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Q0BGU9 (ASTB_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 48. 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:Bamb_1065
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length446 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 – 446446N-succinylarginine dihydrolase HAMAP-Rule MF_01172
PRO_1000065715

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

Sequences

Sequence LengthMass (Da)Tools
Q0BGU9 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 9C8CAD015D021187

FASTA44648,330
        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 
GDGRVHFTPA NLCSKLHRAI EHDATRRTLS TLFADPAHFA VHEALTGTPA LGDEGAANHT 

       190        200        210        220        230        240 
RFCAEYGKPG VEFFVYGRAE YRRGPEPKRF PARQTFEASR AVAQRHGLDE TATVYAQQDP 

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

       310        320        330        340        350        360 
VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENAKVAAYL DELAAGNGPI RDVLVFDLRE 

       370        380        390        400        410        420 
SMKNGGGPAC LRLRVVLNDA ERAAVTSNVW MNDTLFASLD AWIEKHYRDR LAPEDLADPT 

       430        440 
LLDESRTALD ELTQILRVGS LYDFQR 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000440 Genomic DNA. Translation: ABI86624.1.
RefSeqYP_772958.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BGU9.
SMRQ0BGU9. Positions 2-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339670.Bamb_1065.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI86624; ABI86624; Bamb_1065.
GeneID4311246.
KEGGbam:Bamb_1065.
PATRIC19017696. VBIBurAmb61564_1144.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3724.
HOGENOMHOG000226005.
KOK01484.
OMAREVNFDG.
OrthoDBEOG6B8XDW.

Enzyme and pathway databases

BioCycBAMB339670:GH48-1101-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_BURCM
AccessionPrimary (citable) accession number: Q0BGU9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 48 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