ID Q5FQV9_GLUOX Unreviewed; 335 AA.
AC Q5FQV9;
DT 01-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Putative oxidoreductase {ECO:0000313|EMBL:AAW61237.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:AAW61237.1};
GN OrderedLocusNames=GOX1494 {ECO:0000313|EMBL:AAW61237.1};
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633 {ECO:0000313|EMBL:AAW61237.1, ECO:0000313|Proteomes:UP000006375};
RN [1] {ECO:0000313|EMBL:AAW61237.1, ECO:0000313|Proteomes:UP000006375}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H {ECO:0000313|EMBL:AAW61237.1,
RC ECO:0000313|Proteomes:UP000006375};
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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DR EMBL; CP000009; AAW61237.1; -; Genomic_DNA.
DR RefSeq; WP_011253023.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FQV9; -.
DR STRING; 290633.GOX1494; -.
DR KEGG; gox:GOX1494; -.
DR eggNOG; COG1319; Bacteria.
DR HOGENOM; CLU_058050_1_0_5; -.
DR Proteomes; UP000006375; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.465.10; -; 2.
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:SF1; BLR6160 PROTEIN; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Oxidoreductase {ECO:0000313|EMBL:AAW61237.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006375}.
FT DOMAIN 1..219
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 335 AA; 36074 MW; 4A62BF209A1DE211 CRC64;
MRQFSYSRPD TLDTASHTPD HTRFLAGGTN LIDLMKSDVE RPEHVVDLNA LSMSQIEECP
DGGLRLGALA TNADTAAHPL VSERYPLLAS AILAGASPQI RNRATNGGNL NQRTRCHYFY
DPDMACNKRS PGTGCSAKGG RNRIMAILGT SDACIATFPS DMCVALAALN ATVNLTGPEG
ERSVPLRDYH RLPEDTPWQD NILRTGEIVT SIDLPSISFG PHHTYLKIRD RLSFAFAIVS
VAAGLQMENN TIQKACIAMG GVGTKPWCVP EAEALFEGKT PSPSLFRDAA ECLLQGAVTD
RDNAAKLKLA PRVIIRALSQ AAAGTPQSQT QKTIF
//
