ID A0A0D2AWF0_9EURO Unreviewed; 630 AA.
AC A0A0D2AWF0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KIW29582.1};
GN ORFNames=PV07_05388 {ECO:0000313|EMBL:KIW29582.1};
OS Cladophialophora immunda.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=569365 {ECO:0000313|EMBL:KIW29582.1, ECO:0000313|Proteomes:UP000054466};
RN [1] {ECO:0000313|EMBL:KIW29582.1, ECO:0000313|Proteomes:UP000054466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 83496 {ECO:0000313|EMBL:KIW29582.1,
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; KN847042; KIW29582.1; -; Genomic_DNA.
DR RefSeq; XP_016249798.1; XM_016392279.1.
DR AlphaFoldDB; A0A0D2AWF0; -.
DR STRING; 569365.A0A0D2AWF0; -.
DR GeneID; 27344582; -.
DR VEuPathDB; FungiDB:PV07_05388; -.
DR HOGENOM; CLU_014271_3_0_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 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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 66980 MW; 27F7C5D1D526441F CRC64;
MATNQPSTAP AQNGDSHSSI SKDYDLSQPI TSTSGLRSGL TSYGDAHFSL FLRKVFIKAL
GYSDSALSSP IIGVINTYSS FNPCHSNVPQ LIESVKRGVL ASGGLPVDFP TISIHESFAS
PTSMYLRNLM SMDTEEMIKA QPVDAVVMIG GCDKTVPAQL MGAISANKPV IPLITGPMMP
GSVEGVRVGA CTDCRSYWAR YRAGGVDLED IMSVNEELAP TGGTCGVMGT ASTMACVTAG
LGLLELKSGA TAAAVSSARL RVAEQAGRNA VAMLTKDGMR PQDLLTRESF LNAITVLQAI
GGSTNAVVHL LAIINRHPKV AGTIDLNTFD EIGRKTPLLV DLKPSGDNYM TDFHNAGGML
ALMHTLRPLL HLGAKTYSGQ TLGELLDTTP FKSFQYSRQI VRSLQDPLYP SSSLVVLHGN
ICPQGAVMKA SASKDRKLLH HRGSACVFEN TADMANRIDS PDLEVDANSV LILKSIGPVG
NPGMPEAGLI PIPQKLGKQG VTDMLRISDG RMSGTAGGTI ILHISPESAD LDSVFGVVQT
GDKIICDVEK RTLLLEVEEQ EIARRIADRK TRSQVASASG KADGQMSHNP EPWVERAGRR
GYRGLYEREV NQAHLGCDFG FLTAKGPSGT
//
