ID E9DEV0_COCPS Unreviewed; 773 AA.
AC E9DEV0;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00014371, ECO:0000256|PIRNR:PIRNR001418};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998, ECO:0000256|PIRNR:PIRNR001418};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|ARBA:ARBA00031631, ECO:0000256|PIRNR:PIRNR001418};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|ARBA:ARBA00033368, ECO:0000256|PIRNR:PIRNR001418};
GN ORFNames=CPSG_08350 {ECO:0000313|EMBL:EFW15162.1};
OS Coccidioides posadasii (strain RMSCC 757 / Silveira) (Valley fever fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=443226 {ECO:0000313|Proteomes:UP000002497};
RN [1] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
RN [2] {ECO:0000313|Proteomes:UP000002497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 757 / Silveira {ECO:0000313|Proteomes:UP000002497};
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Orbach M., Henn M.R., Cole G.T., Galgiani J., Gardner M.J.,
RA Kirkland T.N., Taylor J.W., Young S.K., Zeng Q., Koehrsen M., Alvarado L.,
RA Berlin A., Borenstein D., Chapman S.B., Chen Z., Engels R., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Jen D., Larson L., Mehta T., Neiman D., Park D., Pearson M.,
RA Richards J., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Walk T., White J., Yandava C., Haas B., Nusbaum C., Birren B.;
RT "The genome sequence of Coccidioides posadasii strain Silveira.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-
CC isopropylmalate, via the formation of 2-isopropylmaleate.
CC {ECO:0000256|ARBA:ARBA00002695, ECO:0000256|PIRNR:PIRNR001418}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate;
CC Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121;
CC EC=4.2.1.33; Evidence={ECO:0000256|ARBA:ARBA00000491,
CC ECO:0000256|PIRNR:PIRNR001418};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine
CC from 3-methyl-2-oxobutanoate: step 2/4. {ECO:0000256|ARBA:ARBA00004729,
CC ECO:0000256|PIRNR:PIRNR001418}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|PIRNR:PIRNR001418}.
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DR EMBL; GL636502; EFW15162.1; -; Genomic_DNA.
DR STRING; 443226.E9DEV0; -.
DR VEuPathDB; FungiDB:CPSG_08350; -.
DR VEuPathDB; FungiDB:D8B26_004501; -.
DR eggNOG; KOG0454; Eukaryota.
DR HOGENOM; CLU_006714_0_1_1; -.
DR OMA; EDNEPHT; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000002497; Unassembled WGS sequence.
DR GO; GO:0009316; C:3-isopropylmalate dehydratase complex; IEA:InterPro.
DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01583; IPMI; 1.
DR CDD; cd01577; IPMI_Swivel; 1.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR HAMAP; MF_01026; LeuC_type1; 1.
DR HAMAP; MF_01031; LeuD_type1; 1.
DR InterPro; IPR004430; 3-IsopropMal_deHydase_lsu.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
DR InterPro; IPR012235; 3-IsopropMal_deHydtase_ssu/lsu.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR InterPro; IPR033941; IPMI_cat.
DR InterPro; IPR033940; IPMI_Swivel.
DR NCBIfam; TIGR00170; leuC; 1.
DR NCBIfam; TIGR00171; leuD; 1.
DR PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PIRSF; PIRSF001418; ACN; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR001418};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PIRNR:PIRNR001418}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430,
KW ECO:0000256|PIRNR:PIRNR001418};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR001418};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002497}.
SQ SEQUENCE 773 AA; 84396 MW; BA9F45167253B968 CRC64;
MPSAEKRPKT LYDKVFQDHV VNEQDDGTIL LYIDRHLVHE VTSPQAFEGL KNAGRRVRRP
DCTLATVDHN VPTTSRKTFK NVADFVQEAD SRLQCLTLEE NVKDFGLTYF GLGDKRQGIV
HIIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQTL ITKRSKNMRV
QVEGDLLPGV TSKDVVLHVI GVIGTAGGTG CVIEFCGSAI RGLSMEARMS ICNMSIEAGA
RAGMIAPDEI TFEYLKGRPL APKYDSAEWK KAVKYWSSLK SDEGASYDKE VFIDAKDIAP
TVSWGTSPQD VVAITGVVPG PDDFDDEVKK ASARRALEYM GLTAGTRMQD ISIDKVFIGS
CTNSRLEDLR SAAHIVQGKK VAPNVKRAMI VPGSGLVKEQ AEEEGLDKIF LDAGFEWREA
GCSMCLGMNP DILSPRERCA STSNRNFEGR QGAGGRTHLM SPVMAAAAAI VGKLADVRDL
THAVPISKRA SPKVEVQPEV DDIDTDDDLD RILDCPNDSE PHTNCSASKS SSGLPKFTTL
KGIAAHLDRA NVDTDAIIPK QFLKTIKRTG LGSALFYSLR YNEDGSENPD FILNKEPYRQ
SKILVGGENF GCGSSREHAP WALLDFGIKC VIAPSFADIF FNNTFKNGML PVIIRDEAAL
KKIAAEAERG NDIEVDLVNQ RINDATGSKL ADFDVEQFRK HCLVNGLDDI GLTMQMEDQI
KEFERIRSQE TPWLDGSGYL KQKNGRKTGP VMVEAAPVPK TNRGEVKGEP LEW
//
