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Database: UniProt
Entry: A0A0M4M0F8_9GAMM
LinkDB: A0A0M4M0F8_9GAMM
Original site: A0A0M4M0F8_9GAMM 
ID   A0A0M4M0F8_9GAMM        Unreviewed;       543 AA.
AC   A0A0M4M0F8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:ALE02062.1};
GN   ORFNames=W908_05575 {ECO:0000313|EMBL:ALE02062.1};
OS   Candidatus Pseudothioglobus singularis PS1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Candidatus Pseudothioglobus.
OX   NCBI_TaxID=1125411 {ECO:0000313|EMBL:ALE02062.1, ECO:0000313|Proteomes:UP000068905};
RN   [1] {ECO:0000313|EMBL:ALE02062.1, ECO:0000313|Proteomes:UP000068905}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PS1 {ECO:0000313|EMBL:ALE02062.1,
RC   ECO:0000313|Proteomes:UP000068905};
RX   PubMed=26494659;
RA   Marshall K.T., Morris R.M.;
RT   "Genome Sequence of 'Candidatus Thioglobus singularis' Strain PS1, a
RT   Mixotroph from the SUP05 Clade of Marine Gammaproteobacteria.";
RL   Genome Announc. 3:e01155-e01115(2015).
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP006911; ALE02062.1; -; Genomic_DNA.
DR   RefSeq; WP_053820278.1; NZ_CP006911.1.
DR   AlphaFoldDB; A0A0M4M0F8; -.
DR   STRING; 1125411.W908_05575; -.
DR   KEGG; tsn:W908_05575; -.
DR   PATRIC; fig|1125411.7.peg.1099; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000068905; 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; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068905}.
FT   DOMAIN          81..104
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          254..268
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         83
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         91..94
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   543 AA;  59961 MW;  20F76FF979EC1F6A CRC64;
     MDSYDYVIVG AGSAGCVLAN KLGEDKGHRI LVLEAGPMDS NLMIHIPAGV YKAYRNPKTN
     WNYLTENEPE LFNRKVPMPR GKVVGGSSSI NSMVYMRGHP LDYDRWQSEC GLKEWSYDQC
     LPYFKEGESS DRGEDQWRGG SGNLGVSKGS FENPLFEAFE EAGRQSGQGY SEDLNGYNPE
     GIARLDATRK HGRRCSAAVA HLRPALARGN VTLLTKSQVL KINMTNNSVS GVTFKHRGET
     RSIKANKEVI LSGGAINSPH LLMLSGIGPE KHLKEHGIDV NVDLPGVGQN LQDHSCVILQ
     YACKKSFPIH KVNQPHRKLA TGIKWVFTKK GIGASNIWEA GGLIRSSSKV AYPDIQYHFG
     PVGFEYEDNK ISLLQAFAIH VDQLRPRSRG EVTLKSADPL EKPLMTFNYL QHPEDLAEML
     CGVKKARELI SQQAFDEYRG EELIPGPEVE SDDDLVKFIR DVAETDYHPS CSCVMGNSKM
     AVVDEQMKVH GVKNLRVVDA SVMPQIISGN LNAPTQMIAA RAADMILGKE QLSPIKASFA
     FND
//
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