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Reviewed, UniProtKB/Swiss-Prot A9L516 (ASTB_SHEB9)

Last modified June 16, 2009. Version 11. 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

Names and origin

Protein namesRecommended name:
    N-succinylarginine dihydrolase
    EC=3.5.3.23
Gene names
Name: astB
Ordered Locus Names: Sbal195_2610
OrganismShewanella baltica (strain OS195) [Complete proteome] [HAMAP]
Taxonomic identifier399599 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

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...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444N-succinylarginine dihydrolase HAMAP MF_01172
PRO_1000085397

Regions

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

Sites

Active site1741 By similarity
Active site2501 By similarity
Active site3681Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2141Substrate By similarity
Binding site2521Substrate By similarity
Binding site3621Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9L516-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 9F0A1E5B99A9C6A4

FASTA44449,176
        10         20         30         40         50         60 
MKHFEANFDG LVGPTHNYAG LSFGNVASLS NAALVSNPKA AAKQGLQKAK ALADMGMVQG 

        70         80         90        100        110        120 
MLAPQERPDL YTLRRIGFSG SDANVLKQAA KEAPMLLNAC CSASSMWTAN AATVSPSADT 

       130        140        150        160        170        180 
RDGKLHFTPA NLVDKLHRSI EPLTTGRILT ATFSDPHYFH HHSHLPEHNS FGDEGAANQT 

       190        200        210        220        230        240 
RLCNEYGHAG VELFVYGQEA TNPNAPKPQK YPARQTLEAS MAVARLHQLE EDNCVFIQQN 

       250        260        270        280        290        300 
PDVIDQGVFH NDVIAVGNQN VLFYHEQAFL NTQHKIDEIK RKLDTELYFI EVPTAKVAIN 

       310        320        330        340        350        360 
DAVKSYLFNT QIITLPSGEM AIIAPTDCQE NPAVFAYLNE LLTLNTPIKQ VLYFDVKQSM 

       370        380        390        400        410        420 
QNGGGPACLR LRVAMNEMEV AAVNQHTLMN DALFARLNLW VDKHYRDRLT TQDLADPQLI 

       430        440 
IESRTALDEL TQIMKLGSVY QFQR 

« Hide

References

[1]"Complete sequence of chromosome of Shewanella baltica OS195."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Brettar I., Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000891 Genomic DNA. Translation: ABX49778.1.
RefSeqYP_001555038.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5754369.
GenomeReviewsGene locus Sbal195_2610 in contig CP000891_GR.
KEGGsbn:Sbal195_2610.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAA9L516. KMKALME.

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...

Entry information

Entry nameASTB_SHEB9
AccessionPrimary (citable) accession number: A9L516
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 11 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)

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