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Database: UniProt
Entry: M9RAP7_9RHOB
LinkDB: M9RAP7_9RHOB
Original site: M9RAP7_9RHOB 
ID   M9RAP7_9RHOB            Unreviewed;       547 AA.
AC   M9RAP7;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   Name=betA {ECO:0000313|EMBL:AGI66840.1};
GN   ORFNames=OAN307_c11380 {ECO:0000313|EMBL:AGI66840.1};
OS   Octadecabacter antarcticus 307.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=391626 {ECO:0000313|EMBL:AGI66840.1, ECO:0000313|Proteomes:UP000005307};
RN   [1] {ECO:0000313|EMBL:AGI66840.1, ECO:0000313|Proteomes:UP000005307}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=307 {ECO:0000313|EMBL:AGI66840.1,
RC   ECO:0000313|Proteomes:UP000005307};
RX   PubMed=23671678;
RA   Vollmers J., Voget S., Dietrich S., Gollnow K., Smits M., Meyer K.,
RA   Brinkhoff T., Simon M., Daniel R.;
RT   "Poles Apart: Arctic and Antarctic Octadecabacter strains Share High Genome
RT   Plasticity and a New Type of Xanthorhodopsin.";
RL   PLoS ONE 8:E63422-E63422(2013).
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; CP003740; AGI66840.1; -; Genomic_DNA.
DR   RefSeq; WP_015498882.1; NC_020911.1.
DR   AlphaFoldDB; M9RAP7; -.
DR   STRING; 391626.OAN307_c11380; -.
DR   KEGG; oat:OAN307_c11380; -.
DR   eggNOG; COG2303; Bacteria.
DR   HOGENOM; CLU_002865_7_1_5; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000005307; 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.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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   ECO:0000313|EMBL:AGI66840.1}.
FT   DOMAIN          79..102
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          251..265
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         81
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   547 AA;  58874 MW;  8A9520A80A8C613B CRC64;
     MKAEYVIVGA GSAGCAMAYR LAEAGKSVIV IETGGSDVGP FINMPAALSY PMSMKRYDWG
     YQSEPEPHLG GRKLACPRGK VIGGSSSING MIYVRGHARD FDYWAENGAH GWAYADVLPY
     YKRMEDWHDG GRGGDADWRG QGGPLHVTRG PGDNPLTQAF IKAGGQAGYQ LTSDYNGEQQ
     EGFGPFDATI WQGKRWSAAS AYLRPAQATG NCEVVHGTAA RIVIVDGHAT GVELTDGRSV
     SADAEVIIAA SAINSPKLLM LSGIGPAKHL SEHGIAVVAD RAGVGQNLQD HLELYVQMAA
     KGRHSLYKYW SLLGKALVGA RWLFTKTGIG ASNQFEACGF IRSKAGLDYP DIQFHFLPLA
     VRYDGVGARE GYQAHVGPMR SKSRGAVTLN SADPNDDPSI FFNYMSHPDD WDEFRACIRL
     TREIFSQDAF TPFACEELIP GVDAQSDAAL DATIRAHVES AYHPCGTCKM GSADDPDAVV
     DPMGRVIGVT GLRVADSSIF PRITNGNLNA PSIMVGEKMA DHVLGKQPIA PSNDAPWIHP
     DWKTAQR
//
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