ID D2SDH1_GEOOG Unreviewed; 561 AA.
AC D2SDH1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN OrderedLocusNames=Gobs_1710 {ECO:0000313|EMBL:ADB74424.1};
OS Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC
OS A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=526225 {ECO:0000313|EMBL:ADB74424.1, ECO:0000313|Proteomes:UP000001382};
RN [1] {ECO:0000313|EMBL:ADB74424.1, ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RX PubMed=21304698;
RA Ivanova N., Sikorski J., Jando M., Munk C., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Meincke L.,
RA Brettin T., Detter J.C., Detter J.C., Rohde M., Goeker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.-P.;
RT "Complete genome sequence of Geodermatophilus obscurus type strain (G-
RT 20).";
RL Stand. Genomic Sci. 2:158-167(2010).
RN [2] {ECO:0000313|Proteomes:UP000001382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 /
RC NBRC 13315 / NRRL B-3577 / G-20 {ECO:0000313|Proteomes:UP000001382};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Munk A.C., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Jando M.,
RA Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Geodermatophilus obscurus DSM 43160.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710,
CC ChEBI:CHEBI:17499; EC=1.1.99.1;
CC Evidence={ECO:0000256|RuleBase:RU003969};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (cytochrome c reductase
CC route): step 1/1. {ECO:0000256|RuleBase:RU003969}.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; CP001867; ADB74424.1; -; Genomic_DNA.
DR RefSeq; WP_012947864.1; NC_013757.1.
DR AlphaFoldDB; D2SDH1; -.
DR STRING; 526225.Gobs_1710; -.
DR KEGG; gob:Gobs_1710; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_11; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000001382; Chromosome.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
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; IPR011533; BetA.
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 NCBIfam; TIGR01810; betA; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001382}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 260..274
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 225
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 561 AA; 61203 MW; 5E8069D1F0B86DE9 CRC64;
MSPQVYDVVI VGGGSAGSAL ANRLSADPGN RVLVLEAGRE DSLWDVFVHM PGALTIPIGN
RFYDWRYESE PEPRMGGRRV YHARGKLLGG SSSINGMIFQ RGNPLDYERW GADEGMGTWD
FAHCLPYFKR MENCTAAAPE DPFRGKDGPL VLERGPATSP LFQAFLTAVQ EAGHPLTDDL
NGYRQEGFGP FDRNVHRGRR LSAARAYLHP VRSRPNLTVE TRAFVTRVLF DGGRAVGVEY
RHGRRPARTV RAGEVVLSGG AVNTPQLLQL SGVGNGSELR ALGIDVVADL PGVGENLQDH
LEVYIQHGCT QPVSIAPGMK WWRKPGIGAQ WLFLRTGLGA TNHFEAGGFL RSNDDVAYPN
LMFHFLPIAV RYDGSMPTGE HGYQVHVGPM YSDARGTLKI RSADPRVKPA MRCNYLSTAQ
DRREWVEAVQ VARGIFEQPA LAEFSSGEIS PGPEIETPEQ ILSWVARDAE TALHPSCTAK
MGTGPLSVVD PTSMRVHGLE GLRVVDASAM PYVTNGNIYA PVMMMAEKAA DLILGNTPLA
PEHVEFYRHR PASVGEAAGQ A
//
