ID A0A2H3J7B1_WOLCO Unreviewed; 797 AA.
AC A0A2H3J7B1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=WOLCODRAFT_135865 {ECO:0000313|EMBL:PCH37821.1};
OS Wolfiporia cocos (strain MD-104) (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phaeolaceae; Wolfiporia.
OX NCBI_TaxID=742152 {ECO:0000313|EMBL:PCH37821.1, ECO:0000313|Proteomes:UP000218811};
RN [1] {ECO:0000313|EMBL:PCH37821.1, ECO:0000313|Proteomes:UP000218811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-104 {ECO:0000313|EMBL:PCH37821.1,
RC ECO:0000313|Proteomes:UP000218811};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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 2 subfamily. {ECO:0000256|ARBA:ARBA00009767}.
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DR EMBL; KB467942; PCH37821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3J7B1; -.
DR STRING; 742152.A0A2H3J7B1; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000218811; Unassembled WGS sequence.
DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro.
DR CDD; cd07942; DRE_TIM_LeuA; 1.
DR Gene3D; 3.30.160.270; -; 2.
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; 2.
DR SMART; SM00917; LeuA_dimer; 2.
DR SUPFAM; SSF110921; 2-isopropylmalate synthase LeuA, allosteric (dimerisation) domain; 2.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 2.
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:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000218811};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..312
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 797 AA; 87546 MW; 7E9EB976DCCB04BF CRC64;
MPMLADPSQK YKPYTPLNLP DRQWPSKVIT KPPIWLSTDL RDGNQALANP MTIPQKTLFF
QTLLKCGFKE IEVAYPAASD TDFNFVRGLI EQKQVPDDVW VQVLTPARED LIKRTVESVA
GAKRAIIHMY NATSCLFREV VFRHSKEETL ALAVKHTKII KQLTEECTAK YGTIFKYEYS
PETFTQTEPE FAVEVCEAVK AAWGKAGLGD ERIIFNLPAT VEVGPPNHYA DQVEYFCRHI
SEREKCAISL HPHNDRGQGI AAAELAMLAG ADRVEGCLFG NGERTGNVDI VNLALNQYTQ
GISPGLDFSD LPTIIDVVTQ CNDLPVHPRH PYAGELVFTA FSGSHQDAIK KGFEAQRVRH
AEAAKKGEKQ YWHMPYLPID PAELGCTYEA VIRVNAQSGK GGIAYLVQQH LGLDMPRKMQ
ISFYQVVQEV ADREAREMSV EDITATFRRT YHYGGSSFEG RLVLKSFKIS AGPSSSGDEA
ADERRQFDGA LSVDGVLRVI RGDGNGPLSA LLDALRTHLD IDLSLREYSE HAIGQGQDSK
AASYVELVPP ARDIKEIRQS TSSWWGVGVD ADIAGSGLRA VLSAVNNAIG DRELPELKLS
VGYSASTSQA DIASIILNEL GLELPRRLQA AFFETVQRAA RVSDGKMSYG DLVTLFRTTY
NYEVPDRSSR FAVKNFKMEN LGESGRKELT GEFMINGKLT QVAGEGNGLL TAAIAALNTH
IDGRVSIREY AEHSIGEGSD AKAASYVELA YEADGGAIKL NSWGIAKDTD ITASGLKALL
SACSGVDAMH RKITQQN
//
