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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 oxygen By similarity
Binding sitei92 – 921Citrulline By similarity
Binding sitei97 – 971Citrulline By similarity
Binding sitei122 – 1221ATP; via amide nitrogen By similarity
Binding sitei124 – 1241Aspartate By similarity
Binding sitei128 – 1281Aspartate By similarity
Binding sitei128 – 1281Citrulline By similarity
Binding sitei129 – 1291Aspartate By similarity
Binding sitei132 – 1321Citrulline By similarity
Binding sitei181 – 1811Citrulline By similarity
Binding sitei190 – 1901Citrulline By similarity
Binding sitei266 – 2661Citrulline By similarity
Binding sitei278 – 2781Citrulline By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 229ATP By similarity

GO - Molecular functioni

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

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 synthase (EC:6.3.4.5)
Alternative name(s):
Citrulline--aspartate ligase
Gene namesi
Name:argG
OrganismiHeliobacillus mobilis
Taxonomic identifieri28064 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesHeliobacteriaceaeHeliobacillus

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›408›408Argininosuccinate synthaseUniRule annotation
PRO_0000148598Add
BLAST

Interactioni

Subunit structurei

Homotetramer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8GDU2.
SMRiQ8GDU2. Positions 10-403.

Family & Domainsi

Sequence similaritiesi

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

MKGALGMSKK VVLAYSGGLD TSIIIPWLKE NYGYEVIAMA ADLGQGEELE    50
PLNEKAINTG ATKIYIEDVK EEFVTEFIWP TLKAGAVYEG KYLLGTSFAR 100
PLIAKRLVEI ARKEGAEAIA HGATGKGNDQ VRFELTVKAL APDLKIVAPW 150
REWDIRSRED AIDYAQARNI PVPVKKDRPY SMDRNLWHLS HEGADLESPW 200
NEPQNDLFMI CTPPEQAPDK PEYVEIEFEK GIPVKLNGEA LGPVEMIEKL 250
NAIAAAHGVG ICDMVENRLV GMKSRGVYET PAGTVLYAAH RELEYLCLDR 300
ATMHYKEMVA LRYAELVYDG VWYHPLRKAI DAFVDVTQET VTGLVRMKLF 350
KGSVTPAGAK SPYSLYNEEF STFGRDEVYN QKDAEGFINL FGLPMKVRAL 400
MEQKSGLK 408
Length:408
Mass (Da):45,642
Last modified:March 1, 2003 - v1
Checksum:i9B4DEC08F0640542
GO

Non-terminal residue

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...

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: February 19, 2014
This is version 57 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

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