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 P17444


[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 BETA_ECOLI
Primary accession number P17444
Secondary accession numbers P77861 Q2MCB2
Integrated into Swiss-Prot on August 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 76)
Name and origin of the protein
Protein name Choline dehydrogenase
Synonyms CHD
CDH
EC 1.1.99.1
Gene name
Name: betA
OrderedLocusNames: b0311, JW0303
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].
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; CAA37093.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77738; AAA23504.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U73857; AAB18037.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73414.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76094.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S15182; S10901.
RefSeq AP_000964.1; -.
NP_414845.1; -.
3D structure databases
HSSP P13006; 1CF3. [HSSP ENTRY / PDB]
ModBase P17444.
Protein-protein interaction databases
IntAct P17444; -.
Enzyme and pathway databases
BioCyc EcoCyc:CHD-MON; -.
MetaCyc:CHD-MON; -.
Organism-specific databases
EchoBASE EB0107; -.
EcoGene EG10109; betA.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_00750; -; 1.
PBIL [Tree]
InterPro IPR011533; Choline_dehydrogenase.
IPR012132; GMC_OxRdtase.
IPR000172; GMC_OxRdtase_N.
IPR007867; GMC_OxRtase_C.
Graphical view of domain structure.
Pfam PF05199; GMC_oxred_C; 1.
PF00732; GMC_oxred_N; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000137; Alcohol_oxidase; 1.
TIGRFAMs TIGR01810; betA; 1.
PROSITE PS00623; GMC_OXRED_1; 1.
PS00624; GMC_OXRED_2; 1.
BLOCKS P17444.
Genome annotation databases
GeneID 945716; -.
GenomeReviews U00096_GR; b0311.
AP009048_GR; JW0303.
KEGG ecj:JW0303; -.
eco:b0311; -.
Phylogenomic databases
HOGENOM P17444; -.
Genome annotation databases
CMR P17444; b0311.
Other
ProtoNet P17444.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cell membrane; Complete proteome; FAD; Flavoprotein; Membrane; Oxidoreductase; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   556  556     Choline dehydrogenase. PRO_0000205586
NP_BIND   4    33  30     FAD (Probable). 
ACT_SITE   473   473        By similarity. 
Sequence information
Length: 556 AA [This is the length of the unprocessed precursor] Molecular weight: 61878 Da [This is the MW of the unprocessed precursor] CRC64: E182480168C8E9FD [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQFDYIIIGA GSAGNVLATR LTEDPNTSVL LLEAGGPDYR FDFRTQMPAA LAFPLQGKRY 

        70         80         90        100        110        120 
NWAYETEPEP FMNNRRMECG RGKGLGGSSL INGMCYIRGN ALDLDNWAQE PGLENWSYLD 

       130        140        150        160        170        180 
CLPYYRKAET RDMGENDYHG GDGPVSVTTS KPGVNPLFEA MIEAGVQAGY PRTDDLNGYQ 

       190        200        210        220        230        240 
QEGFGPMDRT VTPQGRRAST ARGYLDQAKS RPNLTIRTHA MTDHIIFDGK RAVGVEWLEG 

       250        260        270        280        290        300 
DSTIPTRATA NKEVLLCAGA IASPQILQRS GVGNAELLAE FDIPLVHELP GVGENLQDHL 

       310        320        330        340        350        360 
EMYLQYECKE PVSLYPALQW WNQPKIGAEW LFGGTGVGAS NHFEAGGFIR SREEFAWPNI 

       370        380        390        400        410        420 
QYHFLPVAIN YNGSNAVKEH GFQCHVGSMR SPSRGHVRIK SRDPHQHPAI LFNYMSHEQD 

       430        440        450        460        470        480 
WQEFRDAIRI TREIMHQPAL DQYRGREISP GVECQTDEQL DEFVRNHAET AFHPCGTCKM 

       490        500        510        520        530        540 
GYDEMSVVDG EGRVHGLEGL RVVDASIMPQ IITGNLNATT IMIGEKIADM IRGQEALPRS 

       550 
TAGYFVANGM PVRAKK 

P17444 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!