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Reviewed, UniProtKB/Swiss-Prot P63487 (ALLA_SHIFL)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ureidoglycolate hydrolase
    EC=3.5.3.19
Gene names
Name: allA
Ordered Locus Names: SF0444, S0451
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length160 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Involved in the anaerobic utilization of allantoin. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate By similarity.

Catalytic activity

(S)-ureidoglycolate + H2O = glyoxylate + 2 NH3 + CO2. HAMAP MF_00616

Pathway

Nitrogen metabolism; (S)-allantoin degradation; glyoxylate from (S)-ureidoglycolate: step 1/1. HAMAP MF_00616

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the ureidoglycolate hydrolase family.

Ontologies

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

Inferred from electronic annotation. Source: InterPro

purine base catabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular functionureidoglycolate hydrolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 160160Ureidoglycolate hydrolase HAMAP MF_00616
PRO_0000120559

Secondary structure

..................................... 160
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63487-1 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: E39014610FE93FC6

FASTA16018,223
        10         20         30         40         50         60 
MKLQVLPLSQ EAFSAYGDVI ETQQRDFFHI NNGLVERYHD LALVEILEQD RTLISINRAQ 

        70         80         90        100        110        120 
PANLPLTIHE LERHPLGTQA FIPMKGEVFV VVVALGDDKP DLSTLRAFIT NGEQGVNYHR 

       130        140        150        160 
NVWHHPLFAW QRVTDFLTID RGGSDNCDVE SIPEQELCFA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
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.

Cross-references

Sequence databases

AE005674 Genomic DNA. Translation: AAN42098.1.
AE014073 Genomic DNA. Translation: AAP15974.1.
RefSeqNP_706391.1.
NP_836168.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1XSRX-ray2.80A/B1-160[»]
ModBaseSearch...

Genome annotation databases

GeneID1027733.
1076890.
GenomeReviewsGene locus SF0444 in contig AE005674_GR.
Gene locus S0451 in contig AE014073_GR.
KEGGsfl:SF0444.
sfx:S0451.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP63487.
OMAYRAGTWH.

Enzyme and pathway databases

BioCycSFLE198214:AAN42098.1-MON.
BRENDA3.5.3.19. 189495.

Family and domain databases

HAMAPMF_00616.
[Tree]
InterProIPR007247. Ureidogly_hydro.
[Graphical view]
PANTHERPTHR21221. Ureidogly_hydro. 1 hit.
PfamPF04115. Ureidogly_hydro. 1 hit.
[Graphical view]
PIRSFPIRSF017306. Ureidogly_hydro. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALLA_SHIFL
AccessionPrimary (citable) accession number: P63487
Secondary accession number(s): Q8XCX8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents