(data stored in ACNUC10821 zone)

SWISSPROT: C8U201_ECO10

ID   C8U201_ECO10            Unreviewed;       562 AA.
AC   C8U201;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 72.
DE   RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=CDH {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=CHD {ECO:0000256|HAMAP-Rule:MF_00750};
DE            EC=1.1.99.1 {ECO:0000256|HAMAP-Rule:MF_00750};
DE   AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00750};
DE            Short=BADH {ECO:0000256|HAMAP-Rule:MF_00750};
DE            EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00750};
GN   Name=betA {ECO:0000256|HAMAP-Rule:MF_00750,
GN   ECO:0000313|EMBL:BAI29159.1};
GN   OrderedLocusNames=ECO103_0288 {ECO:0000313|EMBL:BAI29159.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29159.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29159.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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|HAMAP-Rule:MF_00750, 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|HAMAP-Rule:MF_00750,
CC         ECO:0000256|RuleBase:RU003969, 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|HAMAP-Rule:MF_00750,
CC         ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00750, 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|HAMAP-Rule:MF_00750,
CC       ECO:0000256|RuleBase:RU003969, ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|RuleBase:RU003968,
CC       ECO:0000256|SAAS:SAAS01080758}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI29159.1; -; Genomic_DNA.
DR   RefSeq; WP_001159103.1; NC_013353.1.
DR   EnsemblBacteria; BAI29159; BAI29159; ECO103_0288.
DR   KEGG; eoh:ECO103_0288; -.
DR   HOGENOM; HOG000139600; -.
DR   KO; K00108; -.
DR   OMA; LSWKIHM; -.
DR   BioCyc; ECOL585395:ECO103_RS01510-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 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   PANTHER; PTHR11552:SF157; PTHR11552:SF157; 1.
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; C8U201.
DR   SWISS-2DPAGE; C8U201.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   FAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080744};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00750, ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00750,
KW   ECO:0000256|SAAS:SAAS01080751}.
FT   DOMAIN       82    105       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   DOMAIN      259    273       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00624}.
FT   NP_BIND       4     33       FAD. {ECO:0000256|HAMAP-Rule:MF_00750}.
FT   ACT_SITE    473    473       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00750}.
SQ   SEQUENCE   562 AA;  62550 MW;  A05F23022E2A7E97 CRC64;
     MQFDYIIIGA GSAGNVLATR LTEDPNTSVL LLEAGGPDYR FDFRTQMPAA LAFPLQGKRY
     NWAYETEPEP FMNNRRMECG RGKGLGGSSL INGMCYIRGN ALDLDNWAQE PGLENWSYLD
     CLPYYRKAET RDVGENDYHG GDGPVSVTTS KPGVNPLFEA MIEAGVQAGY PRTDDLNGYQ
     QEGFGPMDRT VTPQGRRAST ARGYLDQAKS RPNLTIRTHA MTDHIIFDGK RAVGVEWLEG
     DSTIPTRATA NKEVLLCAGA IASPQILQRS GVGNAELLAE FDIPLVHELP GVGENLQDHL
     EMYLQYECKE PVSLYPALQW WNQPKIGAEW LFGGTGVGAS NHFEAGGFIR SREEFAWPNI
     QYHFLPVAIN YNGSNAVKEH GFQCHVGSMR SPSRGHVRIK SRDPHQHPAI LFNYMSHEQD
     WQEFRDAIRI TREIMHQPAL DQYRGREISP GTECQTDEQL DEFVRNHAET AFHPCGTCKM
     GYDEMSVVDG EGRVHGLEGL RVVDASIMPQ IITGNLNATT IMIGEKIADM IRGQEALPRS
     TAGYFVANGM PVRAKKMSRD VN
//

If you have problems or comments...

PBIL Back to PBIL home page