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P66899 (DPAL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative diaminopropionate ammonia-lyase

Short name=Diaminopropionatase
EC=4.3.1.15
Alternative name(s):
Alpha,beta-diaminopropionate ammonia-lyase
Gene names
Name:ygeX
Ordered Locus Names:b2871, JW2839
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate, the most suitable substrates to form pyruvate and ammonia. The L- and D-isomers of serine are also degraded, though slowly; it is the only serine dehydratase which can eliminate an amino group at the beta-carbon position By similarity.

Catalytic activity

2,3-diaminopropionate + H2O = pyruvate + 2 NH3.

Cofactor

Pyridoxal phosphate.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Putative diaminopropionate ammonia-lyase
PRO_0000185590

Amino acid modifications

Modified residue771N6-(pyridoxal phosphate)lysine Potential

Secondary structure

................................................................ 398
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P66899 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: FAF1277E86D60232

FASTA39843,328
        10         20         30         40         50         60 
MSVFSLKIDI ADNKFFNGET SPLFSQSQAK LARQFHQKIA GYRPTPLCAL DDLANLFGVK 

        70         80         90        100        110        120 
KILVKDESKR FGLNAFKMLG GAYAIAQLLC EKYHLDIETL SFEHLKNAIG EKMTFATTTD 

       130        140        150        160        170        180 
GNHGRGVAWA AQQLGQNAVI YMPKGSAQER VDAILNLGAE CIVTDMNYDD TVRLTMQHAQ 

       190        200        210        220        230        240 
QHGWEVVQDT AWEGYTKIPT WIMQGYATLA DEAVEQMREM GVTPTHVLLQ AGVGAMAGGV 

       250        260        270        280        290        300 
LGYLVDVYSP QNLHSIIVEP DKADCIYRSG VKGDIVNVGG DMATIMAGLA CGEPNPLGWE 

       310        320        330        340        350        360 
ILRNCATQFI SCQDSVAALG MRVLGNPYGN DPRIISGESG AVGLGVLAAV HYHPQRQSLM 

       370        380        390 
EKLALNKDAV VLVISTEGDT DVKHYREVVW EGKHAVAP 

« Hide

References

[1]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28375 Genomic DNA. Translation: AAA83052.1.
U00096 Genomic DNA. Translation: AAC75909.1.
AP009048 Genomic DNA. Translation: BAE76937.1.
PIRG65070.
RefSeqNP_417347.1. NC_000913.2.
YP_491073.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4D9GX-ray2.45A/B1-398[»]
4D9IX-ray2.00A/B1-398[»]
4D9KX-ray2.19A/B/C/D1-398[»]
4D9MX-ray2.50A/B1-398[»]
4D9NX-ray2.50A/B1-398[»]
ProteinModelPortalP66899.
SMRP66899. Positions 2-397.
ModBaseSearch...

Protein-protein interaction databases

IntActP66899. 1 interaction.
STRING511145.b2871.

Proteomic databases

PaxDbP66899.
PRIDEP66899.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75909; AAC75909; b2871.
BAE76937; BAE76937; BAE76937.
GeneID12933328.
947012.
KEGGecj:Y75_p2804.
eco:b2871.
PATRIC32121152. VBIEscCol129921_2964.

Organism-specific databases

EchoBASEEB2866.
EcoGeneEG13054. ygeX.

Phylogenomic databases

eggNOGCOG1171.
HOGENOMHOG000220594.
KOK01751.
OMAVMAMLEC.
ProtClustDBPRK08206.

Enzyme and pathway databases

BioCycEcoCyc:G7490-MONOMER.
ECOL316407:JW2839-MONOMER.
MetaCyc:G7490-MONOMER.
SABIO-RKP66899.

Gene expression databases

GenevestigatorP66899.

Family and domain databases

InterProIPR010081. DiNH2opropionate_NH3_lyase.
IPR019871. DiNH2propionate_NH3-lyase_sub.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PANTHERPTHR10314:SF7. PTHR10314:SF7. 1 hit.
PfamPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMSSF53686. PyrdxlP-dep_enz_bsu. 1 hit.
TIGRFAMsTIGR03528. 2_3_DAP_am_ly. 1 hit.
TIGR01747. diampropi_NH3ly. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPAL_ECOLI
AccessionPrimary (citable) accession number: P66899
Secondary accession number(s): Q2M9W9, Q46804
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references