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A1ABS6 (ASTB_ECOK1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
N-succinylarginine dihydrolase

EC=3.5.3.23
Gene names
Name:astB
Ordered Locus Names:Ecok1_16220
ORF Names:APECO1_814
OrganismEscherichia coli O1:K1 / APEC [Complete proteome] [HAMAP]
Taxonomic identifier405955 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO2 By similarity. HAMAP MF_01172

Catalytic activity

N(2)-succinyl-L-arginine + 2 H2O = N(2)-succinyl-L-ornithine + 2 NH3 + CO2. HAMAP MF_01172

Pathway

Amino-acid degradation; L-arginine degradation via AST pathway; L-glutamate and succinate from L-arginine: step 2/5. HAMAP MF_01172

Subunit structure

Homodimer By similarity. HAMAP MF_01172

Sequence similarities

Belongs to the succinylarginine dihydrolase family.

Ontologies

Keywords
   Biological processArginine metabolism
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionN-succinylarginine dihydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447N-succinylarginine dihydrolase HAMAP MF_01172
PRO_1000065725

Regions

Region19 – 2810Substrate binding By similarity
Region137 – 1382Substrate binding By similarity

Sites

Active site1741 By similarity
Active site2481 By similarity
Active site3651Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2121Substrate By similarity
Binding site2501Substrate By similarity
Binding site3591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A1ABS6 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: D0A508A29B8B66FD

FASTA44749,539
        10         20         30         40         50         60 
MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK KLADAGFPQA 

        70         80         90        100        110        120 
VIPPHERPFI PVLRQLGFRG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT 

       130        140        150        160        170        180 
LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS VHSALPQVAL LGDEGAANHN 

       190        200        210        220        230        240 
RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD 

       250        260        270        280        290        300 
VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVFVSDAV 

       310        320        330        340        350        360 
STYLFNSQLL SRDDGSMVLV LPQECREHAG VWRYLNELLA ADNPISELKV FDLRESMANG 

       370        380        390        400        410        420 
GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLREG 

       430        440 
REALDTLTQL LDLGSVYPFQ REGGGNG 

« Hide

References

[1]"The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7 shares strong similarities with human extraintestinal pathogenic E. coli genomes."
Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.
J. Bacteriol. 189:3228-3236(2007) [PubMed: 17293413] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000468 Genomic DNA. Translation: ABJ01116.1.
RefSeqYP_852830.1. NC_008563.1.

3D structure databases

ProteinModelPortalA1ABS6.
SMRA1ABS6. Positions 2-441.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1ABS6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000037619; EBESCP00000036136; EBESCG00000036669.
GeneID4495253.
GenomeReviewsGene locus Ecok1_16220 in contig CP000468_GR.
KEGGecv:APECO1_814.
PATRIC18215116. VBIEscCol127180_1834.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3724.
GeneTreeEBGT00050000010790.
HOGENOMHBG289862.
OMAHFAHHPA.
ProtClustDBPRK13281.

Enzyme and pathway databases

BioCycECOL405955:APECO1_814-MONOMER.

Family and domain databases

HAMAPMF_01172. AstB.
[Tree]
InterProIPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]
Gene3DG3DSA:3.75.10.20. SuccinylArg_di_hydro. 1 hit.
KOK01484.
PfamPF04996. AstB. 1 hit.
[Graphical view]
TIGRFAMsTIGR03241. Arg_catab_astB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASTB_ECOK1
AccessionPrimary (citable) accession number: A1ABS6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: December 14, 2011
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families