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Reviewed, UniProtKB/Swiss-Prot A0K609 (ASTB_BURCH)

Last modified June 16, 2009. Version 16. 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: Bcen2424_1184
OrganismBurkholderia cenocepacia (strain HI2424) [Complete proteome] [HAMAP]
Taxonomic identifier331272 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

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Protein attributes

Sequence length446 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 – 446446N-succinylarginine dihydrolase HAMAP MF_01172
PRO_1000065714

Regions

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

Sites

Active site1741 By similarity
Active site2491 By similarity
Active site3701Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2131Substrate By similarity
Binding site2511Substrate By similarity
Binding site3641Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
A0K609-1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 15E1E87E4AB138B7

FASTA44648,327
        10         20         30         40         50         60 
MNAQEANFDG LVGPTHNYAG LSFGNVASLN NEKSAANPKA AAKQGLRKMK QLADLGFAQG 

        70         80         90        100        110        120 
VLPPQERPSL RLLRELGFSG KDADVIAKAA KQAPELLAAA SSASAMWTAN AATVSPSADT 

       130        140        150        160        170        180 
SDGRVHFTPA NLCSKLHRAI EHEATRRTLS TLFADPTHFA VHEALTGTPA LGDEGAANHT 

       190        200        210        220        230        240 
RFCAEYGKPG IEFFVYGRAE YRRGPEPKRF PARQTFEASR AVAHRHGLAE EATVYAQQDP 

       250        260        270        280        290        300 
DVIDAGVFHN DVISVGNRDT LFTHERAFVN KQAIYDTLTA ALDARGARLN VIEVPDAAVS 

       310        320        330        340        350        360 
VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENARVAAYL DQLAAGNGPI HDVLVFDLRE 

       370        380        390        400        410        420 
SMKNGGGPAC LRLRVVLNDA ERAAVTSNVW INDTLFASLD AWIDKHYRDR LAPEDLADPA 

       430        440 
LLDESRTALD ELTQILRVGS LYDFQR

« Hide

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References

[1]"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000458 Genomic DNA. Translation: ABK07936.1.
RefSeqYP_834829.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4448252.
GenomeReviewsGene locus Bcen2424_1184 in contig CP000458_GR.
KEGGbch:Bcen2424_1184.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMA0K609.
OMAA0K609. 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_BURCH
AccessionPrimary (citable) accession number: A0K609
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: June 16, 2009
This is version 16 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