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Database: UniProt
Entry: A0A0C9YDI4_9AGAR
LinkDB: A0A0C9YDI4_9AGAR
Original site: A0A0C9YDI4_9AGAR 
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
//
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