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Protein

N-succinylarginine dihydrolase

Gene

astB

Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei110 – 1101SubstrateUniRule annotation
Active sitei174 – 1741UniRule annotation
Binding sitei213 – 2131SubstrateUniRule annotation
Active sitei249 – 2491UniRule annotation
Binding sitei251 – 2511SubstrateUniRule annotation
Binding sitei364 – 3641SubstrateUniRule annotation
Active sitei370 – 3701NucleophileUniRule annotation

GO - Molecular functioni

  1. N-succinylarginine dihydrolase activity Source: UniProtKB-HAMAP

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Arginine metabolism

Enzyme and pathway databases

BioCyciBAMB339670:GH48-1101-MONOMER.
UniPathwayiUPA00185; UER00280.

Names & Taxonomyi

Protein namesi
Recommended name:
N-succinylarginine dihydrolaseUniRule annotation (EC:3.5.3.23UniRule annotation)
Gene namesi
Name:astBUniRule annotation
Ordered Locus Names:Bamb_1065
OrganismiBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD))
Taxonomic identifieri339670 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex
ProteomesiUP000000662: Chromosome 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446N-succinylarginine dihydrolasePRO_1000065715Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi339670.Bamb_1065.

Structurei

3D structure databases

ProteinModelPortaliQ0BGU9.
SMRiQ0BGU9. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the succinylarginine dihydrolase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG3724.
HOGENOMiHOG000226005.
KOiK01484.
OMAiREVNFDG.
OrthoDBiEOG6B8XDW.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q0BGU9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNAQEANFDG LVGPTHNYAG LSFGNVASLN NEKSAANPKA AAKQGLRKMK
60 70 80 90 100
QLADLGFAQG VLPPQERPSL RLLRELGFSG KDADVIAKAA KQAPELLAAA
110 120 130 140 150
SSASAMWTAN AATVSPSADT GDGRVHFTPA NLCSKLHRAI EHDATRRTLS
160 170 180 190 200
TLFADPAHFA VHEALTGTPA LGDEGAANHT RFCAEYGKPG VEFFVYGRAE
210 220 230 240 250
YRRGPEPKRF PARQTFEASR AVAQRHGLDE TATVYAQQDP DVIDAGVFHN
260 270 280 290 300
DVISVGNRDT LFTHERAFVN KQAIYDTLTA TLDARGARLN VIEVPDAAVS
310 320 330 340 350
VNDAVTSYLF NSQLLSRADG SQVLVVPQEC RENAKVAAYL DELAAGNGPI
360 370 380 390 400
RDVLVFDLRE SMKNGGGPAC LRLRVVLNDA ERAAVTSNVW MNDTLFASLD
410 420 430 440
AWIEKHYRDR LAPEDLADPT LLDESRTALD ELTQILRVGS LYDFQR
Length:446
Mass (Da):48,330
Last modified:October 17, 2006 - v1
Checksum:i9C8CAD015D021187
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI86624.1.
RefSeqiWP_011656402.1. NC_008390.1.
YP_772958.1. NC_008390.1.

Genome annotation databases

EnsemblBacteriaiABI86624; ABI86624; Bamb_1065.
GeneIDi4311246.
KEGGibam:Bamb_1065.
PATRICi19017696. VBIBurAmb61564_1144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000440 Genomic DNA. Translation: ABI86624.1.
RefSeqiWP_011656402.1. NC_008390.1.
YP_772958.1. NC_008390.1.

3D structure databases

ProteinModelPortaliQ0BGU9.
SMRiQ0BGU9. Positions 2-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi339670.Bamb_1065.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI86624; ABI86624; Bamb_1065.
GeneIDi4311246.
KEGGibam:Bamb_1065.
PATRICi19017696. VBIBurAmb61564_1144.

Phylogenomic databases

eggNOGiCOG3724.
HOGENOMiHOG000226005.
KOiK01484.
OMAiREVNFDG.
OrthoDBiEOG6B8XDW.

Enzyme and pathway databases

UniPathwayiUPA00185; UER00280.
BioCyciBAMB339670:GH48-1101-MONOMER.

Family and domain databases

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

Publicationsi

  1. "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.
    , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-244 / AMMD.

Entry informationi

Entry nameiASTB_BURCM
AccessioniPrimary (citable) accession number: Q0BGU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 51 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

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.