ID F7NDC2_9FIRM Unreviewed; 292 AA.
AC F7NDC2;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Xanthine dehydrogenase subunit XdhB {ECO:0000313|EMBL:EGO65954.1};
DE EC=1.17.1.4 {ECO:0000313|EMBL:EGO65954.1};
GN ORFNames=ALO_00145 {ECO:0000313|EMBL:EGO65954.1};
OS Acetonema longum DSM 6540.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Acetonema.
OX NCBI_TaxID=1009370 {ECO:0000313|EMBL:EGO65954.1, ECO:0000313|Proteomes:UP000003240};
RN [1] {ECO:0000313|EMBL:EGO65954.1, ECO:0000313|Proteomes:UP000003240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6540 {ECO:0000313|EMBL:EGO65954.1,
RC ECO:0000313|Proteomes:UP000003240};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
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:EGO65954.1}.
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; AFGF01000005; EGO65954.1; -; Genomic_DNA.
DR RefSeq; WP_004091593.1; NZ_AFGF01000005.1.
DR AlphaFoldDB; F7NDC2; -.
DR STRING; 1009370.ALO_00145; -.
DR eggNOG; COG1319; Bacteria.
DR OrthoDB; 9789842at2; -.
DR Proteomes; UP000003240; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0004854; F:xanthine dehydrogenase activity; IEA:UniProtKB-EC.
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:SF5; ALDEHYDE OXIDOREDUCTASE FAD-BINDING SUBUNIT PAOB-RELATED; 1.
DR PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR Pfam; PF03450; CO_deh_flav_C; 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 Oxidoreductase {ECO:0000313|EMBL:EGO65954.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003240}.
FT DOMAIN 1..176
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 292 AA; 31591 MW; 6C96E8A39ED7D46A CRC64;
MFDIANYEEA RDLEQAIELL TKDPRAKLVA GGTDILLHVR EGKLPEAHLV SIHEVAELKG
IHLEADSTIV IKPVTTFTQV SSHPLIREHL PFLGEAVNWV GGPQTRHAGT IGGNICNGAT
SADSAPTLFA LNARLQITGP AGIRTIAIQD FYTGPGKVAL TQGEILTAIR IAPEDYRGFS
GHYIKYAMRN AMDIATLSCS VLCKLGDANL VEDFRLALGV AAPTPIRCLK TETAVKGQTF
SKELAATAGK TAVTEVNPRT SWRASKEYRL QLVAELSKRA FREAVAKRRN PA
//