We are aiming to switch to the new UniProt website on Monday, May 9. Please explore and share your feedback.
Take me to the new website.
UniProtKB - P76216 (ASTB_ECOLI)
Protein
N-succinylarginine dihydrolase
Gene
astB
Organism
Escherichia coli (strain K12)
Status
Functioni
Catalyzes the hydrolysis of N2-succinylarginine into N2-succinylornithine, ammonia and CO2.
2 PublicationsCatalytic activityi
: L-arginine degradation via AST pathway Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes L-glutamate and succinate from L-arginine.1 Publication 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 110 | Substrate | 1 | |
Active sitei | 174 | 1 | ||
Binding sitei | 212 | Substrate | 1 | |
Active sitei | 248 | 1 | ||
Binding sitei | 250 | Substrate | 1 | |
Binding sitei | 359 | Substrate | 1 | |
Active sitei | 365 | Nucleophile | 1 |
GO - Molecular functioni
- N-succinylarginine dihydrolase activity Source: EcoCyc
GO - Biological processi
- arginine catabolic process Source: EcoliWiki
- arginine catabolic process to glutamate Source: UniProtKB-UniRule
- arginine catabolic process to succinate Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Hydrolase |
Biological process | Arginine metabolism, Stress response |
Enzyme and pathway databases
BioCyci | EcoCyc:SUCCARGDIHYDRO-MONOMER |
BRENDAi | 3.5.3.23, 2026 |
UniPathwayi | UPA00185;UER00280 |
Names & Taxonomyi
Protein namesi | |
Gene namesi | Name:astB Synonyms:ydjT Ordered Locus Names:b1745, JW1734 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 365 | C → S: Large decrease in N-succinylarginine dihydrolase activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB02501, N(2)-succinyl-L-arginine DB03582, N~2~-Succinylornithine |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000064715 | 1 – 447 | N-succinylarginine dihydrolaseAdd BLAST | 447 |
Proteomic databases
jPOSTi | P76216 |
PaxDbi | P76216 |
PRIDEi | P76216 |
Expressioni
Inductioni
By nitrogen starvation, and arginine. Induced at stationary phase via sigma S.1 Publication
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 4262234, 10 interactors |
IntActi | P76216, 1 interactor |
STRINGi | 511145.b1745 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P76216 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P76216 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 19 – 28 | Substrate binding | 10 | |
Regioni | 137 – 138 | Substrate binding | 2 |
Sequence similaritiesi
Belongs to the succinylarginine dihydrolase family.Curated
Phylogenomic databases
eggNOGi | COG3724, Bacteria |
HOGENOMi | CLU_053835_0_0_6 |
InParanoidi | P76216 |
PhylomeDBi | P76216 |
Family and domain databases
DisProti | DP02760 |
Gene3Di | 3.75.10.20, 1 hit |
HAMAPi | MF_01172, AstB, 1 hit |
InterProi | View protein in InterPro IPR037031, AstB_sf IPR007079, SuccinylArg_d-Hdrlase_AstB |
Pfami | View protein in Pfam PF04996, AstB, 1 hit |
TIGRFAMsi | TIGR03241, arg_catab_astB, 1 hit |
i Sequence
Sequence statusi: Complete.
P76216-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U00096 Genomic DNA Translation: AAC74815.1 AP009048 Genomic DNA Translation: BAE76516.1 |
PIRi | A64934 |
RefSeqi | NP_416259.1, NC_000913.3 WP_000994973.1, NZ_SSZK01000001.1 |
Genome annotation databases
EnsemblBacteriai | AAC74815; AAC74815; b1745 BAE76516; BAE76516; BAE76516 |
GeneIDi | 946259 |
KEGGi | ecj:JW1734 eco:b1745 |
PATRICi | fig|1411691.4.peg.511 |
Similar proteinsi
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 |
PIRi | A64934 |
RefSeqi | NP_416259.1, NC_000913.3 WP_000994973.1, NZ_SSZK01000001.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
SMRi | P76216 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262234, 10 interactors |
IntActi | P76216, 1 interactor |
STRINGi | 511145.b1745 |
Chemistry databases
DrugBanki | DB02501, N(2)-succinyl-L-arginine DB03582, N~2~-Succinylornithine |
Proteomic databases
jPOSTi | P76216 |
PaxDbi | P76216 |
PRIDEi | P76216 |
Genome annotation databases
EnsemblBacteriai | AAC74815; AAC74815; b1745 BAE76516; BAE76516; BAE76516 |
GeneIDi | 946259 |
KEGGi | ecj:JW1734 eco:b1745 |
PATRICi | fig|1411691.4.peg.511 |
Organism-specific databases
EchoBASEi | EB3752 |
Phylogenomic databases
eggNOGi | COG3724, Bacteria |
HOGENOMi | CLU_053835_0_0_6 |
InParanoidi | P76216 |
PhylomeDBi | P76216 |
Enzyme and pathway databases
UniPathwayi | UPA00185;UER00280 |
BioCyci | EcoCyc:SUCCARGDIHYDRO-MONOMER |
BRENDAi | 3.5.3.23, 2026 |
Miscellaneous databases
EvolutionaryTracei | P76216 |
PROi | PR:P76216 |
Family and domain databases
DisProti | DP02760 |
Gene3Di | 3.75.10.20, 1 hit |
HAMAPi | MF_01172, AstB, 1 hit |
InterProi | View protein in InterPro IPR037031, AstB_sf IPR007079, SuccinylArg_d-Hdrlase_AstB |
Pfami | View protein in Pfam PF04996, AstB, 1 hit |
TIGRFAMsi | TIGR03241, arg_catab_astB, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ASTB_ECOLI | |
Accessioni | P76216Primary (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: | February 23, 2022 | |
This is version 152 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- 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