(data stored in ACNUC7421 zone)

SWISSPROT: BETB_ECO57

ID   BETB_ECO57              Reviewed;         490 AA.
AC   Q7AH91; Q8XEC9;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   05-JUL-2017, entry version 90.
DE   RecName: Full=NAD/NADP-dependent betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE            Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN   Name=betB {ECO:0000255|HAMAP-Rule:MF_00804};
GN   OrderedLocusNames=Z0399, ECs0358;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the reversible oxidation of betaine
CC       aldehyde to the corresponding acid. {ECO:0000255|HAMAP-
CC       Rule:MF_00804}.
CC   -!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine +
CC       NADH. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC       Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00804};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine from betaine aldehyde: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
DR   EMBL; AE005174; AAG54654.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33781.1; -; Genomic_DNA.
DR   PIR; B85524; B85524.
DR   PIR; F90673; F90673.
DR   RefSeq; NP_308385.1; NC_002695.1.
DR   RefSeq; WP_000089099.1; NZ_MWVM01000022.1.
DR   ProteinModelPortal; Q7AH91; -.
DR   SMR; Q7AH91; -.
DR   STRING; 155864.Z0399; -.
DR   EnsemblBacteria; AAG54654; AAG54654; Z0399.
DR   EnsemblBacteria; BAB33781; BAB33781; BAB33781.
DR   GeneID; 914459; -.
DR   KEGG; ece:Z0399; -.
DR   KEGG; ecs:ECs0358; -.
DR   PATRIC; fig|386585.9.peg.450; -.
DR   eggNOG; ENOG4105C26; Bacteria.
DR   eggNOG; COG1012; LUCA.
DR   HOGENOM; HOG000271505; -.
DR   KO; K00130; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00804; BADH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR011264; BADH.
DR   PANTHER; PTHR11699:SF246; PTHR11699:SF246; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01804; BADH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q7AH91.
DR   SWISS-2DPAGE; Q7AH91.
KW   Complete proteome; Metal-binding; NAD; NADP; Oxidation;
KW   Oxidoreductase; Potassium.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    490       NAD/NADP-dependent betaine aldehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_0000056542.
FT   NP_BIND     150    153       NAD/NADP. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   NP_BIND     176    179       NAD/NADP. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   NP_BIND     229    234       NAD/NADP. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   ACT_SITE    162    162       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   ACT_SITE    252    252       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   ACT_SITE    464    464       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   METAL        26     26       Potassium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   METAL        27     27       Potassium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   METAL        93     93       Potassium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   METAL       180    180       Potassium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   METAL       246    246       Potassium 2; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   METAL       457    457       Potassium 2; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   METAL       460    460       Potassium 2; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   BINDING     209    209       NAD/NADP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   BINDING     286    286       NAD/NADP. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   BINDING     387    387       NAD/NADP. {ECO:0000255|HAMAP-
FT                                Rule:MF_00804}.
FT   SITE        248    248       Seems to be a necessary countercharge to
FT                                the potassium cations.
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   MOD_RES     286    286       Cysteine sulfenic acid (-SOH).
FT                                {ECO:0000255|HAMAP-Rule:MF_00804}.
FT   CONFLICT    361    361       D -> Y (in Ref. 2; BAB33781).
FT                                {ECO:0000305}.
SQ   SEQUENCE   490 AA;  52877 MW;  4FDEF67FCD8882E8 CRC64;
     MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW
     AAMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI
     PSLEGSQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV
     TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN
     SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCNA
     AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGDVLKG
     DGLDNGAWVA PTVFTDCSDE MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV
     TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ
     VEMAKFQSIF
//

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