH75702.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498I0D3; -.
DR   STRING; 3750.A0A498I0D3; -.
DR   UniPathway; UPA00048; UER00070.
DR   Proteomes; UP000290289; Chromosome 15.
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; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290289};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003523}.
FT   DOMAIN          87..373
FT                   /note="Pyruvate carboxyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS50991"
SQ   SEQUENCE   642 AA;  70108 MW;  42FC59DEAF09D9F0 CRC64;
     MAAVCTNPKI LPSPAATMSS VNIPNTSQSQ LLFRSHLHKP KMPKFLVSRP NLHNTCNPHI
     LCSQTDNPKP TPRPDYIPNR ISDPNYVRIF DTTLRDGEQS PGASLTSKEK LDIARKLAKL
     GVDIIEAGFP ASSKDDAEAV KMIAKEVGNA VDKDGYVPVI CGLSRCNRND IQTAWDAVKY
     AKRPRIHTFI ATSPIHLEYK LRKTKEQVIE IARNMVKFAR ELGCDDVEFS PEDAGRIIFL
     FFVVPYPTRS EREFLYQILG EVIKAGATTL NIPDTVGYNV PDEYSQLIAD IKSNTPGIDN
     IIISTHCQND LGLSTANTLA GACAGARQLE VTINGIGERA GNASLEEVVM TLNCRGEHVL
     GGLYTGINTK HIYVTSKMVE EYTGLHVQPH KAIVGANAFA HESGIHQDGM LKHKGTYEII
     SPEDIGYERS NEAGIVLGKL SGRHALRNRL AELGYELEDD QLATVFEHFK AVAEQKKIIT
     DADLGALVRD EVFQPEVVWK LHDLQVTCGT LGLSTATVKL IDADGREHVA CSVGTGPVDS
     AYKAVDLIVK EPVMLVEYSM NAVTEGNDAI ATTRVVIRPE NRRMVTHAHT GESVQRTFSG
     VAAGMDIVVS SVKAYIGALN KIIGFNKRSP TKIPAELTPV SA
//
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