ID W9YJM7_9EURO Unreviewed; 619 AA.
AC W9YJM7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:EXJ93112.1};
GN ORFNames=A1O3_01668 {ECO:0000313|EMBL:EXJ93112.1};
OS Capronia epimyces CBS 606.96.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX NCBI_TaxID=1182542 {ECO:0000313|EMBL:EXJ93112.1, ECO:0000313|Proteomes:UP000019478};
RN [1] {ECO:0000313|EMBL:EXJ93112.1, ECO:0000313|Proteomes:UP000019478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 606.96 {ECO:0000313|EMBL:EXJ93112.1,
RC ECO:0000313|Proteomes:UP000019478};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia epimyces CBS 606.96.";
RL Submitted (MAR-2013) 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:EXJ93112.1}.
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DR EMBL; AMGY01000001; EXJ93112.1; -; Genomic_DNA.
DR RefSeq; XP_007730002.1; XM_007731812.1.
DR AlphaFoldDB; W9YJM7; -.
DR STRING; 1182542.W9YJM7; -.
DR GeneID; 19165802; -.
DR eggNOG; KOG2448; Eukaryota.
DR HOGENOM; CLU_014271_3_0_1; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000019478; 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:UP000019478}.
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 66108 MW; 8ECF912C14D84C60 CRC64;
MDSHDTSKAD GSPDVHSSDY DLSRPITSTS GLRSGLTSYG DAHFSLFLRK VFIKALGYSD
SALSLPIIGI INTYSSFNPC HSNVPQLIES VKRGVLASGG LPVDFPTISV HESFSSPTSM
YLRNLMSMDT EEMIKAQPVD AVVMIGGCDK TVPAQLMGGI SANKPVIPLI TGPMIPGSVE
GVRVGACTDC RSYWAKYRAG DVDLEDIMSV NEELAPTGGT CGVMGTASTM ACVTAALGLL
DLRAGATSAA VSSARLRVAE QAGRNAVAML KMEHSRPQDL LTRESFLNAI TVLQAIGGST
NAVVHLMAII NRHPKVAGTI DLSTIDEIGK KTPLLVDLKP SGDNYMTDFH NAGGMLTLMK
TLRPLLHLNA RTYTGQTLGE LLDSSPSKLF PYARQIVRSL EGPLYPNSSL VVLYGNVCPN
GAVMKASASK NRKLLQHSGR ACVFENSADM ARRIDSPDLD VDADSVLVLK SIGPVGNPGM
PEAGLIPIPQ KLGRQGVTDM LRISDGRMSG TAGGTIILHI APESADLDSV FGVVETGDRI
VCDVENRKLL LDVDEHEISR RIAERKKSAQ SVSSSGSREP WVERAHVRGY RGLYEREVNQ
AHLGCDFGFL TAQGPTISQ
//