ID A0A0G4L047_9PEZI Unreviewed; 719 AA.
AC A0A0G4L047;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00011998};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
GN ORFNames=BN1708_011329 {ECO:0000313|EMBL:CRK15060.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK15060.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK15060.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK15060.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-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}.
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 -!- 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.
CC {ECO:0000256|ARBA:ARBA00004729}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185}.
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DR EMBL; CVQH01006113; CRK15060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4L047; -.
DR STRING; 100787.A0A0G4L047; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000044602; 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; 3.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR004431; 3-IsopropMal_deHydase_ssu.
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; TIGR00171; leuD; 1.
DR PANTHER; PTHR43822:SF9; 3-ISOPROPYLMALATE DEHYDRATASE; 1.
DR PANTHER; PTHR43822; HOMOACONITASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00330; Aconitase; 2.
DR Pfam; PF00694; Aconitase_C; 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 Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Leucine biosynthesis {ECO:0000256|ARBA:ARBA00022430};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 13..136
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 134..426
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 508..604
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 448..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 77954 MW; 7BD9049E57787C17 CRC64;
MPVAEGSQQT LYDKVLQAHV VDEKLDGTLL LYIDRHLVHE VTSPQAFEGL KNAGRQVRRP
DCTLATTDHN VPTTSRASMK DIGSFIDEDD SRLQCMTLEE NVKDFGLTYF GLGDKRQGIV
HVIGPEQGFT LPGTTVDGEL APGVSSKDVV LHAIGMIGTA GGNGAVIEFC GSVIRSLSME
ARMSICNMSI EGGARAGMVA PDEITFEYLK GRPLAPKVGS EEWERATTYW KSLQSDAGAV
YDIDVFIDAK DIIPTVTWGT SPEDVIPITG TVPDPETFAT EAKKAGGRRK LEYMGLIAGT
PMDQIVVDKV FIGSCTNSRI EDLRAAANVV KGKKIAANIK RAMIVPGSGL VKDQAEAEGL
DKIFIDAGFE WREAGCSMCL GMNPDILSPQ ERCASTSNRN FEGRQGAGGR THLMSPVMAA
AAAIVGTLTD VRKLSEYKTS PHVQAAIAPA AKPHVDERVE ESAAERDLIG DQPEDSQPHV
NSSVSSSSAG LPKFTTLKGI AAPLDMTNFL KTIKRTGLGS ALFHELRFNG DGSENPAFVL
NQDPYRQAKI LVVTGPNFGC GSSREHAPWA LLDFGIKTII APSYSDIFFN NTFKNGMLPI
IVSNKDDLEA VAAEARAGRD VEIDLPNQLI KNATGYTICS FDVEEFRKHC LVNGLDDIGL
TMQMDDKISE YERRMSKQTP WLDGTAYLKR KGRSNQLAAK PVPVPKTNRG ETKTEPLEW
//
