ID   K9PNR5_9CYAN            Unreviewed;       494 AA.
AC   K9PNR5;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:AFY34601.1};
DE            EC=1.1.99.1 {ECO:0000313|EMBL:AFY34601.1};
DE   Flags: Precursor;
GN   ORFNames=Cal7507_4222 {ECO:0000313|EMBL:AFY34601.1};
OS   Calothrix sp. PCC 7507.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC   Calothrix.
OX   NCBI_TaxID=99598 {ECO:0000313|EMBL:AFY34601.1, ECO:0000313|Proteomes:UP000010390};
RN   [1] {ECO:0000313|EMBL:AFY34601.1, ECO:0000313|Proteomes:UP000010390}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7507 {ECO:0000313|EMBL:AFY34601.1,
RC   ECO:0000313|Proteomes:UP000010390};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Teshima H., Chen A.,
RA   Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L., Pitluck S.,
RA   Woyke T., Kerfeld C.;
RT   "Finished genome of Calothrix sp. PCC 7507.";
RL   Submitted (APR-2012) 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}.
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DR   EMBL; CP003943; AFY34601.1; -; Genomic_DNA.
DR   RefSeq; WP_015130403.1; NC_019682.1.
DR   AlphaFoldDB; K9PNR5; -.
DR   STRING; 99598.Cal7507_4222; -.
DR   KEGG; calo:Cal7507_4222; -.
DR   PATRIC; fig|99598.3.peg.4761; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_2_3; -.
DR   OrthoDB; 9785276at2; -.
DR   Proteomes; UP000010390; Chromosome.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; 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; 2.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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   Oxidoreductase {ECO:0000313|EMBL:AFY34601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010390}.
FT   DOMAIN          245..259
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         88
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         96..99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         210
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   494 AA;  54147 MW;  3D4E2071C6D2147F CRC64;
     MTKITHYDYI VIGAGSAGSV VASKLAACDS DVSILLLEAG GTPDNEKMWT PSDWFEVLQK
     CPEIDWGYQS VPQANLNNRV IKLAQAKVLG GCALHNAMVY VRGSRSDFDA WGKVAPGWLW
     NDVLPHFQNV EQIMKVLTGE ADEFINDLFT AAAQYGLPHN PNYNTSESQY GYALFQFNVT
     GASNLIRETT YSTFQPERYQ NVTVHQMAFV NRILFEDTKA IGVEYVKDRQ QQLAYVQNEI
     ILSAGAIASP KILMLSGIGD ENELAKFDIS LVANVPEVGQ NLYDDLFVSV GFSLPQNKDV
     PFYDYGLAPA VIFGSTENSS SVIDIESSVG VGTLKGFPGP ERSFWLWPNI MHLKSRGTVT
     LRSSNPDDAP VIDPGYLTAP EDIQMCKTAL ELGIDIGNQL GLSQWRSKQI APQTGASLES
     YIRETADTTQ HYCGTCRMGT DEDSVVDTEL RVRGTSGLRV IDSSVFPLSI TANTAAATMM
     IADKGTDIII RSLQ
//