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Reviewed, UniProtKB/Swiss-Prot A8A0T7 (ASTB_ECOHS)

Last modified June 16, 2009. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    N-succinylarginine dihydrolase
    EC=3.5.3.23
Gene names
Name: astB
Ordered Locus Names: EcHS_A1828
OrganismEscherichia coli O9:H4 (strain HS) [Complete proteome] [HAMAP]
Taxonomic identifier331112 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

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

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.

Sequence similarities

Belongs to the succinylarginine dihydrolase family.

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Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular functionN-succinylarginine dihydrolase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447N-succinylarginine dihydrolase HAMAP MF_01172
PRO_1000065724

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

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Sequences

Sequence LengthMass (Da)Tools
A8A0T7-1 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: A1C0469442DF753F

FASTA44749,394
        10         20         30         40         50         60 
MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRQ AAKQGLLKMK TLADAGFPQA 

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

       130        140        150        160        170        180 
LDGKVHFTVA NLNNKFHRSL EALVTESLLK 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 ATQVSVSDTV 

       310        320        330        340        350        360 
STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV FDLRESMANG 

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

       430        440 
REALDVLSQL LNLGSVYPFQ REGGGNG

« Hide

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References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000802 Genomic DNA. Translation: ABV06141.1.
RefSeqYP_001458524.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5591865.
GenomeReviewsGene locus EcHS_A1828 in contig CP000802_GR.
KEGGecx:EcHS_A1828.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA8A0T7. HFAHHPA.

Family and domain databases

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

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Entry information

Entry nameASTB_ECOHS
AccessionPrimary (citable) accession number: A8A0T7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 10 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)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

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