ID D6XWE2_BACIE Unreviewed; 470 AA.
AC D6XWE2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=FAD linked oxidase domain protein {ECO:0000313|EMBL:ADH99896.1};
GN OrderedLocusNames=Bsel_2394 {ECO:0000313|EMBL:ADH99896.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99896.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99896.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP001791; ADH99896.1; -; Genomic_DNA.
DR RefSeq; WP_013173318.1; NC_014219.1.
DR AlphaFoldDB; D6XWE2; -.
DR STRING; 439292.Bsel_2394; -.
DR KEGG; bse:Bsel_2394; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR OrthoDB; 9767256at2; -.
DR Proteomes; UP000000271; Chromosome.
DR GO; GO:0009339; C:glycolate oxidase complex; IEA:InterPro.
DR GO; GO:0003973; F:(S)-2-hydroxy-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004490; GlcD.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00387; glcD; 1.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF2; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 37..216
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 470 AA; 51133 MW; A92BEF0250A87C6B CRC64;
MLKKKVRKQL ADIVGEENLL DSPQDLLVYS YDSTPDFQSM PDAVIKPRST EEVSQICKVC
NESGTPIVPR GNGTNLSAGT TPLRGGVVMI FTHMDKLLEI DEENLTATVQ PGLITLDLIN
AVEAVDLFYA PDPSSMKIST IAGNINEGSG GLRGLKYGVT RDYVMGLEFV LANGDIVRTG
GKLAKDVAGY DLTRLMVGSE GTLGVMTEAT LKLIPKPETK KTMLALYPDL ETAGDTVSTI
IANKIIPATL EFLDQPTIRV VEDFAQIGLP TDAGAILLIE QDGPKEVVER DMERMREICV
QTGALSAEIA KTPEEGEALT AARRSALSAL ARMKPTTILE DATVPRSKVA EMVRAIEEIA
KKHNVEICTF GHAGDGNLHP TCMTDARDRE EMKRVEEAFE DIFMRAIEMG GTITGEHGVG
AMKSPYLAWK VGETGVEIMK NIKMAFDPNN IMNPDKIFAK NEKFRVVVSK
//
