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Database: UniProt
Entry: B4D2Q4_9BACT
LinkDB: B4D2Q4_9BACT
Original site: B4D2Q4_9BACT 
ID   B4D2Q4_9BACT            Unreviewed;       590 AA.
AC   B4D2Q4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:EDY19494.1};
DE   Flags: Precursor;
GN   ORFNames=CfE428DRAFT_3179 {ECO:0000313|EMBL:EDY19494.1};
OS   Chthoniobacter flavus Ellin428.
OC   Bacteria; Verrucomicrobiota; Spartobacteria; Chthoniobacterales;
OC   Chthoniobacteraceae; Chthoniobacter.
OX   NCBI_TaxID=497964 {ECO:0000313|EMBL:EDY19494.1, ECO:0000313|Proteomes:UP000005824};
RN   [1] {ECO:0000313|EMBL:EDY19494.1, ECO:0000313|Proteomes:UP000005824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin428 {ECO:0000313|EMBL:EDY19494.1,
RC   ECO:0000313|Proteomes:UP000005824};
RX   PubMed=21460085; DOI=10.1128/JB.00295-11;
RA   Kant R., van Passel M.W., Palva A., Lucas S., Lapidus A.,
RA   Glavina Del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S.,
RA   Larimer F.W., Land M.L., Hauser L., Sangwan P., de Vos W.M., Janssen P.H.,
RA   Smidt H.;
RT   "Genome sequence of Chthoniobacter flavus Ellin428, an aerobic
RT   heterotrophic soil bacterium.";
RL   J. Bacteriol. 193:2902-2903(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDY19494.1}.
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DR   EMBL; ABVL01000008; EDY19494.1; -; Genomic_DNA.
DR   RefSeq; WP_006980504.1; NZ_ABVL01000008.1.
DR   AlphaFoldDB; B4D2Q4; -.
DR   STRING; 497964.CfE428DRAFT_3179; -.
DR   GeneID; 78184061; -.
DR   eggNOG; COG2303; Bacteria.
DR   InParanoid; B4D2Q4; -.
DR   Proteomes; UP000005824; Unassembled WGS sequence.
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:UP000005824}.
FT   DOMAIN          27..324
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          445..573
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   590 AA;  64115 MW;  E44ECB8E4084A8CF CRC64;
     MPFLDTSKTR SPRYDVVIIG SGAAGGMAAY VLAKAGVKVL MLEAGRKYDP ATETPMFETN
     ADAPLRGVDT PDKPNGFFDA TIGGWTVKGE PYVVENQKEK TWVEGAFQNR NKTDQGFMWW
     RARMLGGRTN HWGRVSLRLG PLDFKPKSFD GLGFDWPISY EDVAPYYDQV DQLIGVFGSK
     EGLENNPDSD FFQPPPKPRA YEHLIMRGGK KLGIPVVASR LAILTKPING RAACFYATSC
     GRGCAIRANF QSTTVLIPPA LETGNLDILT GAMAREVTLD AQGRATGVHF IDTATGKEEH
     VAARAVILGA SACESARLLM NSKSAKFPQG LGNSTGHLGR WLTDSTGSDL GGQIPALENM
     PLHNEDGTSN MHTYGPWVKH HEAKAGKLGF PRGYYLAWGG GRTMPGMGAA TSSLLGNVYG
     KKLKEEARRY YGSFVSISCR GEMIPNEQSY MELDPEKKDQ WGIPVARFHF KWSDYELKQV
     AYAQQNFADL IEAAGGKVTR PPEKDGSKAI TAGGSVKHEI GVTRMSAEPK DGVTNSFGQL
     WDCQNVVVAD GGVFVSGPYK NPTLTILALA WRACDRLIDG MKKGEIAAPV
//
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