Skip Header

Contribute Send feedback
Read comments (?) or add your own

A7ZML3 (ASTB_ECO24) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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
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:EcE24377A_1967
OrganismEscherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]
Taxonomic identifier331111 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length447 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 MF_01172

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. HAMAP 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 metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionN-succinylarginine dihydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447N-succinylarginine dihydrolase HAMAP MF_01172
PRO_1000065723

Regions

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

Sites

Active site1741 By similarity
Active site2481 By similarity
Active site3651Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site2121Substrate By similarity
Binding site2501Substrate By similarity
Binding site3591Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A7ZML3 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: 5E8293820910D15D

FASTA44749,212
        10         20         30         40         50         60 
MNAWEVNFDG LVGLTHHYAG LSFGNEASTC HRFQVSNPRQ AAKQGLLKMK ALADAGFPQA 

        70         80         90        100        110        120 
VIPPHERPFI PVLRQLGFSG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT 

       130        140        150        160        170        180 
LDGKVHLTVA NLNNKFHRSL EAHVTESLLK AIFNDKEKFS VHSALPQVAL LGDEGAANHN 

       190        200        210        220        230        240 
RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD 

       250        260        270        280        290        300 
VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVSVSDAV 

       310        320        330        340        350        360 
STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV FDLRESMANG 

       370        380        390        400        410        420 
GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLRGG 

       430        440 
REALDILSQL LNLGSVYPFQ REGGGNG

« Hide

References

[1]"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E24377A / ETEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000800 Genomic DNA. Translation: ABV17269.1.
RefSeqYP_001463042.1. NC_009801.1.

3D structure databases

ProteinModelPortalA7ZML3.
SMRA7ZML3. Positions 2-441.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7ZML3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000023006; EBESCP00000022068; EBESCG00000022060.
GeneID5585946.
GenomeReviewsGene locus EcE24377A_1967 in contig CP000800_GR.
KEGGecw:EcE24377A_1967.
NMPDRfig|331111.3.peg.4388.
PATRIC18293180. VBIEscCol31211_2243.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3724.
GeneTreeEBGT00050000010790.
HOGENOMHBG289862.
OMAHFAHHPA.
ProtClustDBPRK13281.

Enzyme and pathway databases

BioCycECOL331111:ECE24377A_1967-MONOMER.

Family and domain databases

HAMAPMF_01172. AstB.
[Tree]
InterProIPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]
Gene3DG3DSA:3.75.10.20. SuccinylArg_di_hydro. 1 hit.
KOK01484.
PfamPF04996. AstB. 1 hit.
[Graphical view]
TIGRFAMsTIGR03241. Arg_catab_astB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASTB_ECO24
AccessionPrimary (citable) accession number: A7ZML3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents