ID W1SBI8_9BACI Unreviewed; 280 AA.
AC W1SBI8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Xanthine dehydrogenase, FAD binding subunit {ECO:0000313|EMBL:ETI66440.1};
GN ORFNames=BAVI_22598 {ECO:0000313|EMBL:ETI66440.1};
OS Neobacillus vireti LMG 21834.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1131730 {ECO:0000313|EMBL:ETI66440.1, ECO:0000313|Proteomes:UP000018877};
RN [1] {ECO:0000313|EMBL:ETI66440.1, ECO:0000313|Proteomes:UP000018877}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21834 {ECO:0000313|EMBL:ETI66440.1,
RC ECO:0000313|Proteomes:UP000018877};
RX PubMed=24708037; DOI=10.1111/1462-2920.12478;
RA Mania D., Heylen K., van Spanning R.J., Frostegard A.;
RT "The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a
RT potent source and sink for nitric and nitrous oxide under high nitrate
RT conditions.";
RL Environ. Microbiol. 16:3196-3210(2014).
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:ETI66440.1}.
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DR EMBL; ALAN01000139; ETI66440.1; -; Genomic_DNA.
DR RefSeq; WP_024030684.1; NZ_ALAN01000139.1.
DR AlphaFoldDB; W1SBI8; -.
DR STRING; 220686.AA980_04035; -.
DR PATRIC; fig|1131730.3.peg.4734; -.
DR eggNOG; COG1319; Bacteria.
DR OrthoDB; 9774454at2; -.
DR Proteomes; UP000018877; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR PANTHER; PTHR42659:SF2; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR Pfam; PF00941; FAD_binding_5; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Reference proteome {ECO:0000313|Proteomes:UP000018877}.
FT DOMAIN 1..176
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 280 AA; 31074 MW; F7620A0F6B7FAEFF CRC64;
MLPFDFDYYK PETLQEAVEL YQYLDQQGKQ PMVFSGGTEL ITLGRIDLAY TEAVIDIKWI
AECKVMQVSG DHLLLGSTLT LTQIEEANLF PLLTKTASEV ADHSARGKIT LGGNICARIF
YREAVLPFLL ADSQVVIAGP DGGKVAAIHD VFHEELKLKR GEFLVQTATE SRFIRAPFFS
VKRRQQWETG YPLITVAALK IDQELRVAIS GLCPFPFRSK EIEAAINKSG QSATVRVDGA
LAVLPKPILN DVEGSAEYRL FVLRNLLIDV LAALDGARFR
//
