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
//