ID A0A0D1Z653_9EURO Unreviewed; 649 AA.
AC A0A0D1Z653;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KIW23041.1};
GN ORFNames=PV07_11273 {ECO:0000313|EMBL:KIW23041.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW23041.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW23041.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW23041.1,
RC ECO:0000313|Proteomes:UP000054466};
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 Cladophialophora immunda CBS83496.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; KN847046; KIW23041.1; -; Genomic_DNA.
DR RefSeq; XP_016243257.1; XM_016398695.1.
DR AlphaFoldDB; A0A0D1Z653; -.
DR STRING; 569365.A0A0D1Z653; -.
DR GeneID; 27350467; -.
DR VEuPathDB; FungiDB:PV07_11273; -.
DR HOGENOM; CLU_014271_3_1_1; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000054466; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054466}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..49
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 70842 MW; A7B305EF530C8020 CRC64;
MTESCGKGCN QPCREQNDTP DIEDFRTEIK SLKQRNEELA RKLSDLAYAG STSSSRTLRS
ENWFSNDREP ALSTLYADRY LNFGLTTEEL MSKKPVIGIA QSGSDLSPCN RYHVQTAKRM
REGIIAAGAI PLEFSTHPIQ ESSRRPTATL DRNLAYLVLV EILHSYPLDG VVLLTGCDKT
TPACLMAAAT VNIPAICLNV GPMLNGRRNR DLIGTGTILW RARELKAEGT IDDTEFFDMV
TSGTPSAGHC NTMGTASSMN ALAEALGMAL PGSAAIPAVY RERLQCAYKT GQQIVEMVHS
NRRPSDIMTR EAFENAIVVN SAIGGSSNCP IHLIAIARHM GITLDLDDWD RLGYRIPLLV
NVQPAGEMLC EEYHHAGGLP AVMAELLAAG KLHAKALSCT GRTIGDIVKG KFSWDRKTIR
PYGEPLKKNA GFLHLKGTLF DSAIMKTSVI SEEFEAKFLW NASQPGKFAA FECKARVFDG
PEDYNEHLDD NVPMDDRTVL VMRGAGPIGY PGAPEVVNMH APGRLLKAGV RSLPCIGDGR
QSGTSGSPSI LHASPEAAAG GNLAILRTGD TIRIDLESRR VDLLLSDEEI RSRRATVAGK
MEELTAPSQT PWQDIFRREV GQLSDGMALK NAVNYQRIAD HFAVPRHNH
//
