ID A0A0E3ZBY5_9BACT Unreviewed; 571 AA.
AC A0A0E3ZBY5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=GMC family oxidoreductase {ECO:0000313|EMBL:AKD02275.1};
GN ORFNames=PKOR_02915 {ECO:0000313|EMBL:AKD02275.1};
OS Pontibacter korlensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=400092 {ECO:0000313|EMBL:AKD02275.1, ECO:0000313|Proteomes:UP000033109};
RN [1] {ECO:0000313|EMBL:AKD02275.1, ECO:0000313|Proteomes:UP000033109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X14-1T {ECO:0000313|EMBL:AKD02275.1,
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP009621; AKD02275.1; -; Genomic_DNA.
DR RefSeq; WP_046309037.1; NZ_CP009621.1.
DR AlphaFoldDB; A0A0E3ZBY5; -.
DR STRING; 400092.PKOR_02915; -.
DR KEGG; pko:PKOR_02915; -.
DR PATRIC; fig|400092.3.peg.662; -.
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; PTHR46056; LONG-CHAIN-ALCOHOL OXIDASE; 1.
DR PANTHER; PTHR46056:SF4; LONG-CHAIN-ALCOHOL 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 109..323
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; 64186 MW; 622690F15557E255 CRC64;
MANLNIDSVK QRTYDAIVIG SGISGGWAAK ELTEKGLKTL VLERGRDVKH NRDYPTTNKM
PYEFEHRGEV PLEIRKKEPV VSRCYAFRED AMHFFVKDSE HPYVQEKPFD WIRGYQVGGK
SLLWARQTQR WSELDFEGPA RDGFAVDWPI RYKDLAPWYT YVERFAGISG NSDGLAELPD
GDFLPAFPLN SVEDYFKQQL QKQYGNRHVI SARCAHLSKP NQIHLDQGRA QCQNRTLCQR
GCPFGGYFSS NSSTLPWAER TGNLTLLPFS VVESVIYDEK AGKASGVRVI DANTKEVTEY
YANIIFVNAA ALNTNHILLN STSSRFPNGL GNDNGLLGKY VAFHNYRARI SAEYDGLMEY
ATDGRNPAGG GYIPRFRNLH KQETDFLRGY AAGFSAGRYN TEDRSGFGAD LKQQLLNPGL
TNWRVGSHMM GETIPKEESQ VSLSKDQKDA WGMPLLNISI GYDDNDEKMV KDYLEQMTEM
FTKAGFTNIR TTDSKQAPGL DIHEMGGVRM GHDPKTSLLN KYNQLHACKN VFVTDGACMT
STATQNPSLT YMALTARAVD YAVSEMKKGN L
//
