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Reviewed, UniProtKB/Swiss-Prot Q5WVZ3 (ASTB_LEGPL)

Last modified June 16, 2009. Version 30. 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: lpl1667
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

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Protein attributes

Sequence length448 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 – 448448N-succinylarginine dihydrolase HAMAP MF_01172
PRO_0000262355

Regions

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

Sites

Active site1741 By similarity
Active site2521 By similarity
Active site3721Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2161Substrate By similarity
Binding site2541Substrate By similarity
Binding site3661Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5WVZ3-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 86B2FBD856161173

FASTA44850,198
        10         20         30         40         50         60 
MNVYELNMDG LVGQTHHYAG LSSGNIASTN NALSISNPQA AARQGLEKMR RLYNMGLKQG 

        70         80         90        100        110        120 
LLPPHQRPNL NLLYQLGFKG TPSEQINKAY KTAPELLSAC YSASCMWTAN AATVSASVDT 

       130        140        150        160        170        180 
EDNKVHFTAA NLISNLHRHQ EADFSKKLLE FIFSNSDYFN HHPLLPKSMG TSDEGAANHN 

       190        200        210        220        230        240 
RLCQSHAHSG INLFVYGKKV LGNHQFEQSP IKYPARQTKE ASEAIARNHL LNPERVIFAC 

       250        260        270        280        290        300 
QNPLAIDQGV FHNDVISVAN EHVFLVHEEA FYNQTYVLDQ LREKADFPLV IIQISKEQIS 

       310        320        330        340        350        360 
VSEAVDTYLF NSQLITLPDQ KNMILIAPAE CQANLKVKTC IDGLVADPQN PINSVYYLDL 

       370        380        390        400        410        420 
KQSMRNGGGP ACLRLRVPLN DYELKAMHQG ILIDNDLLDI LDKWVLKYYR TELKISDLAD 

       430        440 
PQLLYECLDA LDELTQILKL GSIYPFQS

« Hide

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References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CR628337 Genomic DNA. Translation: CAH15907.1.
RefSeqYP_127006.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3113610.
GenomeReviewsGene locus lpl1667 in contig CR628337_GR.
KEGGlpf:lpl1667.
NMPDRfig|297245.3.peg.1849.

Organism-specific databases

LegioListlpl1667.
CMRSearch...

Phylogenomic databases

HOGENOMQ5WVZ3.
OMAQ5WVZ3. HFAHHPA.

Enzyme and pathway databases

BioCycLPNE297245:LPL1667-MON.

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_LEGPL
AccessionPrimary (citable) accession number: Q5WVZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: November 23, 2004
Last modified: June 16, 2009
This is version 30 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