ID A0A0C9YDI4_9AGAR Unreviewed; 736 AA.
AC A0A0C9YDI4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
DE RecName: Full=3-isopropylmalate dehydratase {ECO:0000256|ARBA:ARBA00014371};
DE EC=4.2.1.33 {ECO:0000256|ARBA:ARBA00011998};
DE AltName: Full=Alpha-IPM isomerase {ECO:0000256|ARBA:ARBA00031631};
DE AltName: Full=Isopropylmalate isomerase {ECO:0000256|ARBA:ARBA00033368};
GN ORFNames=K443DRAFT_85266 {ECO:0000313|EMBL:KIK08417.1};
OS Laccaria amethystina LaAM-08-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hydnangiaceae; Laccaria.
OX NCBI_TaxID=1095629 {ECO:0000313|EMBL:KIK08417.1, ECO:0000313|Proteomes:UP000054477};
RN [1] {ECO:0000313|EMBL:KIK08417.1, ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|EMBL:KIK08417.1,
RC ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LaAM-08-1 {ECO:0000313|Proteomes:UP000054477};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
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}.
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; KN838542; KIK08417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9YDI4; -.
DR STRING; 1095629.A0A0C9YDI4; -.
DR HOGENOM; CLU_006714_1_2_1; -.
DR OrthoDB; 1122834at2759; -.
DR UniPathway; UPA00048; UER00071.
DR Proteomes; UP000054477; 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; 2.
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:UP000054477}.
FT DOMAIN 13..473
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 515..637
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 482..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 79953 MW; 587569A75EECA9ED CRC64;
MPSAIPTPRT LYDKIWDDHV VDVKEDGLAL IYIDRHLVHE VTSPQAFEGL RNAGRPVRRP
DCTLATVDHN VPTVSRKNFT SVESFIAEPD SRAQCAALED NVKEFGLTYF GMKDRRQGIV
HVIGPEQGFT LPGITCVCGD SHTSTHGAFG SLAFGIGTSE VEHVLATQTL LQKKGKNMRI
TVDGELHEGV TSKDVILHII GVIGTAGGTG CVIEYAGSVF RGFSMEARMS VCNMSIEAGA
RAGMIAPDDV TFNYLRNRPL SPKGDEWDHA VTYWRSLKTD EGAKFDIEVN IPASDIIPTV
TWGTSPQDVV PITGSVPDPS KMSDSGKRAS AERSLAYMGL TANTSMEEIK VDKVFIGSCT
NSRIEDLRSA AKIVLAAGPD AKVAPGVVAM IVPGSGLIKQ HAEAEGLDVV FKRAGFDWRE
AGCSMCLGMN PDQLAPGERC ASTSNRNFEG RQGAGGRTHL LSPAMAAAAA ITGKLTDVRN
DFLDEPQASP SPAAKQSSDG TSSALPAITS PTSVEKFVIW RGIAAPLHIE NVDTDMIIPK
QFLKTLKRTG LAEALFYTLR KDPHTGKVTD FILNRAPYDQ SKIIVCTGKN FGCGSSREHA
PWSLNDFGIR CVIAPSFADI FRNNAMQNGM LPVAVPEEDC RALARDAEAG LELEVDLEAE
EIRRANGQRS VKFTTDPFRR HCLLNGLDDI ALTMQRRASI EIFEKTRSEM WPWLDGFGYQ
GKIPVGATKR TKKTDW
//