Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101Substrate
Active sitei174 – 1741
Binding sitei212 – 2121Substrate
Active sitei248 – 2481
Binding sitei250 – 2501Substrate
Binding sitei359 – 3591Substrate
Active sitei365 – 3651Nucleophile

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13996. astB.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi365 – 3651C → S: Large decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 447447N-succinylarginine dihydrolasePRO_0000064715Add
BLAST

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 interactions.
IntActiP76216. 1 interaction.
STRINGi511145.b1745.

Structurei

Secondary structure

1
447
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi26 – 305Combined sources
Turni31 – 333Combined sources
Helixi38 – 5417Combined sources
Beta strandi59 – 624Combined sources
Helixi70 – 756Combined sources
Helixi82 – 9211Combined sources
Helixi95 – 995Combined sources
Helixi104 – 1063Combined sources
Helixi108 – 1103Combined sources
Beta strandi112 – 1154Combined sources
Turni117 – 1193Combined sources
Beta strandi123 – 1297Combined sources
Helixi136 – 1394Combined sources
Helixi142 – 15211Combined sources
Turni156 – 1583Combined sources
Beta strandi159 – 1624Combined sources
Helixi169 – 1713Combined sources
Helixi175 – 1784Combined sources
Beta strandi179 – 1824Combined sources
Beta strandi191 – 1988Combined sources
Beta strandi207 – 2093Combined sources
Helixi215 – 22410Combined sources
Helixi229 – 2313Combined sources
Beta strandi232 – 2376Combined sources
Helixi239 – 2424Combined sources
Turni243 – 2453Combined sources
Helixi249 – 2513Combined sources
Beta strandi253 – 2564Combined sources
Beta strandi259 – 2635Combined sources
Helixi270 – 28011Combined sources
Beta strandi285 – 2895Combined sources
Turni291 – 2933Combined sources
Helixi296 – 3027Combined sources
Turni303 – 3053Combined sources
Beta strandi306 – 3116Combined sources
Beta strandi317 – 3226Combined sources
Helixi323 – 3264Combined sources
Helixi329 – 34012Combined sources
Beta strandi341 – 35111Combined sources
Helixi354 – 3585Combined sources
Turni363 – 3664Combined sources
Beta strandi367 – 3726Combined sources
Helixi374 – 3796Combined sources
Helixi382 – 3843Combined sources
Helixi388 – 40114Combined sources
Helixi408 – 4125Combined sources
Helixi414 – 43017Combined sources
Helixi438 – 4403Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP76216.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 2810Substrate binding
Regioni137 – 1382Substrate binding

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
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. Positions 2-441.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262234. 10 interactions.
IntActiP76216. 1 interaction.
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: September 7, 2016
This is version 120 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.