ID B1KK16_SHEWM Unreviewed; 527 AA.
AC B1KK16;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ACA87203.1};
GN OrderedLocusNames=Swoo_2930 {ECO:0000313|EMBL:ACA87203.1};
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500 {ECO:0000313|EMBL:ACA87203.1, ECO:0000313|Proteomes:UP000002168};
RN [1] {ECO:0000313|EMBL:ACA87203.1, ECO:0000313|Proteomes:UP000002168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32 {ECO:0000313|Proteomes:UP000002168};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; CP000961; ACA87203.1; -; Genomic_DNA.
DR RefSeq; WP_012325539.1; NC_010506.1.
DR AlphaFoldDB; B1KK16; -.
DR STRING; 392500.Swoo_2930; -.
DR KEGG; swd:Swoo_2930; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_008878_4_0_6; -.
DR Proteomes; UP000002168; 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:UP000002168}.
FT DOMAIN 73..307
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 395..513
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 527 AA; 57071 MW; BAF16A45EF98F815 CRC64;
MTNIAKFALD DDSLVVIIGS GAGGGTVANE LAQKGISSVV LEAGKRFTLE DLKNNEWEMF
MKLSWLDKRI SAGGWHHSKN HTNLPAWIVK GVGGSSIHWA GVSLRFKPHE FKMKSTNGNI
EGANVADWPV TYEEVAPYYV KAEHKMGVTG KATDTPDLPE SSHTKLHRIA AERTGMTFTN
APMAINSVPN DGRPACQQIG FCMQGCRIGA KWSTMYTELP KAEATGLCEI RPNCMVLKIE
HDESGKATGV LYVDKDGNKK LQKARIVCVA ANSIESPRLL LNSASQMFPD GLANSSGQVG
RNYMGHVTGG VYGVFPEPVN MHRGTSVPSL ITSEQANKPE RGFVAGYTLE VLSLGLGFLS
AFLKPGTSGW GREIAEALEN YQNMAGVWIC GEDLPVETNR ITLHPTEKDQ HGLPVPVITK
TDHNNDVVMR NHAYSQMAKL YKSVGATKVH NLPAYPSSHN MGTNRMSEHP SDGVVNKWGQ
AHDVPNLFIS DGSQFVTSAA VNPTLTIVAL AIRQADHIAG LMKSGQV
//
