ID A0A0E3ZH71_9BACT Unreviewed; 571 AA.
AC A0A0E3ZH71;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:AKD05379.1};
GN ORFNames=PKOR_22950 {ECO:0000313|EMBL:AKD05379.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD05379.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD05379.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD05379.1,
RC ECO:0000313|Proteomes:UP000033109};
RX PubMed=26057562; DOI=10.1038/srep10929;
RA Dai J., Dai W., Qiu C., Yang Z., Zhang Y., Zhou M., Zhang L., Fang C.,
RA Gao Q., Yang Q., Li X., Wang Z., Wang Z., Jia Z., Chen X.;
RT "Unraveling adaptation of Pontibacter korlensis to radiation and
RT infertility in desert through complete genome and comparative
RT transcriptomic analysis.";
RL Sci. Rep. 5:10929-10929(2015).
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; CP009621; AKD05379.1; -; Genomic_DNA.
DR RefSeq; WP_046313763.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3ZH71; -.
DR STRING; 400092.PKOR_22950; -.
DR KEGG; pko:PKOR_22950; -.
DR PATRIC; fig|400092.3.peg.5056; -.
DR HOGENOM; CLU_008878_4_0_10; -.
DR OrthoDB; 1154541at2; -.
DR Proteomes; UP000033109; 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:UP000033109}.
FT DOMAIN 105..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 435..558
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 571 AA; 64061 MW; ADA9CEE800A504DC CRC64;
MANSNSSKFS DRTFDTIVIG SGISGGWAAK ELCEKGLRTL VLERGRNVEH VKDYPTAIKN
PWDFPHRGRL PLEVKEENPI ASKCYAFRED ATHFFVKDSE HPYVQEKPFD WIRGYQVGGK
SLMWARQTQR WSRYDFEGPA RDGFAVDWPI RYEDLAPWYS YVERFVGISG NKDGVDTLPD
GEFLPPWEMN VVEKAIRNRI VEAYQDRYVV IGRCAHLTKP EEIHHQQGRG QCQARTLCQR
GCPYGAYFSS NSSTLPWAAK TGKLTLRPDS VVHSILYDEK KGRAVGVRVI DAHTMEVQEY
FAKIIFVNAA TLNTNLILLN STSGRFPAGL GNDNGLLGKY VAFHNYRGTL SASMEGYEDS
YYFGRRPCAV MMPNFRNVHR QETDFLRGYM VFYSASRARA GAPANGEQLG AAYKDALLEP
GNWGIYMMMQ GETIPKESNH VSLSGSEKDA WGVPLLKVSV GYDENDEKSL KDFLEQGAEM
LDKAGCKSIH ANDSRQAPGL DIHEMGGVRM GRDPKTSLLN KYNQLHACKN VFVTDGACMT
STGTQNPSLT FMALTARAVN YAVSEMRKGS L
//
