ID X8E8V0_MYCXE Unreviewed; 223 AA. AC X8E8V0; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 12-AUG-2020, entry version 16. DE SubName: Full=Lactate 2-monooxygenase {ECO:0000313|EMBL:EUA76398.1}; DE EC=1.13.12.4 {ECO:0000313|EMBL:EUA76398.1}; GN ORFNames=I553_7379 {ECO:0000313|EMBL:EUA76398.1}; OS Mycobacterium xenopi 4042. OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=1299334 {ECO:0000313|EMBL:EUA76398.1}; RN [1] {ECO:0000313|EMBL:EUA76398.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=4042 {ECO:0000313|EMBL:EUA76398.1}; RA Brown-Elliot B., Wallace R., Lenaerts A., Ordway D., DeGroote M.A., RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N., RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.; RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={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: Lacks conserved residue(s) required for the propagation of CC feature annotation. {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:EUA76398.1}. 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; JAOB01000006; EUA76398.1; -; Genomic_DNA. DR EnsemblBacteria; EUA76398; EUA76398; I553_7379. DR PATRIC; fig|1299334.3.peg.408; -. DR GO; GO:0050040; F:lactate 2-monooxygenase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. 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 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|PROSITE-ProRule:PRU00683}; KW Monooxygenase {ECO:0000313|EMBL:EUA76398.1}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:EUA76398.1}. FT DOMAIN 1..223 FT /note="FMN hydroxy acid dehydrogenase" FT /evidence="ECO:0000259|PROSITE:PS51349" FT NP_BIND 150..174 FT /note="FMN" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT ACT_SITE 120 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 15 FT /note="FMN" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 24 FT /note="Substrate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 96 FT /note="FMN" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" FT BINDING 123 FT /note="Substrate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00683" SQ SEQUENCE 223 AA; 23742 MW; 214DE56141BB1438 CRC64; MHRAETAGYK GIVVTLDTWV PGWRPRDLGT ANFPQLRGHC LSNYTSDPVF RAGLQRPPEE DPQGVVLRWV QQFGHSLTWD DLPWLRSLTK LPLIVKGICH PDDARRAKDG GVDAIYCSNH GGRQANGGLP ALDCLPGVVE AADGLPVLFD SGVRSGADII KALALGATAV GIGRPYAYGL ALGGVDGIVH VLRALLAEAD LIMAVDGYPT LRDLTPAALR PVG //