Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A5W0D6 (ASTB_PSEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:Pput_1438
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length449 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-Rule MF_01172

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule 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 catabolic process to glutamate

Inferred from electronic annotation. Source: UniProtKB-HAMAP

arginine catabolic process to succinate

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionN-succinylarginine dihydrolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 449449N-succinylarginine dihydrolase HAMAP-Rule MF_01172
PRO_1000065733

Regions

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

Sites

Active site1741 By similarity
Active site2501 By similarity
Active site3711Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2141Substrate By similarity
Binding site2521Substrate By similarity
Binding site3651Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5W0D6 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: FE58561DB0608119

FASTA44948,817
        10         20         30         40         50         60 
MKSYEVNFDG LVGPTHNYGG LSYGNVASQS NSQQASNPRE AARQGLAKMK ALADMGFKQG 

        70         80         90        100        110        120 
VLAPQERPDV AALRRLGFSG SDADVIQRAA REAMPLLVAS CSASSMWVAN AATVSPSADT 

       130        140        150        160        170        180 
ADGRVHFTAA NLNCKYHRSI EHPTTSRVLG AMFNNEKHFA HHAALPAVAQ FGDEGAANHT 

       190        200        210        220        230        240 
RFCRAYGEAG VEFFVYGRSA FDSRYPAPQK YPARQTLEAS QAVARLHGLS DDGVVYAQQN 

       250        260        270        280        290        300 
PAVIDQGVFH NDVISVGNGE VLFYHEEAFL ETDAVLGQLR AKLASKGGNF QAICVPRAAV 

       310        320        330        340        350        360 
AVEDAVRSYL FNSQLLSRDD GSMLLVVPEE CRNNERVWAY LGQLTSQGGP VKEVKVFDLK 

       370        380        390        400        410        420 
QSMQNGGGPA CLRLRVALKE AELAAVNQGV IMTAPLYDTL LQWVDRHYRD RLGEADLADP 

       430        440 
QLLVECRTAL DELTQILKLG SVYPFQRQP 

« Hide

References

[1]"Complete sequence of Pseudomonas putida F1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000712 Genomic DNA. Translation: ABQ77596.1.
RefSeqYP_001266780.1. NC_009512.1.

3D structure databases

ProteinModelPortalA5W0D6.
SMRA5W0D6. Positions 3-447.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING351746.Pput_1438.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ77596; ABQ77596; Pput_1438.
GeneID5194776.
KEGGppf:Pput_1438.
PATRIC19918939. VBIPsePut56420_1462.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3724.
HOGENOMHOG000226005.
KOK01484.
OMAIAPTNCQ.
OrthoDBEOG6B8XDW.
ProtClustDBPRK13281.

Enzyme and pathway databases

BioCycPPUT351746:GI26-1476-MONOMER.
UniPathwayUPA00185; UER00280.

Family and domain databases

Gene3D3.75.10.20. 1 hit.
HAMAPMF_01172. AstB.
InterProIPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]
PfamPF04996. AstB. 1 hit.
[Graphical view]
TIGRFAMsTIGR03241. arg_catab_astB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASTB_PSEP1
AccessionPrimary (citable) accession number: A5W0D6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways