Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Argininosuccinate synthase

Gene

argG

Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Status
Reviewed-Annotation score: -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 sitei34ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei85CitrullineUniRule annotation1
Binding sitei90CitrullineUniRule annotation1
Binding sitei115ATP; via amide nitrogenUniRule annotation1
Binding sitei117AspartateUniRule annotation1
Binding sitei121AspartateUniRule annotation1
Binding sitei121CitrullineUniRule annotation1
Binding sitei122AspartateUniRule annotation1
Binding sitei125CitrullineUniRule annotation1
Binding sitei174CitrullineUniRule annotation1
Binding sitei183CitrullineUniRule annotation1
Binding sitei259CitrullineUniRule annotation1
Binding sitei271CitrullineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi7 – 15ATPUniRule annotation9

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLigase
Biological processAmino-acid biosynthesis, Arginine biosynthesis
LigandATP-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:PTH_0507
OrganismiPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Taxonomic identifieri370438 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum
Proteomesi
  • UP000006556 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000738231 – 401Argininosuccinate synthaseAdd BLAST401

Proteomic databases

PRIDEiA5D510

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi370438.PTH_0507

Structurei

3D structure databases

ProteinModelPortaliA5D510
SMRiA5D510
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
OMAiGVGRIDM
OrthoDBiPOG091H01U0

Family and domain databases

CDDicd01999 Argininosuccinate_Synthase, 1 hit
Gene3Di3.40.50.620, 2 hits
3.90.1260.10, 2 hits
HAMAPiMF_00005 Arg_succ_synth_type1, 1 hit
InterProiView protein in InterPro
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
PANTHERiPTHR11587 PTHR11587, 1 hit
PfamiView protein in Pfam
PF00764 Arginosuc_synth, 1 hit
TIGRFAMsiTIGR00032 argG, 1 hit
PROSITEiView protein in PROSITE
PS00564 ARGININOSUCCIN_SYN_1, 1 hit
PS00565 ARGININOSUCCIN_SYN_2, 1 hit

Sequencei

Sequence statusi: Complete.

A5D510-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVVLAYSG GLDTSVAIPW LKENYGYEVI AMSADLGQGE ELAPLREKAI
60 70 80 90 100
KSGASKIYIE DVRREFVEDY IFPTLKAGAV YEGKYLLGTS MARPLIAKKL
110 120 130 140 150
VEIARKEGAE AVAHGATGKG NDQVRFELAV KALAPDLKII APWREWDIRS
160 170 180 190 200
REDAVDYASA RGIPVPVTRE RPYSLDRNLW HLSHEGADLE DPGNEPPSDV
210 220 230 240 250
LLLITPPEKA PDKPAYVKIE FERGVPVKLD GEALDPVTLI ERLNKIAGEN
260 270 280 290 300
GVGIADMVEN RLVGMKSRGV YETPGGTVLF LAHRELELLT LDRATLHFKE
310 320 330 340 350
IVASRYAELV YDGMWFVPLR EALDAFVDVT QRTVTGTVVM KLYKGNCTPA
360 370 380 390 400
GVKSPYSLYD QELSTFGRDE IYNQRDAEGF INLFGLPLKV RALMEKKAGL

R
Length:401
Mass (Da):44,450
Last modified:June 12, 2007 - v1
Checksum:iEDB302A0C34ED593
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009389 Genomic DNA Translation: BAF58688.1

Genome annotation databases

EnsemblBacteriaiBAF58688; BAF58688; PTH_0507
KEGGipth:PTH_0507

Similar proteinsi

Entry informationi

Entry nameiASSY_PELTS
AccessioniPrimary (citable) accession number: A5D510
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 23, 2018
This is version 68 of the entry and version 1 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health