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Database: UniProt
Entry: A3VHT5_9RHOB
LinkDB: A3VHT5_9RHOB
Original site: A3VHT5_9RHOB 
ID   A3VHT5_9RHOB            Unreviewed;       547 AA.
AC   A3VHT5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   05-JUN-2019, entry version 72.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=RB2654_08722 {ECO:0000313|EMBL:EAQ12276.1};
OS   Maritimibacter alkaliphilus HTCC2654.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Maritimibacter.
OX   NCBI_TaxID=314271 {ECO:0000313|EMBL:EAQ12276.1, ECO:0000313|Proteomes:UP000002931};
RN   [1] {ECO:0000313|EMBL:EAQ12276.1, ECO:0000313|Proteomes:UP000002931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2654 {ECO:0000313|EMBL:EAQ12276.1,
RC   ECO:0000313|Proteomes:UP000002931};
RX   PubMed=20729358; DOI=10.1128/JB.00873-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of Pelagibaca bermudensis HTCC2601T and
RT   Maritimibacter alkaliphilus HTCC2654T, the type strains of two marine
RT   Roseobacter genera.";
RL   J. Bacteriol. 192:5552-5553(2010).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the oxidation of choline to betaine
CC       aldehyde and betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000256|SAAS:SAAS00321133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde;
CC         Xref=Rhea:RHEA:17433, ChEBI:CHEBI:13193, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969,
CC         ECO:0000256|SAAS:SAAS01117340};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8;
CC         Evidence={ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2,
CC         ECO:0000256|SAAS:SAAS01080756};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase route): step 1/1. {ECO:0000256|RuleBase:RU003969,
CC       ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080758}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EAQ12276.1}.
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DR   EMBL; AAMT01000009; EAQ12276.1; -; Genomic_DNA.
DR   RefSeq; WP_008330599.1; NZ_CH902578.1.
DR   STRING; 314271.RB2654_08722; -.
DR   EnsemblBacteria; EAQ12276; EAQ12276; RB2654_08722.
DR   eggNOG; ENOG4105CZ6; Bacteria.
DR   eggNOG; COG2303; LUCA.
DR   OrthoDB; 543793at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000002931; Unassembled WGS sequence.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR01810; betA; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000002931};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080744}; NAD {ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01080751,
KW   ECO:0000313|EMBL:EAQ12276.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002931}.
FT   DOMAIN       79    102       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      250    264       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND      89     92       FAD. {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   REGION      525    547       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A3VHT5}.
FT   BINDING      81     81       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
SQ   SEQUENCE   547 AA;  60399 MW;  F76359ECFD478F41 CRC64;
     MQADYVIVGA GSAGCAMAYR LGEAGHSVIV IEHGGTDAGP FIQMPGALSY PMNMPRYDWG
     FSSEPEPQLN NRRMAVPRGK VVGGSSSVNG MVYVRGHAKD YDHWADSGAT GWGYADVLPY
     FQRMEHWHGK GESDWRGTQG PLHVQQARQW NPLFHAFVAA GREAGYPVTE DYNGHQQEGF
     GAFDMTVWQG RRWSAANAYL KPAMAKWDVT LVNGLAKRVV FEGGRAVGVE IGRRTDETIR
     ATREVILAAS SINTPKLLML SGIGPGAHLR DHGIEVRANR PGVGQNLQDH LEVYMQYASK
     KPITLYRYWN LLGKAWVGAQ WLFTRTGHGA SNQFESCAFI RSQAGVEYPD IQFHFLPIAV
     RYDGKAAAEG HGFQAHVGPM RSKSRGAVTL ASADPADPPR ITFNYMSHDE DWQDWRRAVR
     LTREIFRQPA MEEFVKHEIQ PGGGDTDGEI DAFVREHAES AYHPCGTARM GAADDPNAVV
     DPECRVIGVE GLRVADSSIF PRITNGNTNA PSILVGEKAA DHVLGRTPLP RDNRGPWINP
     DWRTAQR
//
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