ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P17445


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name BETB_ECOLI
Primary accession number P17445
Secondary accession number Q2MCB1
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 76)
Name and origin of the protein
Protein name Betaine aldehyde dehydrogenase
Synonyms BADH
EC 1.2.1.8
Gene name
Name: betB
OrderedLocusNames: b0312, JW0304
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-29.
STRAIN=K12;
PubMed=1956285 [NCBI, ExPASy, EBI, Israel, Japan]
Lamark T., Kaasen E., Eshoo M.W., Falkenberg P., McDougall J., Strom A.R.;
"DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli.";
Mol. Microbiol. 5:1049-1064(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0378-1119(91)90389-S; PubMed=1879697 [NCBI, ExPASy, EBI, Israel, Japan]
Boyd L.A., Adam L., Pelcher L.E., McHughen A., Hirji R., Selvaraj G.;
"Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant BADH.";
Gene 103:45-52(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X52905; CAA37092.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77739; AAA23506.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77739; AAA23505.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18038.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73415.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76095.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15181; S15181.
RefSeq AP_000965.1; -.
NP_414846.1; -.
3D structure databases
HSSP P56533; 1A4S. [HSSP ENTRY / PDB]
ModBase P17445.
Protein-protein interaction databases
DIP DIP:9208N; -.
IntAct P17445; -.
Enzyme and pathway databases
BioCyc EcoCyc:BADH-MON; -.
Organism-specific databases
EchoBASE EB0108; -.
EcoGene EG10110; betB.
Ontologies
GO
GO:0008802; Molecular function: betaine-aldehyde dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0019285; Biological process: glycine betaine biosynthetic process from choline (inferred from electronic annotation from HAMAP).
QuickGo view.
Family and domain databases
HAMAP MF_00804; -; 1.
PBIL [Tree]
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
IPR011264; Betaine_Ald_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR01804; BADH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.
BLOCKS P17445.
Genome annotation databases
GeneID 947376; -.
GenomeReviews U00096_GR; b0312.
AP009048_GR; JW0304.
KEGG ecj:JW0304; -.
eco:b0312; -.
Phylogenomic databases
HOGENOM P17445; -.
Genome annotation databases
CMR P17445; b0312.
Other
ProtoNet P17445.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   490  489     Betaine aldehyde dehydrogenase. PRO_0000056541
NP_BIND   229   234  6     NAD (By similarity). 
ACT_SITE   252   252        By similarity. 
ACT_SITE   286   286        By similarity. 
CONFLICT   232   232        A -> R (in Ref. 2; AAA23506/AAA23505). 
CONFLICT   312   312        R -> P (in Ref. 2; AAA23506/AAA23505). 
Sequence information
Length: 490 AA [This is the length of the unprocessed precursor] Molecular weight: 52911 Da [This is the MW of the unprocessed precursor] CRC64: 747F822DA1233808 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRMAEQQLY IHGGYTSATS GRTFETINPA NGNVLATVQA AGREDVDRAV KSAQQGQKIW 

        70         80         90        100        110        120 
ASMTAMERSR ILRRAVDILR ERNDELAKLE TLDTGKAYSE TSTVDIVTGA DVLEYYAGLI 

       130        140        150        160        170        180 
PALEGSQIPL RETSFVYTRR EPLGVVAGIG AWNYPIQIAL WKSAPALAAG NAMIFKPSEV 

       190        200        210        220        230        240 
TPLTALKLAE IYSEAGLPDG VFNVLPGVGA ETGQYLTEHP GIAKVSFTGG VASGKKVMAN 

       250        260        270        280        290        300 
SAASSLKEVT MELGGKSPLI VFDDADLDLA ADIAMMANFF SSGQVCTNGT RVFVPAKCKA 

       310        320        330        340        350        360 
AFEQKILARV ERIRAGDVFD PQTNFGPLVS FPHRDNVLRY IAKGKEEGAR VLCGGDVLKG 

       370        380        390        400        410        420 
DGFDNGAWVA PTVFTDCSDD MTIVREEIFG PVMSILTYES EDEVIRRAND TDYGLAAGIV 

       430        440        450        460        470        480 
TADLNRAHRV IHQLEAGICW INTWGESPAE MPVGGYKHSG IGRENGVMTL QSYTQVKSIQ 

       490 
VEMAKFQSIF 

P17445 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by kr flag YPRC Korea Mirror sites: Australia  Brazil  Canada  China  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!