ID A0A167V1R7_9HOMO Unreviewed; 393 AA. AC A0A167V1R7; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 18-JAN-2017, entry version 4. DE SubName: Full=FMN-dependent alpha-hydroxy acid dehydrogenase {ECO:0000313|EMBL:KZP04547.1}; GN ORFNames=FIBSPDRAFT_1054609 {ECO:0000313|EMBL:KZP04547.1}; OS Fibulorhizoctonia sp. CBS 109695. OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Atheliales; Atheliaceae; OC mitosporic Atheliaceae; Fibulorhizoctonia. OX NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP04547.1, ECO:0000313|Proteomes:UP000076532}; RN [1] {ECO:0000313|EMBL:KZP04547.1, ECO:0000313|Proteomes:UP000076532} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP04547.1, RC ECO:0000313|Proteomes:UP000076532}; RX PubMed=26659563; DOI=10.1093/molbev/msv337; RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H., RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., RA Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., RA Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.; RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi RT Provides Insights into the Origins of Lignocellulose Decay RT Capabilities."; RL Mol. Biol. Evol. 33:959-970(2016). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|PROSITE- CC ProRule:PRU00683}; CC -!- SIMILARITY: Belongs to the FMN-dependent alpha-hydroxy acid CC dehydrogenase family. {ECO:0000256|PROSITE-ProRule:PRU00683}. CC -!- SIMILARITY: Contains 1 FMN hydroxy acid dehydrogenase domain. CC {ECO:0000256|PROSITE-ProRule:PRU00683}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00683}. 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; KV417912; KZP04547.1; -; Genomic_DNA. DR Proteomes; UP000076532; Unassembled WGS sequence. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012133; Alpha-hydoxy_acid_DH_FMN. DR InterPro; IPR000262; FMN-dep_DH. DR Pfam; PF01070; FMN_dh; 2. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000076532}; KW Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683}; KW FMN {ECO:0000256|PROSITE-ProRule:PRU00683}; KW Reference proteome {ECO:0000313|Proteomes:UP000076532}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 19 {ECO:0000256|SAM:SignalP}. FT CHAIN 20 393 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5007893261. FT DOMAIN 58 220 FMN_dh. {ECO:0000259|Pfam:PF01070}. FT DOMAIN 231 379 FMN_dh. {ECO:0000259|Pfam:PF01070}. FT NP_BIND 310 334 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT ACT_SITE 276 276 Proton acceptor. {ECO:0000256|PROSITE- FT ProRule:PRU00683}. FT BINDING 152 152 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 176 176 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 178 178 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 204 204 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 214 214 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 252 252 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 279 279 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. SQ SEQUENCE 393 AA; 42656 MW; 649C309907174C92 CRC64; MLRAHILLLA GLCATLSSAV TIDMEGLPDT GLDTSTWVTG VAPPLEDLYE LNDLQIAAKN TLKPSSYASY RTGALDEITY QANLEIWQYI KLNGFTFRDV SDLNLNTSIL GYNFSLPFFI APAANAGLAN STTAELSLVE AAGDAGMLYV PSISSTKSIE QIASASVSPD QVMFHQEYVW SNKTRLQDEL TRIEAAGFKA IFLTVDNTGI NGIRTRSIRF TGEETDPGHA STFDLKALAA VRNMTSLPIV PKGIKTWQDA KTCLDLGFEA IYVSNHGGRV LDGAPTSVEV LLDIRKNAPE VFEKMEVYAD GGVRRANHVI TLLALGARAV GLGRSAMFSN LYGKEGVARM IYLLQTELGT SMKLMGESDV SAINSSYINT KWVENRYFGF GSS //