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P59285

- ALLA_PSEPK

UniProt

P59285 - ALLA_PSEPK

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Protein

Ureidoglycolate lyase

Gene
allA, PP_4288
Organism
Pseudomonas putida (strain KT2440)
Status
Reviewed - 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 By similarity.UniRule annotation

Catalytic activityi

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

Cofactori

Nickel By similarity.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. ureidoglycolate hydrolase activity Source: InterPro
  2. ureidoglycolate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. allantoin catabolic process Source: UniProtKB-UniPathway
  2. purine nucleobase metabolic process Source: UniProtKB-KW
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 lyase (EC:4.3.2.3)
Alternative name(s):
Ureidoglycolatase
Gene namesi
Name:allA
Ordered Locus Names:PP_4288
OrganismiPseudomonas putida (strain KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
ProteomesiUP000000556: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 167167Ureidoglycolate lyaseUniRule annotationPRO_0000120551Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 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 – 83
Helixi11 – 144
Turni15 – 173
Beta strandi18 – 214
Beta strandi29 – 313
Turni32 – 354
Beta strandi36 – 4510
Beta strandi47 – 493
Beta strandi53 – 6210
Beta strandi66 – 705
Beta strandi72 – 754
Beta strandi81 – 877
Beta strandi91 – 966
Beta strandi98 – 1014
Helixi104 – 1063
Beta strandi108 – 1125
Beta strandi117 – 1204
Beta strandi130 – 14415
Beta strandi151 – 1544
Helixi157 – 1593
Beta strandi161 – 1633

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2BDRX-ray1.60A/B1-167[»]
ProteinModelPortaliP59285.
SMRiP59285. Positions 1-166.

Miscellaneous databases

EvolutionaryTraceiP59285.

Family & Domainsi

Sequence similaritiesi

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_hydro.
IPR023525. Ureidogly_hydro_bac.
IPR024060. Ureidoglycolate_hydrolase_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

MRTLMIEPLT KEAFAQFGDV IETDGSDHFM INNGSTMRFH KLATVETAEP    50
EDKAIISIFR ADAQDMPLTV RMLERHPLGS QAFIPLLGNP FLIVVAPVGD 100
APVSGLVRAF RSNGRQGVNY HRGVWHHPVL TIEKRDDFLV VDRSGSGNNC 150
DEHYFTEEQM LILNPHQ 167
Length:167
Mass (Da):18,768
Last modified:February 12, 2003 - v1
Checksum:i670B9A0AF8A8B1D3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN69868.1.
RefSeqiNP_746404.1. 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:
EMBL
GenBank
DDBJ
Links Updated
AE015451 Genomic DNA. Translation: AAN69868.1 .
RefSeqi NP_746404.1. NC_002947.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2BDR X-ray 1.60 A/B 1-167 [» ]
ProteinModelPortali P59285.
SMRi P59285. Positions 1-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 160488.PP_4288.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN69868 ; AAN69868 ; PP_4288 .
GeneIDi 1041802.
KEGGi ppu:PP_4288.
PATRICi 19947234. VBIPsePut30601_4560.

Phylogenomic databases

eggNOGi COG3194.
HOGENOMi HOG000256169.
KOi K01483.
OMAi NCDIFQF.
OrthoDBi EOG6JX7JB.

Enzyme and pathway databases

UniPathwayi UPA00395 .
BioCyci PPUT160488:GIXO-4368-MONOMER.

Miscellaneous databases

EvolutionaryTracei P59285.

Family and domain databases

Gene3Di 2.60.120.480. 1 hit.
HAMAPi MF_00616. Ureidogly_lyase.
InterProi IPR011051. RmlC_Cupin.
IPR007247. Ureidogly_hydro.
IPR023525. Ureidogly_hydro_bac.
IPR024060. Ureidoglycolate_hydrolase_dom.
[Graphical view ]
PANTHERi PTHR21221. PTHR21221. 1 hit.
Pfami PF04115. Ureidogly_hydro. 1 hit.
[Graphical view ]
PIRSFi PIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMi SSF51182. SSF51182. 1 hit.
ProtoNeti Search...

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 14, 2014
This is version 78 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

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

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