ID A0A124SQ59_BURCE Unreviewed; 413 AA. AC A0A124SQ59; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 20-DEC-2017, entry version 9. DE SubName: Full=2-hydroxy-acid oxidase {ECO:0000313|EMBL:KVK86178.1}; GN ORFNames=WS90_07840 {ECO:0000313|EMBL:KVK86178.1}; OS Burkholderia cepacia (Pseudomonas cepacia). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex. OX NCBI_TaxID=292 {ECO:0000313|EMBL:KVK86178.1, ECO:0000313|Proteomes:UP000069001}; RN [1] {ECO:0000313|EMBL:KVK86178.1, ECO:0000313|Proteomes:UP000069001} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MSMB1302 {ECO:0000313|EMBL:KVK86178.1, RC ECO:0000313|Proteomes:UP000069001}; RA Sahl J., Keim P., Wagner D.; RT "Expanding the genomic diversity of Burkholderia species for the RT development of highly accurate diagnostics."; RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KVK86178.1}. 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; LOYH01000027; KVK86178.1; -; Genomic_DNA. DR RefSeq; WP_059728422.1; NZ_LOYH01000027.1. DR EnsemblBacteria; KVK86178; KVK86178; WS90_07840. DR Proteomes; UP000069001; Unassembled WGS sequence. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR CDD; cd02809; alpha_hydroxyacid_oxid_FMN; 1. 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 InterPro; IPR037396; FMN_HAD. DR InterPro; IPR008259; FMN_hydac_DH_AS. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF000138; Al-hdrx_acd_dh; 1. DR PROSITE; PS00557; FMN_HYDROXY_ACID_DH_1; 1. DR PROSITE; PS51349; FMN_HYDROXY_ACID_DH_2; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000069001}; KW Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683}; KW FMN {ECO:0000256|PROSITE-ProRule:PRU00683}. FT DOMAIN 25 409 FMN hydroxy acid dehydrogenase. FT {ECO:0000259|PROSITE:PS51349}. FT NP_BIND 335 359 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT ACT_SITE 304 304 Proton acceptor. {ECO:0000256|PIRSR: FT PIRSR000138-1, ECO:0000256|PROSITE- FT ProRule:PRU00683}. FT BINDING 51 51 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 133 133 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 153 153 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 155 155 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 181 181 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 190 190 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 280 280 FMN. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. FT BINDING 307 307 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU00683}. SQ SEQUENCE 413 AA; 44819 MW; EE4E617D16A0AF32 CRC64; MTPSASSVPG TRRPLADTRT PHMPRVLRKM LCLHDFEAAA RRALPRPIFG YVSGAAEDNR TRDDNRAVFD EYGFATRVLR NVSQREQGIE LFGRRYASPF GIAPMGIHAL SAYRGDIVLA RAAQRAGIAS IMSGSSLIPL EEVAAAAPDT WFQAYLPGDA SRISALLERV ARAGYRTLVI TVDIPVSANR ENNVRTGFTT PLRPGPRLFW DGIVRPRWLA GTFARTLLAH GMPHFENSFA TRGAPILSST VQRDFSARDH LDWGHLERIR QEWKGELVIK GILSVDDAVI ARDAGADGII LSNHGGRQLD GAVSPMRILP DVVRALGADY PVMIDSGFRR GSDVLKAVAM GAHMVFVGRP FNYAAAVAGE AGVMHAIGLL RDEVDRNMAM LGVERCGGLT PDVLIRKGGV PAA //