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Database: UniProt
Entry: A0A139I507_9PEZI
LinkDB: A0A139I507_9PEZI
Original site: A0A139I507_9PEZI 
ID   A0A139I507_9PEZI        Unreviewed;       221 AA.
AC   A0A139I507;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=AC579_9325 {ECO:0000313|EMBL:KXT09756.1};
OS   Pseudocercospora musae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX   NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT09756.1, ECO:0000313|Proteomes:UP000073492};
RN   [1] {ECO:0000313|EMBL:KXT09756.1, ECO:0000313|Proteomes:UP000073492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT09756.1,
RC   ECO:0000313|Proteomes:UP000073492};
RA   Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT   "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT   link between parallel evolutionary changes in Pseudocercospora fijiensis
RT   and Pseudocercospora eumusae and increased virulence on the banana host.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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:KXT09756.1}.
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DR   EMBL; LFZO01000309; KXT09755.1; -; Genomic_DNA.
DR   EMBL; LFZO01000309; KXT09756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139I507; -.
DR   Proteomes; UP000073492; 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   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   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:UP000073492}.
FT   COILED          30..57
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         221
FT                   /evidence="ECO:0000313|EMBL:KXT09756.1"
SQ   SEQUENCE   221 AA;  24258 MW;  CFD5F1007370F22D CRC64;
     MSSCQPSPEA CNACPEKTNG WSENGHSVDI EDYKTELSSL RARTKELEAK LSQLTIDSGK
     ELRSTKWFNR QDDKALSALY VERYLNYGLT KEELMSSKPI IGIANSGSDL TPCNRYHTTL
     SHRVREGIRS AGGIAIEFPT HPIQESTRRP TATLDRNLSY LTLVELLYAY PFDGVVLMTG
     CDKTTPACLM AAATVNIPAI CLNVGPMLNG YNHDSSSSSS S
//
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