N-succinylarginine dihydrolase - Escherichia coli (strain K12)

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P76216 (ASTB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
N-succinylarginine dihydrolase
EC=3.5.3.23

Gene names

Name:	astB
Synonyms:	ydjT
Ordered Locus Names:	b1745, JW1734

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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-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. 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.

Ontologies

Keywords
Biological process	Arginine metabolism Stress response
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	arginine catabolic process Inferred from mutant phenotype Ref.3. Source: EcoliWiki arginine catabolic process to glutamate Inferred from electronic annotation. Source: HAMAP arginine catabolic process to succinate Inferred from electronic annotation. Source: UniProtKB-UniPathway response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	N-succinylarginine dihydrolase activity Inferred from direct assay Ref.6. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-1125311,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 447

447

N-succinylarginine dihydrolase HAMAP-Rule MF_01172

PRO_0000064715

Regions

Region

19 – 28

Substrate binding HAMAP-Rule MF_01172

Region

137 – 138

Substrate binding HAMAP-Rule MF_01172

Sites

Active site

174

Active site

248

Active site

365

Nucleophile

Binding site

110

Substrate

Binding site

212

Substrate

Binding site

250

Substrate

Binding site

359

Substrate

Experimental info

Mutagenesis

365

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

Secondary structure

447

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P76216 [UniParc].

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

FASTA

447

49,299

        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

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC74815.1.
AP009048 Genomic DNA. Translation: BAE76516.1.

PIR

A64934.

RefSeq

NP_416259.1. NC_000913.2.
YP_490006.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1YNF	X-ray	1.90	A/B/C/D/E/F	2-447	[»]
1YNH	X-ray	1.95	A/B/C/D	2-447	[»]
1YNI	X-ray	2.20	A/B/C/D	2-447	[»]

ProteinModelPortal

P76216.

SMR

P76216. Positions 2-441.

ModBase

Search...

Protein-protein interaction databases

IntAct

P76216. 1 interaction.

STRING

511145.b1745.

Proteomic databases

PaxDb

P76216.

PRIDE

P76216.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74815; AAC74815; b1745.
BAE76516; BAE76516; BAE76516.

GeneID

12933240.
946259.

KEGG

ecj:Y75_p1720.
eco:b1745.

PATRIC

32118799. VBIEscCol129921_1817.

Organism-specific databases

EchoBASE

EB3752.

EcoGene

EG13996. astB.

Phylogenomic databases

eggNOG

COG3724.

HOGENOM

HOG000226005.

K01484.

OMA

HFAHHPA.

ProtClustDB

PRK13281.

Enzyme and pathway databases

BioCyc

EcoCyc:SUCCARGDIHYDRO-MONOMER.
ECOL316407:JW1734-MONOMER.
MetaCyc:SUCCARGDIHYDRO-MONOMER.

BRENDA

3.5.3.23. 2026.

UniPathway

UPA00185; UER00280.

Gene expression databases

Genevestigator

P76216.

Family and domain databases

Gene3D

3.75.10.20. 1 hit.

HAMAP

MF_01172. AstB.

InterPro

IPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]

Pfam

PF04996. AstB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03241. arg_catab_astB. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P76216.

Entry information

Entry name

ASTB_ECOLI

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents