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UniProtKB/Swiss-Prot entry P0A8Y8


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

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Entry information
Entry name YBDB_ECOLI
Primary accession number P0A8Y8
Secondary accession numbers P15050 Q2MBK4
Integrated into Swiss-Prot on June 21, 2005
Sequence was last modified on June 21, 2005 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 30)
Name and origin of the protein
Protein name Esterase ybdB
Synonyms EC 3.1.-.-
p15
Gene name
Name: ybdB
OrderedLocusNames: b0597, JW0589
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].
PubMed=2521621 [NCBI, ExPASy, EBI, Israel, Japan]
Nahlik M.S., Brickman T.J., Ozenberger B.A., McIntosh M.A.;
"Nucleotide sequence and transcriptional organization of the Escherichia coli enterobactin biosynthesis cistrons entB and entA.";
J. Bacteriol. 171:784-790(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2521622 [NCBI, ExPASy, EBI, Israel, Japan]
Liu J., Duncan K., Walsh C.T.;
"Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.";
J. Bacteriol. 171:791-798(1989).
[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).
[6]
FUNCTION.
DOI=10.1016/j.femsre.2004.12.006; PubMed=15808744 [NCBI, ExPASy, EBI, Israel, Japan]
Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
"Enzyme genomics: application of general enzymatic screens to discover new enzymes.";
FEMS Microbiol. Rev. 29:263-279(2005).
[7]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 2-137.
Murshudov G.N., Vagin A.A., Dodson E.J.;
"Crystal structure of a putative thioesterase.";
Submitted (DEC-2003) to the PDB data bank.
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
M24148; AAA16104.1; -; Unassigned_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24143; AAA76837.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U82598; AAB40797.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73698.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76352.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B91904; Q3ECEA.
RefSeq AP_001244.1; -.
NP_415129.1; -.
3D structure databases
PDB
1VH9; X-ray; 2.15 A; A/B=2-137.[ExPASy / RCSB / EBI]
PDBsum 1VH9; -.
ModBase P0A8Y8.
Protein-protein interaction databases
IntAct P0A8Y8; 1.
Enzyme and pathway databases
BioCyc EcoCyc:EG11105-MON; -.
Organism-specific databases
EchoBASE EB1097; -.
EcoGene EG11105; ybdB.
Ontologies
GO
GO:0016787; Molecular function: hydrolase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR003736; PAAI.
IPR006683; Thioestr_supf.
Graphical view of domain structure.
Pfam PF03061; 4HBT; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00369; unchar_dom_1; 1.
Genome annotation databases
GeneID 945215; -.
GenomeReviews AP009048_GR; JW0589.
U00096_GR; b0597.
KEGG ecj:JW0589; -.
eco:b0597; -.
Phylogenomic databases
HOGENOM P0A8Y8; -.
Genome annotation databases
CMR P0A8Y8; b0597.
Other
ProtoNet P0A8Y8.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Hydrolase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   137  137     Esterase ybdB. PRO_0000156676
HELIX   9    14  6      
HELIX   20    23  4      
STRAND   27    31  5      
STRAND   36    41  6      
TURN   44    46  3      
STRAND   51    53  3      
HELIX   55    71  17      
STRAND   80    89  10      
STRAND   95   107  13      
STRAND   109   119  11      
STRAND   125   135  11      
Sequence information
Length: 137 AA [This is the length of the unprocessed precursor] Molecular weight: 14970 Da [This is the MW of the unprocessed precursor] CRC64: C8DF8DE63815F206 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MIWKRHLTLD ELNATSDNTM VAHLGIVYTR LGDDVLEAEM PVDTRTHQPF GLLHGGASAA 

        70         80         90        100        110        120 
LAETLGSMAG FMMTRDGQCV VGTELNATHH RPVSEGKVRG VCQPLHLGRQ NQSWEIVVFD 

       130 
EQGRRCCTCR LGTAVLG 

P0A8Y8 in FASTA format

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