ID C1GHU8_PARBD Unreviewed; 647 AA.
AC C1GHU8;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=2-isopropylmalate synthase {ECO:0000256|ARBA:ARBA00012973};
DE EC=2.3.3.13 {ECO:0000256|ARBA:ARBA00012973};
GN ORFNames=PADG_06834 {ECO:0000313|EMBL:EEH50755.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH50755.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH50755.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH50755.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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; KN275965; EEH50755.2; -; Genomic_DNA.
DR RefSeq; XP_010762108.1; XM_010763806.1.
DR AlphaFoldDB; C1GHU8; -.
DR STRING; 502780.C1GHU8; -.
DR GeneID; 22585463; -.
DR KEGG; pbn:PADG_06834; -.
DR VEuPathDB; FungiDB:PADG_06834; -.
DR eggNOG; KOG2367; Eukaryota.
DR HOGENOM; CLU_004588_3_0_1; -.
DR InParanoid; C1GHU8; -.
DR OMA; WPDKVID; -.
DR OrthoDB; 275559at2759; -.
DR Proteomes; UP000001628; 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; -; 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:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..311
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
SQ SEQUENCE 647 AA; 71781 MW; AEE8C3DD83A2F5F6 CRC64;
MPMLKDPSKK YQRFKPLDLP NRQWPSKTID KPPRWLTTDL RDGNQSLVDP MDGDQKLRFF
RMLVEIGYKE IEISFPSASQ TDFDFTRRLI ETPGEVPDDV WLQVLCPCRE DFIRRTVESL
KGAKKAILHL YLATSECFQR IVFGMTRQES LELAVQSTKY ARSITKDDPS TAGTEWLFEF
SPETFSDSDP DFVLEICEAV KAAWEPTVEA PLIFNLPATV EMSTPNAYAD QIEYFSTHIS
EREKVCVSLH PHNDRGCAVA AAELAQMAGA QRVEGTLFGN GERTGNVDLV TLALNLYTQG
ISPKVDFSDI NSIIKVVEES NKIPVNERCP YGGQLVVCAF SGSHQDAIKK GFQLREKTHA
TDEDRWQIPY LPIDPRDIGR NYEAIIRVNS QSGKGGVAWV ILRSLELDLP RGLQVAFSKI
IQKQADALGR ELLPKEIVSL FEDSYHLKQN PRFSLVDYNI TTDRSQSPTA PQPGKALNTQ
NLKRRFAGII EIDGLQHAIV GVGNGAISSL ANALKSLGID LDVVDYKEHA IGAHRDTKAA
TYIECTSTNS SEKVWGVGIH HDVVQASLTA LLSAASSFLT SRATTPAPFR PSRVEALSQA
DLEALYQIQG NTGPARALLP DNANLGATFT QPKVDIAKLE TQVNGFK
//
