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Protein

Argininosuccinate synthase

Gene

argG

Organism
Heliobacillus mobilis
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate.UniRule annotation

Pathway: L-arginine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Argininosuccinate synthase (argG)
  3. Argininosuccinate lyase
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei41 – 411ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei92 – 921CitrullineUniRule annotation
Binding sitei97 – 971CitrullineUniRule annotation
Binding sitei122 – 1221ATP; via amide nitrogenUniRule annotation
Binding sitei124 – 1241AspartateUniRule annotation
Binding sitei128 – 1281AspartateUniRule annotation
Binding sitei128 – 1281CitrullineUniRule annotation
Binding sitei129 – 1291AspartateUniRule annotation
Binding sitei132 – 1321CitrullineUniRule annotation
Binding sitei181 – 1811CitrullineUniRule annotation
Binding sitei190 – 1901CitrullineUniRule annotation
Binding sitei266 – 2661CitrullineUniRule annotation
Binding sitei278 – 2781CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate synthaseUniRule annotation (EC:6.3.4.5UniRule annotation)
Alternative name(s):
Citrulline--aspartate ligaseUniRule annotation
Gene namesi
Name:argGUniRule annotation
OrganismiHeliobacillus mobilis
Taxonomic identifieri28064 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacillus

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›408›408Argininosuccinate synthasePRO_0000148598Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8GDU2.
SMRiQ8GDU2. Positions 10-403.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 1 subfamily.UniRule annotation

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q8GDU2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGALGMSKK VVLAYSGGLD TSIIIPWLKE NYGYEVIAMA ADLGQGEELE
60 70 80 90 100
PLNEKAINTG ATKIYIEDVK EEFVTEFIWP TLKAGAVYEG KYLLGTSFAR
110 120 130 140 150
PLIAKRLVEI ARKEGAEAIA HGATGKGNDQ VRFELTVKAL APDLKIVAPW
160 170 180 190 200
REWDIRSRED AIDYAQARNI PVPVKKDRPY SMDRNLWHLS HEGADLESPW
210 220 230 240 250
NEPQNDLFMI CTPPEQAPDK PEYVEIEFEK GIPVKLNGEA LGPVEMIEKL
260 270 280 290 300
NAIAAAHGVG ICDMVENRLV GMKSRGVYET PAGTVLYAAH RELEYLCLDR
310 320 330 340 350
ATMHYKEMVA LRYAELVYDG VWYHPLRKAI DAFVDVTQET VTGLVRMKLF
360 370 380 390 400
KGSVTPAGAK SPYSLYNEEF STFGRDEVYN QKDAEGFINL FGLPMKVRAL

MEQKSGLK
Length:408
Mass (Da):45,642
Last modified:March 1, 2003 - v1
Checksum:i9B4DEC08F0640542
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei408 – 4081

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY142882 Genomic DNA. Translation: AAN87486.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY142882 Genomic DNA. Translation: AAN87486.1.

3D structure databases

ProteinModelPortaliQ8GDU2.
SMRiQ8GDU2. Positions 10-403.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1.
InterProiIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR023434. Arginosuc_synth_type_1_subfam.
IPR024074. AS_cat/multimer_dom_body.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00032. argG. 1 hit.
PROSITEiPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiASSY_HELMO
AccessioniPrimary (citable) accession number: Q8GDU2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: March 1, 2003
Last modified: January 7, 2015
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.