ID A0A428PAU9_9HYPO Unreviewed; 594 AA.
AC A0A428PAU9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CEP54_012055 {ECO:0000313|EMBL:RSL50191.1};
OS Fusarium duplospermum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL50191.1, ECO:0000313|Proteomes:UP000288168};
RN [1] {ECO:0000313|EMBL:RSL50191.1, ECO:0000313|Proteomes:UP000288168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL50191.1,
RC ECO:0000313|Proteomes:UP000288168};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) 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:RSL50191.1}.
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DR EMBL; NKCI01000167; RSL50191.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A428PAU9; -.
DR STRING; 1325734.A0A428PAU9; -.
DR Proteomes; UP000288168; Unassembled WGS sequence.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
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; PTHR21000:SF13; DIHYDROXY-ACID DEHYDRATASE; 1.
DR PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 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 Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000288168}.
SQ SEQUENCE 594 AA; 64136 MW; 11B1A8BED72FC7BA CRC64;
MSRQYLNFPS LPDDAEKDGK LRLNRHSSYI TNEHDFPAAK TMLYAAGVPD EHTMQNSPQV
GIASVWWEGN PCNMHLLEIG KVAKEAVMKE GFLAWQYNTI GVSDGITMGH NGMRFSLQSR
EIIADSIETV TCAQSHDACI AIPGCDKNMP GCVMGIARHN RPSVIIYGGT QRGGFSKLLQ
RPIDINTSSE VRGAYILGRM NEWAKRSDYT PEELMCDVEK NAVPGPGACG GMYTANSLAV
VIEVLGLSIP GSSSSPAKSP TKMRECSSMG KIIRNCLEKN IRPSDLLTRK AFENALTMIM
CLGGSTNSVL HTIAMAKTAN VDLTLDDFQR ASNKTPYIAN MQPSGRYNME DLYNIGGIPS
VVKLLIAGGL LFGDTLTVTG KTLAENVESW PSLPQGQEII RSLDSPIKPT GHIEILRGNI
APGGAVAKIT GKQGLQFTGK ARVFDGEQAL CTALDKGQVP RDENIVLVVR YEGPKGGPGM
PEQLRASGSL IGGNFKNVAL ITDGRYSGAS HGFIVGHIVP EAAERGPIAI VEDDDVICID
AVSHRIDMPH VTEEEVKRRL GCLKPFEMPV TRGALAKYAH LVKDASRGAV TDIF
//