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Protein

Ureidoglycolate lyase

Gene

allA

Organism
Pseudomonas putida (strain KT2440)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the utilization of allantoin as nitrogen source.UniRule annotation

Catalytic activityi

(S)-ureidoglycolate = glyoxylate + urea.UniRule annotation

Cofactori

Ni2+UniRule annotation

Pathway: (S)-allantoin degradation

This protein is involved in the pathway (S)-allantoin degradation, which is part of Nitrogen metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway (S)-allantoin degradation and in Nitrogen metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Purine metabolism

Enzyme and pathway databases

BioCyciPPUT160488:GIXO-4368-MONOMER.
UniPathwayiUPA00395.

Names & Taxonomyi

Protein namesi
Recommended name:
Ureidoglycolate lyaseUniRule annotation (EC:4.3.2.3UniRule annotation)
Alternative name(s):
UreidoglycolataseUniRule annotation
Gene namesi
Name:allAUniRule annotation
Ordered Locus Names:PP_4288
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000556 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Ureidoglycolate lyasePRO_0000120551Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi160488.PP_4288.

Structurei

Secondary structure

1
167
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi11 – 144Combined sources
Turni15 – 173Combined sources
Beta strandi18 – 214Combined sources
Beta strandi29 – 313Combined sources
Turni32 – 354Combined sources
Beta strandi36 – 4510Combined sources
Beta strandi47 – 493Combined sources
Beta strandi53 – 6210Combined sources
Beta strandi66 – 705Combined sources
Beta strandi72 – 754Combined sources
Beta strandi81 – 877Combined sources
Beta strandi91 – 966Combined sources
Beta strandi98 – 1014Combined sources
Helixi104 – 1063Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi117 – 1204Combined sources
Beta strandi130 – 14415Combined sources
Beta strandi151 – 1544Combined sources
Helixi157 – 1593Combined sources
Beta strandi161 – 1633Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDRX-ray1.60A/B1-167[»]
ProteinModelPortaliP59285.
SMRiP59285. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59285.

Family & Domainsi

Sequence similaritiesi

Belongs to the ureidoglycolate lyase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3194.
HOGENOMiHOG000256169.
KOiK01483.
OMAiNCDIFQF.
OrthoDBiEOG6JX7JB.

Family and domain databases

Gene3Di2.60.120.480. 1 hit.
HAMAPiMF_00616. Ureidogly_lyase.
InterProiIPR011051. RmlC_Cupin.
IPR007247. Ureidogly_lyase.
IPR023525. Ureidogly_lyase_bac.
IPR024060. Ureidoglycolate_lyase_dom.
[Graphical view]
PANTHERiPTHR21221. PTHR21221. 1 hit.
PfamiPF04115. Ureidogly_hydro. 1 hit.
[Graphical view]
PIRSFiPIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P59285-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTLMIEPLT KEAFAQFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP
60 70 80 90 100
EDKAIISIFR ADAQDMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD
110 120 130 140 150
APVSGLVRAF RSNGRQGVNY HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC
160
DEHYFTEEQM LILNPHQ
Length:167
Mass (Da):18,768
Last modified:February 12, 2003 - v1
Checksum:i670B9A0AF8A8B1D3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN69868.1.
RefSeqiNP_746404.1. NC_002947.3.
WP_003254333.1. NC_002947.3.

Genome annotation databases

EnsemblBacteriaiAAN69868; AAN69868; PP_4288.
GeneIDi1041802.
KEGGippu:PP_4288.
PATRICi19947234. VBIPsePut30601_4560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN69868.1.
RefSeqiNP_746404.1. NC_002947.3.
WP_003254333.1. NC_002947.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDRX-ray1.60A/B1-167[»]
ProteinModelPortaliP59285.
SMRiP59285. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160488.PP_4288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN69868; AAN69868; PP_4288.
GeneIDi1041802.
KEGGippu:PP_4288.
PATRICi19947234. VBIPsePut30601_4560.

Phylogenomic databases

eggNOGiCOG3194.
HOGENOMiHOG000256169.
KOiK01483.
OMAiNCDIFQF.
OrthoDBiEOG6JX7JB.

Enzyme and pathway databases

UniPathwayiUPA00395.
BioCyciPPUT160488:GIXO-4368-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP59285.

Family and domain databases

Gene3Di2.60.120.480. 1 hit.
HAMAPiMF_00616. Ureidogly_lyase.
InterProiIPR011051. RmlC_Cupin.
IPR007247. Ureidogly_lyase.
IPR023525. Ureidogly_lyase_bac.
IPR024060. Ureidoglycolate_lyase_dom.
[Graphical view]
PANTHERiPTHR21221. PTHR21221. 1 hit.
PfamiPF04115. Ureidogly_hydro. 1 hit.
[Graphical view]
PIRSFiPIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.

Entry informationi

Entry nameiALLA_PSEPK
AccessioniPrimary (citable) accession number: P59285
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 12, 2003
Last sequence update: February 12, 2003
Last modified: May 27, 2015
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.