ID G0R842_HYPJQ Unreviewed; 616 AA.
AC G0R842;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Dehydratase {ECO:0000313|EMBL:EGR52622.1};
GN ORFNames=TRIREDRAFT_53872 {ECO:0000313|EMBL:EGR52622.1};
OS Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN [1] {ECO:0000313|EMBL:EGR52622.1, ECO:0000313|Proteomes:UP000008984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=QM6a {ECO:0000313|EMBL:EGR52622.1,
RC ECO:0000313|Proteomes:UP000008984};
RX PubMed=18454138; DOI=10.1038/nbt1403;
RA Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT reesei (syn. Hypocrea jecorina).";
RL Nat. Biotechnol. 26:553-560(2008).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; GL985056; EGR52622.1; -; Genomic_DNA.
DR RefSeq; XP_006961501.1; XM_006961439.1.
DR AlphaFoldDB; G0R842; -.
DR STRING; 431241.G0R842; -.
DR EnsemblFungi; EGR52622; EGR52622; TRIREDRAFT_53872.
DR GeneID; 18485618; -.
DR KEGG; tre:TRIREDRAFT_53872; -.
DR VEuPathDB; FungiDB:TRIREDRAFT_53872; -.
DR eggNOG; KOG2448; Eukaryota.
DR HOGENOM; CLU_014271_3_0_1; -.
DR OrthoDB; 238at2759; -.
DR Proteomes; UP000008984; 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:UP000008984}.
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 65800 MW; DA0EE18B8C9BDCAA CRC64;
MDKRKDSRDG TTPGSKADYD LSRPIHPAVG MRQGLPNYGD PHFSLFLRKV FIKALGYSED
ALSRPIIGII NTYSGFNPCH GNVPQLIEAA KRGVQLNGGL AIEFPTISIH ESFSSPTSMF
LRNLMSMDTE EMIKAQPVDA CIVIGGCDKT VPAQLMGGIS ANKPILPLIT GPMMPGSFRG
GRIGACTDCR NNWAAFRANE IDIEDISALN EELAPTAGTC GVMGTASTIA CLTAALGLIP
LRGGATAPAV SSARLRIAEQ TGANAIAAAK HKRTPQSILT EASFHNAITV LQAIGGSTNG
IVHLLAIANR HPEVNGKITL QTIDEIGRRT PLVVDLKPSG DNYMTDLHNA GGIPALFNVL
RPLLKLDALT ITGKTLGEAL DEEGFRPFPL TSQIIRPLDN PLYPSSSLAV LYGNIAPHGA
VIKASASKYR HLLTHRGRAV VFAGPEDLAK RIDDPDLDVD ENSVLVLQGI GPIGFSSPGM
PEAGLIPIPR KLAARGVKDM LRLSDGRMSG TAGGSIVLHI SPEAALPESV FGVVREGDVI
CCDVERRMLE VELDEAEIGR RVAERKDRLE SRLEGLGPAE TRRRPARGYR GLYERSVMQA
QDGVDFDFLT ANGASQ
//
