ID A0A074W8L5_9PEZI Unreviewed; 604 AA.
AC A0A074W8L5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative dihydroxy-acid dehydratase {ECO:0000313|EMBL:KEQ69213.1};
GN ORFNames=M436DRAFT_56459 {ECO:0000313|EMBL:KEQ69213.1};
OS Aureobasidium namibiae CBS 147.97.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043004 {ECO:0000313|EMBL:KEQ69213.1, ECO:0000313|Proteomes:UP000027730};
RN [1] {ECO:0000313|EMBL:KEQ69213.1, ECO:0000313|Proteomes:UP000027730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 147.97 {ECO:0000313|EMBL:KEQ69213.1,
RC ECO:0000313|Proteomes:UP000027730};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; KL584722; KEQ69213.1; -; Genomic_DNA.
DR RefSeq; XP_013423473.1; XM_013568019.1.
DR AlphaFoldDB; A0A074W8L5; -.
DR STRING; 1043004.A0A074W8L5; -.
DR GeneID; 25412319; -.
DR HOGENOM; CLU_014271_3_0_1; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000027730; 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:UP000027730}.
SQ SEQUENCE 604 AA; 64348 MW; 82CF6DB3BE07873E CRC64;
MDHQETKIDP QDDYDLSKPL AATTGLRQGL TSYGDAHFSL FLRKVFIKAA GYGEDALSRP
IIGIINTYSA FNPCHANIPQ LLEAVKRGIH LQGGLAIEFP TISVHESFSS PTSMFLRNLM
SMDTEEMIKA QPVDAVVAIG GCDKTVPAQL MGAISANKVC LPLVTGPMMP GSSRGVRVGA
CTDCRSHWAA YRAGEIDMED IGAVNEELAP TAGTCGVMGT ASTMACVTVA LGLMPFDGAS
AAAVSSARLR IAERTGANAV AAAAAKRLPQ SILTKESFLN AIIVLQAIGG STNAVVHLMA
IVNRHPEVAG SITLETFDEV GRNTPLLVDL KPTGDNYMTD FHNAGGMLAL LHTLRPLLHL
EAKTINGKTL GEELETTPFK PFKYSSELIR PLSNPLYPES AIVVLRGNMA PRGAVMKAAA
SKDRSLLSHI GRAVVFQNTA DMAQRIDDPD LPVTKDSVLV LQSVGPIGNP GMPEAGVIPI
PRKLGAQGVK DMLRISDGRM SGTAGGTIVL HVSPESALPD SVFGCVKDGD LIECDVEKRL
LRLHVSDEEL AKRVAARLAA KKREEHGTRR ISGKQRGYRG LYERCVNQAE EGADFDFLTA
AGPI
//
