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Database: UniProt
Entry: A0A0D2KVA9_9EURO
LinkDB: A0A0D2KVA9_9EURO
Original site: A0A0D2KVA9_9EURO 
ID   A0A0D2KVA9_9EURO        Unreviewed;       775 AA.
AC   A0A0D2KVA9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=Z520_03359 {ECO:0000313|EMBL:KIY00694.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIY00694.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIY00694.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIY00694.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) 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; KN848066; KIY00694.1; -; Genomic_DNA.
DR   RefSeq; XP_016634816.1; XM_016773870.1.
DR   AlphaFoldDB; A0A0D2KVA9; -.
DR   STRING; 1442371.A0A0D2KVA9; -.
DR   GeneID; 27709105; -.
DR   VEuPathDB; FungiDB:Z520_03359; -.
DR   OrthoDB; 1122834at2759; -.
DR   UniPathway; UPA00048; UER00071.
DR   Proteomes; UP000053411; 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:UP000053411}.
FT   DOMAIN          13..472
FT                   /note="Aconitase/3-isopropylmalate dehydratase large
FT                   subunit alpha/beta/alpha"
FT                   /evidence="ECO:0000259|Pfam:PF00330"
FT   DOMAIN          539..661
FT                   /note="Aconitase A/isopropylmalate dehydratase small
FT                   subunit swivel"
FT                   /evidence="ECO:0000259|Pfam:PF00694"
SQ   SEQUENCE   775 AA;  84379 MW;  A2F8E04E568ED9D5 CRC64;
     MPSIESTPRT LYDKVFQDHI VNEERDGTVL LYIDRHLVHE VTSPQAFEGL KNAKRKVRRP
     DCTLATTDHN VPTTSRKNFK NVADFVKEDD SRLQCITLED NVKEFGLTYF GLGDKNQGIV
     HIIGPEQGFT LPGTTVVCGD SHTSTHGAFG ALAFGIGTSE VEHVLATQCL ITKKSKNMRI
     QVDGQLAPGV SSKDIILHVI GVIGTAGGTG AVIEFCGSAI RSLSMEARMS ICNMSIEAGA
     RAGMIAPDQT TFDYLKGRPL APKVDSNEWK KATNYWASLR SDEGAKYDIE VFIDAKDIAP
     TVSWGTSPQD VVPITGVVPG PDDFEDPNRK ASCKRALEYM GLTPGTKMED IEVDKVFIGS
     CTNSRIEDMR AAAKIVEGKK VAPNIKRAMV VPGSGNIKAQ AESEGLDKIF LDAGFEWREA
     GCSMCLGMNP DILSPRERCA STSNRNFEGR QGALGRTHLV SPVMAAAAAI AGKLADVRKY
     SDNATPAKAD PKLDVRPEFA EVDSEEELDR ILDIPTDATS TATNHVEAGA GGAPGTGLPK
     FTVLKGIAAP LDKANVDTDA IIPKQFLKTI KRTGLGSALF HPLRYNEDGS ENPSFILNQE
     PYRQAKILVV TGPNFGCGSS REHAPWALLD FGIKCVIAPS YADIFFNNTF KNGMLPLIMP
     DQDKLNKIAD EARAGREVEV DLPNQVIRDA KGNELATFEV EEFRKHCLVE GLDDIGLTMQ
     MEDKIAQFEA KRTLDTPWLD GSGYLKKWRK GPVKIEAAPV PKTNRGDVKT DPVEW
//
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