ID A4CPJ4_ROBBH Unreviewed; 566 AA.
AC A4CPJ4;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Oxidoreductase, GMC family protein {ECO:0000313|EMBL:EAR14315.1};
GN OrderedLocusNames=RB2501_02785 {ECO:0000313|EMBL:EAR14315.1};
OS Robiginitalea biformata (strain ATCC BAA-864 / HTCC2501 / KCTC 12146).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Robiginitalea.
OX NCBI_TaxID=313596 {ECO:0000313|EMBL:EAR14315.1, ECO:0000313|Proteomes:UP000009049};
RN [1] {ECO:0000313|EMBL:EAR14315.1, ECO:0000313|Proteomes:UP000009049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-864 / HTCC2501 / KCTC 12146
RC {ECO:0000313|Proteomes:UP000009049};
RX PubMed=19767438; DOI=10.1128/JB.01191-09;
RA Oh H.M., Giovannoni S.J., Lee K., Ferriera S., Johnson J., Cho J.C.;
RT "Complete genome sequence of Robiginitalea biformata HTCC2501.";
RL J. Bacteriol. 191:7144-7145(2009).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP001712; EAR14315.1; -; Genomic_DNA.
DR RefSeq; WP_015755751.1; NC_013222.1.
DR AlphaFoldDB; A4CPJ4; -.
DR STRING; 313596.RB2501_02785; -.
DR KEGG; rbi:RB2501_02785; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_10; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000009049; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000009049}.
FT DOMAIN 105..340
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 430..553
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 566 AA; 63359 MW; 917DCBBFEFA62AC3 CRC64;
MANFNIDARQ AMTYDAIVIG SGISGGWAAK ELCEKGLKTL VLERGPIVEH VADYKTMNDD
PWDLELRESL TPEERRKHYK GIRSGFIGKS VEHFYANDAE NPYTEVKPFL WIRGHQMGGR
SLLWGKQTYR WSDLDFEANA RDGYGVDWPI RYKDIEPWYT YVEKFAGISG EPLGLPQLPD
SHFLPPMELN CVEKHVKSRI EEQFPGRHMI IGRVAHLTEP LNGRGKCQYR NRCSRGCPYG
AYFSSNAVTL PAAQATGNLT IRPYSIAQSI LYDEEKGLAN GVRIIDAETG ESMDYRARIV
FCNASALSTT QILLNSKSNR FPEGMGNDSG ELGHNLMDHT YRVGATARVP GFEDKYYSGR
RPNGIYIPRY VNVDEGSRSQ DFVRGFGFQG GGYRGGNPAN IPEFGAGFKD EILKPGPWEF
FITGFAECLP YHENKVTLDT ENTDKWGQPT LAIDCEFKEN EKALNRQIRK DAVEMLEKAG
LENVMGFDNE HEPGYGIHEM GTARMGRDPK TSVLNGTNQV HAVKNVFVTD GACMTSSSCV
NPSLTYMALT ARAADHAVSE LNKFNI
//
