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Q8GDU2

- ASSY_HELMO

UniProt

Q8GDU2 - ASSY_HELMO

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Protein

Argininosuccinate synthase

Gene

argG

Organism
Heliobacillus mobilis
Status
Reviewed - 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

Pathwayi

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

  1. argininosuccinate synthase activity Source: UniProtKB-EC
  2. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-UniPathway
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

  1. cytoplasm Source: UniProtKB-KW
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:
EMBL
GenBank
DDBJ
Links Updated
AY142882 Genomic DNA. Translation: AAN87486.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY142882 Genomic DNA. Translation: AAN87486.1 .

3D structure databases

ProteinModelPortali Q8GDU2.
SMRi Q8GDU2. Positions 10-403.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00068 ; UER00113 .

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPi MF_00005. Arg_succ_synth_type1.
InterProi IPR001518. 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 ]
Pfami PF00764. Arginosuc_synth. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00032. argG. 1 hit.
PROSITEi PS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 59 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