ID A0A317W7U5_9EURO Unreviewed; 668 AA.
AC A0A317W7U5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Dihydroxy-acid and 6-phosphogluconate dehydratase {ECO:0000313|EMBL:PWY81751.1};
GN ORFNames=BO94DRAFT_558151 {ECO:0000313|EMBL:PWY81751.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY81751.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY81751.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY81751.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) 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:PWY81751.1}.
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DR EMBL; MSFK01000020; PWY81751.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317W7U5; -.
DR STRING; 1450535.A0A317W7U5; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000246702; 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:UP000246702}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 58..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72082 MW; 7C7AB3FECA815E41 CRC64;
MTKHGSPPSG HRPRRHASVN PHTRADHSRA IHYYDHAPCS INLSIYLYIH LYHKSTQNAP
SHIPSHPQPN DYDLTTPIPS TTGLRQTLPS YGDAHFSLFL RKVFIKALGY TEDALSRPII
GIINTNSGFN PCHGNAPQLI EAAKRGIHLN GGIAIDFPTI SIHEGFSHPT SMFLRNLMSM
DTEEMIKAQP VDACVMIGGC DKTVPAQIMG GISANKPVLP LLTGPMMPGS HRGKRVGACT
DCRNNWASFR AGTIDLEEIM AVNEELAPTI GTCGVMGTAS TMACITAALG LIPLQGASAP
AVSATRLRIA EQTGANAVAA AKAQRTPQTL LSVQSFYNAA IVLQAIGGST NAMVHLMAMV
NRHPDIKGEF SLETLDKIGR TTPLLVDLKP SGDNYMTDFH NAGGMICLLH RLRPLLHLSA
RTITGETMGE VLDRTPFRDF EYSRSIIRPL EDPLYACSSL AVVRGNIAPN GAVIKASASK
DKRLLKHEGR AVVFENSQDL TKRIDDPELE VDANSVLVLK GIGPIGNPGM PEAGMIPIPR
KLAAQGVTDM LRVSDGRMSG TAGGTIVLHV SPEAAVPGSA FGVVETGDLI RFDAEERRLE
LVVEEGVMET RIERRRAEIM GSAGGEKASV WTQRQTRRGY RGLYERTVNQ AHQGADFDFL
TASGPMSD
//