ID A0A3F3PW21_9EURO Unreviewed; 395 AA.
AC A0A3F3PW21;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Dihydroxyacid dehydratase {ECO:0000313|EMBL:RDH31141.1};
GN ORFNames=BDQ94DRAFT_147537 {ECO:0000313|EMBL:RDH31141.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31141.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31141.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31141.1,
RC ECO:0000313|Proteomes:UP000253729};
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 (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ852056; RDH31141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3F3PW21; -.
DR STRING; 1341132.A0A3F3PW21; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000253729; 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 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; 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.
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:UP000253729}.
SQ SEQUENCE 395 AA; 43155 MW; 1BA61D2216902407 CRC64;
MGTASTMNAL AEALGMALPG SAAIPAPYRE RAQCAYETGL RIVEMVHSDR KPSDIMTREA
FENVIAVNTA IGGSTNAPIH INAIAKHIGV DLSLDDWDRL GFHIPLLLNM QPAGELLGEE
YYRAGGLPAI MAELLDAGKL NADAVTCNGH TVAQNVRGKH TWNRRMIRAY DDPLLKDAGF
LHLTGTLFDS AIMKTCVISE PFRQKFLENP ADPNAFEGSV VVFDGPEDYH HRLEDPSTPI
DDKSILVMRG AGPLGYPGAA EVVNMHPPGR LLREGVKSLP CIGDGRQSGT SGSPSILNAS
PEAAAGGNLA ILRDGDRLRV DLNQRRVDIL VPADELKKRK QELEASGGYN MPESQTPWQE
LFRKETSQLS EGMVLREAVK YQRLAQRYPE PRHNH
//