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Database: UniProt
Entry: A0A1C7N2T9_9FUNG
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ID   A0A1C7N2T9_9FUNG        Unreviewed;       597 AA.
AC   A0A1C7N2T9;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   13-SEP-2023, entry version 29.
DE   RecName: Full=dihydroxy-acid dehydratase {ECO:0000256|ARBA:ARBA00029490};
DE            EC=4.2.1.9 {ECO:0000256|ARBA:ARBA00029490};
GN   Name=ilvD {ECO:0000313|EMBL:OBZ83341.1};
GN   ORFNames=A0J61_08612 {ECO:0000313|EMBL:OBZ83341.1};
OS   Choanephora cucurbitarum.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC   Choanephora.
OX   NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ83341.1, ECO:0000313|Proteomes:UP000093000};
RN   [1] {ECO:0000313|EMBL:OBZ83341.1, ECO:0000313|Proteomes:UP000093000}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ83341.1,
RC   ECO:0000313|Proteomes:UP000093000};
RA   Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT   "Choanephora cucurbitarum.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate
CC         + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:49072; EC=4.2.1.9;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24810;
CC         Evidence={ECO:0000256|ARBA:ARBA00029304};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00029437}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 3/4. {ECO:0000256|ARBA:ARBA00029436}.
CC   -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC       {ECO:0000256|ARBA:ARBA00006486}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OBZ83341.1}.
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DR   EMBL; LUGH01000680; OBZ83341.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7N2T9; -.
DR   STRING; 101091.A0A1C7N2T9; -.
DR   InParanoid; A0A1C7N2T9; -.
DR   OrthoDB; 238at2759; -.
DR   UniPathway; UPA00047; UER00057.
DR   UniPathway; UPA00049; UER00061.
DR   Proteomes; UP000093000; Unassembled WGS sequence.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR   HAMAP; MF_00012; IlvD; 1.
DR   InterPro; IPR042096; Dihydro-acid_dehy_C.
DR   InterPro; IPR004404; DihydroxyA_deHydtase.
DR   InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR   InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR   InterPro; IPR037237; IlvD/EDD_N.
DR   NCBIfam; TIGR00110; ilvD; 1.
DR   PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1.
DR   PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00920; ILVD_EDD; 1.
DR   SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR   SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR   PROSITE; PS00886; ILVD_EDD_1; 1.
DR   PROSITE; PS00887; ILVD_EDD_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093000}.
SQ   SEQUENCE   597 AA;  63722 MW;  44B54C8D39213D77 CRC64;
     MASKLLTRVK PLTTHSLRDA SKVLPVGLRY YASDNTKRLN KYSATITQPK SQGASQAMLY
     ATGLTDEDMN KAQVGISSVW YEGNPCNMHL MDLAGEVKKG VQDAGLIGYR FNTIGVSDGI
     SMGTRGMSYS LQSRDLIADS IETVMGGQWY DANISIPGCD KNMPGVLMAM GRINRPSLMV
     YGGTIQPGKS CGGDKLDIVS AFQAYGEYVS GSIDEDRRYD IIRHACPGPG ACGGMYTANT
     MASAAEAMGM TLPYSSSTPA AYPEKIAECR NAGLAIRNLL EKDIKPRDIM TRAAFENAIV
     LTMVLGGSTN VVLHLIAIAR SVGVNLTLDD FQAASDKTPL LADLKPSGKY VMEDLHGAGG
     IPAILKYLME EGRVDGNVMT VTGKSLEENL HSLPGLPHGQ DIIRPLSNPI KSTGHLQILR
     GNLAPEGSVA KITGKEGLQF TGKARVFDGE ENFITALENN EFKKGEKTVV VIRNEGPKGG
     PGMREMLKPS SAIMGAGLGK DVALLTDGRF SGGSHGFIIG HVCPEAYVGG PIGLVKDGDE
     ITIDAESREM NMNVSNEELA ERKKSFVPPP PKYTRGTLAR YVLTVKSASE GAVTDEA
//
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