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Protein

Argininosuccinate synthase

Gene

argG

Organism
Chelativorans sp. (strain BNC1)
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

Pathwayi: 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 (argH)
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)DescriptionActionsGraphical viewLength
Binding sitei40ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei91CitrullineUniRule annotation1
Binding sitei96CitrullineUniRule annotation1
Binding sitei121ATP; via amide nitrogenUniRule annotation1
Binding sitei123AspartateUniRule annotation1
Binding sitei127AspartateUniRule annotation1
Binding sitei127CitrullineUniRule annotation1
Binding sitei128AspartateUniRule annotation1
Binding sitei131CitrullineUniRule annotation1
Binding sitei182CitrullineUniRule annotation1
Binding sitei191CitrullineUniRule annotation1
Binding sitei267CitrullineUniRule annotation1
Binding sitei279CitrullineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 21ATPUniRule annotation9

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
Ordered Locus Names:Meso_3344
OrganismiChelativorans sp. (strain BNC1)
Taxonomic identifieri266779 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeChelativorans
Proteomesi
  • UP000001820 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002639381 – 408Argininosuccinate synthaseAdd BLAST408

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi266779.Meso_3344.

Structurei

3D structure databases

ProteinModelPortaliQ11D10.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CDH. Bacteria.
COG0137. LUCA.
HOGENOMiHOG000230093.
KOiK01940.
OrthoDBiPOG091H01U0.

Family and domain databases

CDDicd01999. Argininosuccinate_Synthase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1. 1 hit.
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: Complete.

Q11D10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATHKDVKKV VLAYSGGLDT SIILKWLQTE LGAEVVTFTA DLGQGEELEP
60 70 80 90 100
ARRKAEMLGI KEIHIEDLRE EFVRDFVFPM FRANALYEGT YLLGTSIARP
110 120 130 140 150
LIAKRLVEIA AETGADAIAH GATGKGNDQV RFELTAYALN PDIKVIAPWR
160 170 180 190 200
DWTFKSRTDL LNFARDHQIP VPSDKQGEAP FSVDANLLHS SSEGKVLEDP
210 220 230 240 250
WSEPPEYVHQ RTVSPFDAPD RATEITIGFK RGDAVSLNGE AVSPATLLAK
260 270 280 290 300
LNDLGRDNGI GRIDLVENRF VGMKSRGVYE TPGGTILLAA HRAIESITLD
310 320 330 340 350
RGAAHLKDEL MPRYAELIYN GFWYSPEREM LQALIDKSQE DVEGEVRLKL
360 370 380 390 400
YKGNVIVTGR RSDKSLYSDA LVTFEDDRGA YDQKDAAGFI RLNALRLRTL

AARKRLQG
Length:408
Mass (Da):45,384
Last modified:December 12, 2006 - v2
Checksum:i8789F6DC2C4BF6F8
GO

Sequence cautioni

The sequence ABG64715 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000390 Genomic DNA. Translation: ABG64715.1. Different initiation.
RefSeqiWP_041544853.1. NC_008254.1.

Genome annotation databases

EnsemblBacteriaiABG64715; ABG64715; Meso_3344.
KEGGimes:Meso_3344.
PATRICi21347002. VBICheSp72577_4104.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000390 Genomic DNA. Translation: ABG64715.1. Different initiation.
RefSeqiWP_041544853.1. NC_008254.1.

3D structure databases

ProteinModelPortaliQ11D10.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266779.Meso_3344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABG64715; ABG64715; Meso_3344.
KEGGimes:Meso_3344.
PATRICi21347002. VBICheSp72577_4104.

Phylogenomic databases

eggNOGiENOG4105CDH. Bacteria.
COG0137. LUCA.
HOGENOMiHOG000230093.
KOiK01940.
OrthoDBiPOG091H01U0.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Family and domain databases

CDDicd01999. Argininosuccinate_Synthase. 1 hit.
Gene3Di3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00005. Arg_succ_synth_type1. 1 hit.
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...

Entry informationi

Entry nameiASSY_CHESB
AccessioniPrimary (citable) accession number: Q11D10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: December 12, 2006
Last modified: November 2, 2016
This is version 64 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.