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P59285 (ALLA_PSEPK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Ureidoglycolate lyase

EC=4.3.2.3
Alternative name(s):
Ureidoglycolatase
Gene names
Name:allA
Ordered Locus Names:PP_4288
OrganismPseudomonas putida (strain KT2440) [Complete proteome] [HAMAP]
Taxonomic identifier160488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source By similarity. HAMAP-Rule MF_00616

Catalytic activity

(S)-ureidoglycolate = glyoxylate + urea. HAMAP-Rule MF_00616

Cofactor

Nickel By similarity. HAMAP-Rule MF_00616

Pathway

Nitrogen metabolism; (S)-allantoin degradation. HAMAP-Rule MF_00616

Subunit structure

Homodimer. Ref.2

Sequence similarities

Belongs to the ureidoglycolate lyase family.

Ontologies

Keywords
   Biological processPurine metabolism
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processallantoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

purine nucleobase metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionureidoglycolate hydrolase activity

Inferred from electronic annotation. Source: InterPro

ureidoglycolate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 167167Ureidoglycolate lyase HAMAP-Rule MF_00616
PRO_0000120551

Secondary structure

....................................... 167
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59285 [UniParc].

Last modified February 12, 2003. Version 1.
Checksum: 670B9A0AF8A8B1D3

FASTA16718,768
        10         20         30         40         50         60 
MRTLMIEPLT KEAFAQFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP EDKAIISIFR 

        70         80         90        100        110        120 
ADAQDMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD APVSGLVRAF RSNGRQGVNY 

       130        140        150        160 
HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC DEHYFTEEQM LILNPHQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence and comparative analysis of the metabolically versatile Pseudomonas putida KT2440."
Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., Madupu R., Nelson W.C., White O. expand/collapse author list , Peterson J.D., Khouri H.M., Hance I., Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.
Environ. Microbiol. 4:799-808(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT2440.
[2]"Crystal structure of the putative ureidoglycolate hydrolase pp4288 from Pseudomonas putida, Northeast structural genomics target Ppr49."
Northeast structural genomics consortium (NESG)
Submitted (NOV-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE015451 Genomic DNA. Translation: AAN69868.1.
RefSeqNP_746404.1. NC_002947.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDRX-ray1.60A/B1-167[»]
ProteinModelPortalP59285.
SMRP59285. Positions 1-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING160488.PP_4288.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN69868; AAN69868; PP_4288.
GeneID1041802.
KEGGppu:PP_4288.
PATRIC19947234. VBIPsePut30601_4560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3194.
HOGENOMHOG000256169.
KOK01483.
OMANCDIFQF.
OrthoDBEOG6JX7JB.

Enzyme and pathway databases

BioCycPPUT160488:GIXO-4368-MONOMER.
UniPathwayUPA00395.

Family and domain databases

Gene3D2.60.120.480. 1 hit.
HAMAPMF_00616. Ureidogly_lyase.
InterProIPR011051. RmlC_Cupin.
IPR007247. Ureidogly_hydro.
IPR023525. Ureidogly_hydro_bac.
IPR024060. Ureidoglycolate_hydrolase_dom.
[Graphical view]
PANTHERPTHR21221. PTHR21221. 1 hit.
PfamPF04115. Ureidogly_hydro. 1 hit.
[Graphical view]
PIRSFPIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMSSF51182. SSF51182. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP59285.

Entry information

Entry nameALLA_PSEPK
AccessionPrimary (citable) accession number: P59285
Entry history
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: May 14, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways