(data stored in ACNUC7421 zone)

SWISSPROT: BETB_ECO27

ID   BETB_ECO27              Reviewed;         490 AA.
AC   B7UJG5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=E2348C_0274;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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:
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: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; FM180568; CAS07822.1; -; Genomic_DNA.
DR   RefSeq; WP_001339252.1; NC_011601.1.
DR   SMR; B7UJG5; -.
DR   EnsemblBacteria; CAS07822; CAS07822; E2348C_0274.
DR   KEGG; ecg:E2348C_0274; -.
DR   KO; K00130; -.
DR   OMA; DTSWQCL; -.
DR   BioCyc; ECOL574521:E2348C_RS01440-MONOMER; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000008205; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00804; BADH; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
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   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; B7UJG5.
DR   SWISS-2DPAGE; B7UJG5.
KW   Complete proteome; Metal-binding; NAD; NADP; Oxidation;
KW   Oxidoreductase; Potassium.
FT   CHAIN         1    490       NAD/NADP-dependent betaine aldehyde
FT                                dehydrogenase.
FT                                /FTId=PRO_1000148555.
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}.
SQ   SEQUENCE   490 AA;  52928 MW;  D4B25AB4A46AA433 CRC64;
     MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW
     AAMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI
     PALEGCQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV
     TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTDHP GIAKVSFTGG VASGKKVMAN
     SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPTKCKA
     AFEQKVLARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGIEEGAR VLCGGDVLKG
     DSFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV
     TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ
     VEMAKFQSIF
//

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