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Reviewed, UniProtKB/Swiss-Prot P76216 (ASTB_ECOLI)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · 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
Synonyms: ydjT
Ordered Locus Names: b1745, JW1734
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO2. Ref.3 Ref.6

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. Ref.6

Induction

By nitrogen starvation, and arginine. Induced at stationary phase via sigma S. Ref.4

Sequence similarities

Belongs to the succinylarginine dihydrolase family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1125311,EBI-543750

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447N-succinylarginine dihydrolase HAMAP MF_01172
PRO_0000064715

Regions

Region19 – 2810Substrate binding HAMAP MF_01172
Region137 – 1382Substrate binding HAMAP MF_01172

Sites

Active site1741 HAMAP MF_01172
Active site2481 HAMAP MF_01172
Active site3651Nucleophile HAMAP MF_01172
Binding site1101Substrate HAMAP MF_01172
Binding site2121Substrate HAMAP MF_01172
Binding site2501Substrate HAMAP MF_01172
Binding site3591Substrate HAMAP MF_01172

Experimental info

Mutagenesis3651C → S: Large decrease in activity. Ref.6

Secondary structure

1 ...................................................................................... 447
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P76216-1 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 710AE691E413AF64

FASTA44749,299
        10         20         30         40         50         60 
MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK ALADAGFPQA 

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

       130        140        150        160        170        180 
LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS 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 ATQVSVSDTV 

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

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

       430        440 
REALDVLSQL LNLGSVYPFQ REGGGNG

« Hide

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References

« Hide 'large scale' references
[1]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli."
Schneider B.L., Kiupakis A.K., Reitzer L.J.
J. Bacteriol. 180:4278-4286(1998) [PubMed: 9696779] [Abstract]
Cited for: FUNCTION.
[4]"ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli."
Kiupakis A.K., Reitzer L.
J. Bacteriol. 184:2940-2950(2002) [PubMed: 12003934] [Abstract]
Cited for: INDUCTION.
[5]"Prediction of the structure and function of AstA and AstB, the first two enzymes of the arginine succinyltransferase pathway of arginine catabolism."
Shirai H., Mizuguchi K.
FEBS Lett. 555:505-510(2003) [PubMed: 14675764] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[6]"Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli."
Tocilj A., Schrag J.D., Li Y., Schneider B.L., Reitzer L., Matte A., Cygler M.
J. Biol. Chem. 280:15800-15808(2005) [PubMed: 15703173] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-447 OF WILD-TYPE AND MUTANT SER-365 IN COMPLEXES WITH SUBSTRATE, FUNCTION, SUBUNIT, MUTAGENESIS OF CYS-365.

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Cross-references

Sequence databases

U00096 Genomic DNA. Translation: AAC74815.1.
AP009048 Genomic DNA. Translation: BAE76516.1.
PIRA64934.
RefSeqAP_002364.1.
NP_416259.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1YNFX-ray1.90A/B/C/D/E/F2-447[»]
1YNHX-ray1.95A/B/C/D2-447[»]
1YNIX-ray2.20A/B/C/D2-447[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP76216. 1 interaction.

Genome annotation databases

GeneID946259.
GenomeReviewsGene locus JW1734 in contig AP009048_GR.
Gene locus b1745 in contig U00096_GR.
KEGGecj:JW1734.
eco:b1745.

Organism-specific databases

EchoBASEEB3752.
EcoGeneEG13996. astB.
CMRSearch...

Phylogenomic databases

HOGENOMP76216.
OMAP76216. HFAHHPA.

Enzyme and pathway databases

BioCycEcoCyc:SUCCARGDIHYDRO-MON.
MetaCyc:SUCCARGDIHYDRO-MON.
BRENDA3.5.3.23. 246.

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_ECOLI
AccessionPrimary (citable) accession number: P76216
Secondary accession number(s): Q2MB40
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: June 16, 2009
This is version 67 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

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents