ID A0A124SQ59_BURCE Unreviewed; 413 AA. AC A0A124SQ59; DT 13-APR-2016, integrated into UniProtKB/TrEMBL. DT 13-APR-2016, sequence version 1. DT 11-DEC-2019, entry version 14. 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; CC Evidence={ECO:0000256|PIRSR:PIRSR000138-2, CC ECO:0000256|PROSITE-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 EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 Flavoprotein {ECO:0000256|PROSITE-ProRule:PRU00683}; KW FMN {ECO:0000256|PIRSR:PIRSR000138-2, ECO:0000256|PROSITE- KW ProRule:PRU00683}. FT DOMAIN 25..409 FT /note="FMN hydroxy acid dehydrogenase" FT /evidence="ECO:0000259|PROSITE:PS51349" FT NP_BIND 335..359 FT /note="FMN" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT NP_BIND 335..339 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 304 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-1, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 51 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 133 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 153 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 155 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 181 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 190 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 280 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 302 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2" FT BINDING 307 FT /note="Substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2, FT ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 359 FT /note="FMN" FT /evidence="ECO:0000256|PIRSR:PIRSR000138-2" 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 //