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Protein

Ureidoglycolate lyase

Gene

allA

Organism
Shigella flexneri
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 anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate.UniRule annotation

Catalytic activityi

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

Cofactori

Ni2+UniRule annotation

Pathwayi: (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

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:SF0444, S0451
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160Ureidoglycolate lyasePRO_0000120559Add
BLAST

Proteomic databases

PaxDbiP63487.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi198214.SF0444.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Helixi10 – 134Combined sources
Turni14 – 163Combined sources
Beta strandi17 – 204Combined sources
Beta strandi28 – 303Combined sources
Turni31 – 344Combined sources
Beta strandi35 – 384Combined sources
Beta strandi46 – 483Combined sources
Beta strandi53 – 597Combined sources
Beta strandi70 – 734Combined sources
Beta strandi79 – 857Combined sources
Beta strandi90 – 945Combined sources
Beta strandi97 – 993Combined sources
Helixi102 – 1043Combined sources
Beta strandi106 – 1094Combined sources
Beta strandi115 – 1184Combined sources
Beta strandi129 – 1324Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi156 – 1583Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSRX-ray2.80A/B1-160[»]
ProteinModelPortaliP63487.
SMRiP63487. Positions 1-160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63487.

Family & Domainsi

Sequence similaritiesi

Belongs to the ureidoglycolate lyase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108Z2U. Bacteria.
COG3194. LUCA.
HOGENOMiHOG000256169.
KOiK01483.
OMAiEMMERHP.
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_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

P63487-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD
60 70 80 90 100
RTLISINRAQ PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP
110 120 130 140 150
DLSTLRAFIT NGEQGVNYHR NVWHHPLFAW QRVTDFLTID RGGSDNCDVE
160
SIPEQELCFA
Length:160
Mass (Da):18,223
Last modified:October 11, 2004 - v1
Checksum:iE39014610FE93FC6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42098.1.
AE014073 Genomic DNA. Translation: AAP15974.1.
RefSeqiNP_706391.1. NC_004337.2.
WP_000776388.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN42098; AAN42098; SF0444.
AAP15974; AAP15974; S0451.
GeneIDi1027733.
KEGGisfl:SF0444.
sft:NCTC1_00458.
sfx:S0451.
PATRICi18701931. VBIShiFle31049_0498.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN42098.1.
AE014073 Genomic DNA. Translation: AAP15974.1.
RefSeqiNP_706391.1. NC_004337.2.
WP_000776388.1. NZ_LM651928.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XSRX-ray2.80A/B1-160[»]
ProteinModelPortaliP63487.
SMRiP63487. Positions 1-160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF0444.

Proteomic databases

PaxDbiP63487.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN42098; AAN42098; SF0444.
AAP15974; AAP15974; S0451.
GeneIDi1027733.
KEGGisfl:SF0444.
sft:NCTC1_00458.
sfx:S0451.
PATRICi18701931. VBIShiFle31049_0498.

Phylogenomic databases

eggNOGiENOG4108Z2U. Bacteria.
COG3194. LUCA.
HOGENOMiHOG000256169.
KOiK01483.
OMAiEMMERHP.
OrthoDBiEOG6JX7JB.

Enzyme and pathway databases

UniPathwayiUPA00395.

Miscellaneous databases

EvolutionaryTraceiP63487.

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_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF017306. Ureidogly_hydro. 1 hit.
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.
  3. "X-ray structure of Northeast structural genomics consortium target Sfr7."
    Northeast structural genomics consortium (NESG)
    Submitted (JAN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiALLA_SHIFL
AccessioniPrimary (citable) accession number: P63487
Secondary accession number(s): Q8XCX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: July 6, 2016
This is version 87 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

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 one 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.