ID C6XW96_PEDHD Unreviewed; 558 AA.
AC C6XW96;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Glucose-methanol-choline oxidoreductase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Phep_1967 {ECO:0000313|EMBL:ACU04175.1};
OS Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457
OS / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=485917 {ECO:0000313|EMBL:ACU04175.1, ECO:0000313|Proteomes:UP000000852};
RN [1] {ECO:0000313|EMBL:ACU04175.1, ECO:0000313|Proteomes:UP000000852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 /
RC NCIMB 9290 / NRRL B-14731 / HIM 762-3
RC {ECO:0000313|Proteomes:UP000000852};
RX PubMed=21304637; DOI=10.4056/sigs.22138;
RA Han C., Spring S., Lapidus A., Del Rio T.G., Tice H., Copeland A.,
RA Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.C., Saunders E., Chertkov O.,
RA Brettin T., Goker M., Rohde M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT "Complete genome sequence of Pedobacter heparinus type strain (HIM 762-
RT 3).";
RL Stand. Genomic Sci. 1:54-62(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; CP001681; ACU04175.1; -; Genomic_DNA.
DR RefSeq; WP_015807789.1; NZ_AQGK01000001.1.
DR AlphaFoldDB; C6XW96; -.
DR STRING; 485917.Phep_1967; -.
DR KEGG; phe:Phep_1967; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_10; -.
DR OrthoDB; 9787779at2; -.
DR Proteomes; UP000000852; 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:UP000000852}.
FT DOMAIN 96..331
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 423..545
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 558 AA; 62973 MW; 1B79CF244072E8FE CRC64;
MKNLNFYDAI VIGSGISGGW AAMELCKKGL KTLLLERGRD VKHIQDYPTA NLNPWDFELG
FNNTLKDQEN DPIQSMAYTP ADKHFYVSDK DQPYVQEKPF NWFRGYQVGG RSLLWGRQCY
RLSDLDFEAN LKEGVAIDWP IRYKDIASWY SYVESFIGVS GKHENLSQLP DGEFLPPFEL
NCIEEHLADS ILKTEENRLL TPARVANLTK GWDNRGPCQN RNLCTRGCPF GGYFSSNSST
IPSAMATGNL TLRPFSIVVE LIYDEQEQKA KGVKVIDSVS NEVHLFYANI IFINASTIPT
TALLLNSVSS RFPNGFGNDS GQVGHNLMDH HSSAGAFGMH DSFKNQYYKG RRPCGFLIPR
YRNLNNNENL GFSRGYNIQG RGQRQEWVDL SSSNGYGSQF KKEITTPGKW MVWMAGWGEC
LPYFENRVSL VPDKVDKWGQ KLIAIDFEFK DNERKMMDDI KDTATEMLIK AGFNNIDSFN
YNKPGGSTVH EMGTARMGND PKTSVLNRFN QMHSVKNVFI TDGSCMTSSG CQNPSLTYMA
LTARACDYAV KQLKLGNL
//
