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
//