ID A0A0X1T2G5_PSEAA Unreviewed; 553 AA.
AC A0A0X1T2G5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AMB86255.1};
GN ORFNames=AWM79_13465 {ECO:0000313|EMBL:AMB86255.1};
OS Pseudomonas agarici.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=46677 {ECO:0000313|EMBL:AMB86255.1, ECO:0000313|Proteomes:UP000063229};
RN [1] {ECO:0000313|EMBL:AMB86255.1, ECO:0000313|Proteomes:UP000063229}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 2472 {ECO:0000313|EMBL:AMB86255.1,
RC ECO:0000313|Proteomes:UP000063229};
RA McClelland M., Jain A., Saraogi P., Mendelson R., Westerman R.,
RA SanMiguel P., Csonka L.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014135; AMB86255.1; -; Genomic_DNA.
DR RefSeq; WP_017132204.1; NZ_JACAQG010000012.1.
DR AlphaFoldDB; A0A0X1T2G5; -.
DR STRING; 46677.AWM79_13465; -.
DR Proteomes; UP000063229; 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:UP000063229}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 257..271
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 87
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 553 AA; 60233 MW; 9C01D07D68F9C4B3 CRC64;
MSSAHLPYDY VIVGAGPAGC VLANRLSADP RNNVVLLEAG GQDSYPWIHI PVGYLFCIGN
PRTDWCFKTE PQAGLQGRSL SYPRGKVLGG SSSINGMIYM RGQSSDYDRW AEQGNPGWAW
KDVLPLFKHS ENHFGGADAC HGDRGEWRVE QQRYSWPILD AFRAAAAENG IASVSDFNAG
DNQGCGYFQV NQRSGVRWNS AKAFLRPVLK RPNLTILTGV QVNRVSLENG RATAVLARWQ
GEERWFPARR EIILCAGSVG SPAILQRSGI GPRPLLESLG IAVRHELPGV GGNLQDHLQL
RLIYKLSNAR TLNQVANSLW GKAGMGLRYL YDRSGPLAMA PSQLGAFVKS SPEQRSANLQ
YHVQPLSLER FGEPLHRFPA FTASVCNLRP LSRGRIDIRS ANPEDAPLID PNYLSDPEDL
RVAAQAIRLT RRIVDAPALR VFKPEEYLPG ASLQSEEQLY EAAAKIGTTI FHPVGTCRMG
NGAQAVVDAQ LRVHGVPGLR VADASIMPQI TSGNTCSPTV MIAEKAARMI LQTRQATDQG
GLGSTPESVL PSA
//
