(data stored in SCRATCH zone)

SWISSPROT: D6XVU1_BACIE

ID   D6XVU1_BACIE            Unreviewed;       561 AA.
AC   D6XVU1;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 74.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   OrderedLocusNames=Bsel_0165 {ECO:0000313|EMBL:ADH97714.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97714.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97714.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001791; ADH97714.1; -; Genomic_DNA.
DR   RefSeq; WP_013171143.1; NC_014219.1.
DR   STRING; 439292.Bsel_0165; -.
DR   EnsemblBacteria; ADH97714; ADH97714; Bsel_0165.
DR   KEGG; bse:Bsel_0165; -.
DR   eggNOG; ENOG4105CZ6; Bacteria.
DR   eggNOG; COG2303; LUCA.
DR   HOGENOM; HOG000139600; -.
DR   KO; K00108; -.
DR   OMA; LSWKIHM; -.
DR   OrthoDB; 543793at2; -.
DR   BioCyc; BSEL439292:G1GLR-190-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000271; Chromosome.
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;
DR   PRODOM; D6XVU1.
DR   SWISS-2DPAGE; D6XVU1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
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   Reference proteome {ECO:0000313|Proteomes:UP000000271}.
FT   DOMAIN       84    107       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      258    272       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   BINDING      86     86       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     224    224       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   561 AA;  62372 MW;  CBBE3FFD8ABCE85E CRC64;
     MSEKYDVVII GGGSAGCVMA NRLSEDENRS VLVLEAGRKD FSWDLLIQMP AALPFPAGKS
     LYDWKYESDP EPYMGQRRIS HARGKVLGGS SSINGMIYQR GNPLDYERWG KDPGMENWDF
     AHCLPYFKRL ESALGSDKDD PYRGHDGPLK LERGPAKNPL FQAFFDAAVE AGYNRTPDVN
     GFRQEGFGPF DKHLYKGRRM SASRAYLQPV MKRKNLTVKT RAFVSSIDFE GKRAKGVTYK
     RNGKVHQIEA GEVILAGGAI NTPQMLQLSG VGDAQHLRSL GIKPVVDLPG VGENLQDHLE
     AYIQYSCPKP VSEQPNLSLH RMPWIGLQWI FARKGAAATN HFEGGGFVRS NDIVDYPNLM
     FHFLPVAVRY DGTKADTKHG FQVHVGPMYS DARGSLKITS KDPRKHPSMV YNYLSTEQDR
     REWIEAVRIS RNIMAQDAIK PYNSGEIAPG PEVQTDDEIL EWVAKDAETA LHPSCTAKMG
     PASDPMAVVD PESMKVHGLE NVRVVDASAM PYVTNGNIHA PVLMLAEKAA DLIRGKKPLE
     PEHLDFYRHG VHPADAGVEK K
//

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