ID Q24SI7_DESHY Unreviewed; 459 AA.
AC Q24SI7;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN OrderedLocusNames=DSY3216 {ECO:0000313|EMBL:BAE85005.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE85005.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE85005.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE85005.1,
RC ECO:0000313|Proteomes:UP000001946};
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE85005.1; -; Genomic_DNA.
DR RefSeq; WP_005816912.1; NC_007907.1.
DR AlphaFoldDB; Q24SI7; -.
DR STRING; 138119.DSY3216; -.
DR KEGG; dsy:DSY3216; -.
DR eggNOG; COG0277; Bacteria.
DR HOGENOM; CLU_017779_9_2_9; -.
DR Proteomes; UP000001946; Chromosome.
DR GO; GO:0003824; F:catalytic 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; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR42934; GLYCOLATE OXIDASE SUBUNIT GLCD; 1.
DR PANTHER; PTHR42934:SF1; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001946}.
FT DOMAIN 36..215
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 459 AA; 50130 MW; 0C4C4871D84A1B0E CRC64;
MLSQTIVDRL KEIVGEKNVV TKPTELFAYG YDGTLLSGDA IGAVFPETTD QVVELVNYMN
EQDIKLVPRG AGTNVSGGTI PSEKSIVINF TRMTKVLEID TENFVAVVEP GVVNFDLQQE
LEKVGFYYPP DPSSWKASTL GGNIGECSGG PRCFKYGVTR DSILGLEVVL PNGKVIRTGG
RNFKSEPGYD LTRIIVGSEG TLGLVTKAYL RILPKPVTKK TMLAIYNKVE DASQTVADIV
AAGIIPTTLE MMDNLLINTT EDYCHAGLPR DAGAILIIEI DGYPEDMDEQ IETIREVTKK
ANARDFKIAQ TAAEVDQIWL SRRVAFGSVA RVKPCYSIQD ITVPRSEFPQ AIEGILKIAK
EYDMIIGLVA HAGDGNLHPL VLFDQRHADE VERVHGAEGA LSKLAVSLGG TMSGEHGIGV
VKKKYMDVEF TPGAMEAFRK LKKTFDPANR FNPDKIISI
//
