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Protein

N-succinylarginine dihydrolase

Gene

astB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

N(2)-succinyl-L-arginine + 2 H2O = N(2)-succinyl-L-ornithine + 2 NH3 + CO2.

Pathwayi: L-arginine degradation via AST pathway

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate and succinate from L-arginine.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Arginine N-succinyltransferase (astA)
  2. N-succinylarginine dihydrolase (astB)
  3. Succinylornithine transaminase (astC)
  4. N-succinylglutamate 5-semialdehyde dehydrogenase (astD)
  5. Succinylglutamate desuccinylase (astE)
This subpathway is part of the pathway L-arginine degradation via AST pathway, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate and succinate from L-arginine, the pathway L-arginine degradation via AST pathway and in Amino-acid degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei110Substrate1
Active sitei1741
Binding sitei212Substrate1
Active sitei2481
Binding sitei250Substrate1
Binding sitei359Substrate1
Active sitei365Nucleophile1

GO - Molecular functioni

  • N-succinylarginine dihydrolase activity Source: EcoCyc

GO - Biological processi

  • arginine catabolic process Source: EcoliWiki
  • arginine catabolic process to glutamate Source: UniProtKB-HAMAP
  • arginine catabolic process to succinate Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism, Stress response

Enzyme and pathway databases

BioCyciEcoCyc:SUCCARGDIHYDRO-MONOMER.
ECOL316407:JW1734-MONOMER.
MetaCyc:SUCCARGDIHYDRO-MONOMER.
BRENDAi3.5.3.23. 2026.
UniPathwayiUPA00185; UER00280.

Names & Taxonomyi

Protein namesi
Recommended name:
N-succinylarginine dihydrolase (EC:3.5.3.23)
Gene namesi
Name:astB
Synonyms:ydjT
Ordered Locus Names:b1745, JW1734
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13996. astB.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi365C → S: Large decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000647151 – 447N-succinylarginine dihydrolaseAdd BLAST447

Proteomic databases

EPDiP76216.
PaxDbiP76216.
PRIDEiP76216.

Expressioni

Inductioni

By nitrogen starvation, and arginine. Induced at stationary phase via sigma S.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4262234. 10 interactors.
IntActiP76216. 1 interactor.
STRINGi511145.b1745.

Structurei

Secondary structure

1447
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi26 – 30Combined sources5
Turni31 – 33Combined sources3
Helixi38 – 54Combined sources17
Beta strandi59 – 62Combined sources4
Helixi70 – 75Combined sources6
Helixi82 – 92Combined sources11
Helixi95 – 99Combined sources5
Helixi104 – 106Combined sources3
Helixi108 – 110Combined sources3
Beta strandi112 – 115Combined sources4
Turni117 – 119Combined sources3
Beta strandi123 – 129Combined sources7
Helixi136 – 139Combined sources4
Helixi142 – 152Combined sources11
Turni156 – 158Combined sources3
Beta strandi159 – 162Combined sources4
Helixi169 – 171Combined sources3
Helixi175 – 178Combined sources4
Beta strandi179 – 182Combined sources4
Beta strandi191 – 198Combined sources8
Beta strandi207 – 209Combined sources3
Helixi215 – 224Combined sources10
Helixi229 – 231Combined sources3
Beta strandi232 – 237Combined sources6
Helixi239 – 242Combined sources4
Turni243 – 245Combined sources3
Helixi249 – 251Combined sources3
Beta strandi253 – 256Combined sources4
Beta strandi259 – 263Combined sources5
Helixi270 – 280Combined sources11
Beta strandi285 – 289Combined sources5
Turni291 – 293Combined sources3
Helixi296 – 302Combined sources7
Turni303 – 305Combined sources3
Beta strandi306 – 311Combined sources6
Beta strandi317 – 322Combined sources6
Helixi323 – 326Combined sources4
Helixi329 – 340Combined sources12
Beta strandi341 – 351Combined sources11
Helixi354 – 358Combined sources5
Turni363 – 366Combined sources4
Beta strandi367 – 372Combined sources6
Helixi374 – 379Combined sources6
Helixi382 – 384Combined sources3
Helixi388 – 401Combined sources14
Helixi408 – 412Combined sources5
Helixi414 – 430Combined sources17
Helixi438 – 440Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP76216.
SMRiP76216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76216.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni19 – 28Substrate binding10
Regioni137 – 138Substrate binding2

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EY2. Bacteria.
COG3724. LUCA.
HOGENOMiHOG000226005.
InParanoidiP76216.
KOiK01484.
OMAiRVAMNDQ.

Family and domain databases

Gene3Di3.75.10.20. 1 hit.
HAMAPiMF_01172. AstB. 1 hit.
InterProiIPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]
PfamiPF04996. AstB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03241. arg_catab_astB. 1 hit.

Sequencei

Sequence statusi: Complete.

P76216-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK
60 70 80 90 100
ALADAGFPQA VIPPHERPFI PVLRQLGFSG SDEQVLEKVA RQAPHWLSSV
110 120 130 140 150
SSASPMWVAN AATIAPSADT LDGKVHLTVA NLNNKFHRSL EAPVTESLLK
160 170 180 190 200
AIFNDEEKFS VHSALPQVAL LGDEGAANHN RLGGHYGEPG MQLFVYGREE
210 220 230 240 250
GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD VIDQGVFHND
260 270 280 290 300
VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVSVSDTV
310 320 330 340 350
STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV
360 370 380 390 400
FDLRESMANG GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR
410 420 430 440
YYRDRLTAAD LADPQLLREG REALDVLSQL LNLGSVYPFQ REGGGNG
Length:447
Mass (Da):49,299
Last modified:February 1, 1997 - v1
Checksum:i710AE691E413AF64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74815.1.
AP009048 Genomic DNA. Translation: BAE76516.1.
PIRiA64934.
RefSeqiNP_416259.1. NC_000913.3.
WP_000994973.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74815; AAC74815; b1745.
BAE76516; BAE76516; BAE76516.
GeneIDi946259.
KEGGiecj:JW1734.
eco:b1745.
PATRICi32118799. VBIEscCol129921_1817.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74815.1.
AP009048 Genomic DNA. Translation: BAE76516.1.
PIRiA64934.
RefSeqiNP_416259.1. NC_000913.3.
WP_000994973.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP76216.
SMRiP76216.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262234. 10 interactors.
IntActiP76216. 1 interactor.
STRINGi511145.b1745.

Proteomic databases

EPDiP76216.
PaxDbiP76216.
PRIDEiP76216.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74815; AAC74815; b1745.
BAE76516; BAE76516; BAE76516.
GeneIDi946259.
KEGGiecj:JW1734.
eco:b1745.
PATRICi32118799. VBIEscCol129921_1817.

Organism-specific databases

EchoBASEiEB3752.
EcoGeneiEG13996. astB.

Phylogenomic databases

eggNOGiENOG4105EY2. Bacteria.
COG3724. LUCA.
HOGENOMiHOG000226005.
InParanoidiP76216.
KOiK01484.
OMAiRVAMNDQ.

Enzyme and pathway databases

UniPathwayiUPA00185; UER00280.
BioCyciEcoCyc:SUCCARGDIHYDRO-MONOMER.
ECOL316407:JW1734-MONOMER.
MetaCyc:SUCCARGDIHYDRO-MONOMER.
BRENDAi3.5.3.23. 2026.

Miscellaneous databases

EvolutionaryTraceiP76216.
PROiP76216.

Family and domain databases

Gene3Di3.75.10.20. 1 hit.
HAMAPiMF_01172. AstB. 1 hit.
InterProiIPR007079. SuccinylArg_d-Hdrlase_AstB.
[Graphical view]
PfamiPF04996. AstB. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03241. arg_catab_astB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiASTB_ECOLI
AccessioniPrimary (citable) accession number: P76216
Secondary accession number(s): Q2MB40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: February 1, 1997
Last modified: November 2, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.