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Protein

Argininosuccinate synthase

Gene

argG

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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. Ornithine carbamoyltransferase (argF)
  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 sitei43ATP; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei99CitrullineUniRule annotation1
Binding sitei129ATP; via amide nitrogenUniRule annotation1
Binding sitei131AspartateUniRule annotation1
Binding sitei131ATPUniRule annotation1
Binding sitei135AspartateUniRule annotation1
Binding sitei135CitrullineUniRule annotation1
Binding sitei136AspartateUniRule annotation1
Binding sitei136ATPUniRule annotation1
Binding sitei139CitrullineUniRule annotation1
Binding sitei192CitrullineUniRule annotation1
Binding sitei194ATPUniRule annotation1
Binding sitei201CitrullineUniRule annotation1
Binding sitei203CitrullineUniRule annotation1
Binding sitei280CitrullineUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi17 – 25ATPUniRule 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:BP3537
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000002676 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001486921 – 445Argininosuccinate synthaseAdd BLAST445

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

STRINGi257313.BP3537.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 17Combined sources6
Helixi22 – 33Combined sources12
Beta strandi37 – 44Combined sources8
Helixi55 – 62Combined sources8
Beta strandi66 – 72Combined sources7
Helixi74 – 86Combined sources13
Beta strandi92 – 94Combined sources3
Beta strandi97 – 99Combined sources3
Helixi102 – 120Combined sources19
Beta strandi125 – 127Combined sources3
Helixi136 – 147Combined sources12
Beta strandi152 – 154Combined sources3
Helixi156 – 158Combined sources3
Helixi160 – 165Combined sources6
Helixi169 – 178Combined sources10
Beta strandi190 – 195Combined sources6
Beta strandi200 – 204Combined sources5
Helixi205 – 208Combined sources4
Helixi214 – 216Combined sources3
Beta strandi220 – 222Combined sources3
Beta strandi235 – 242Combined sources8
Beta strandi245 – 249Combined sources5
Helixi257 – 269Combined sources13
Turni270 – 274Combined sources5
Beta strandi276 – 281Combined sources6
Beta strandi287 – 293Combined sources7
Helixi295 – 311Combined sources17
Helixi314 – 333Combined sources20
Helixi339 – 351Combined sources13
Helixi353 – 355Combined sources3
Beta strandi358 – 364Combined sources7
Beta strandi370 – 376Combined sources7
Helixi384 – 387Combined sources4
Turni392 – 394Combined sources3
Helixi399 – 407Combined sources9
Helixi410 – 425Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5US8X-ray2.15A/B1-445[»]
ProteinModelPortaliQ7VTJ9.
SMRiQ7VTJ9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the argininosuccinate synthase family. Type 2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105CDH. Bacteria.
COG0137. LUCA.
HOGENOMiHOG000230094.
KOiK01940.
OMAiGVGRIDM.

Family and domain databases

Gene3Di1.10.287.400. 1 hit.
3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPiMF_00581. Arg_succ_synth_type2. 1 hit.
InterProiView protein in InterPro
IPR023437. Arg_succ_synth_type2_subfam.
IPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR024074. AS_cat/multimer_dom_body.
IPR024073. AS_multimer_C_tail.
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.

Q7VTJ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTILPNLPT GQKVGIAFSG GLDTSAALLW MRQKGAVPYA YTANLGQPDE
60 70 80 90 100
PDYDEIPRRA MQYGAEAARL VDCRAQLVAE GIAALQAGAF HISTAGLTYF
110 120 130 140 150
NTTPIGRAVT GTMLVAAMKE DGVNIWGDGS TFKGNDIERF YRYGLLTNPD
160 170 180 190 200
LKIYKPWLDQ TFIDELGGRA EMSEYMRQAG FDYKMSAEKA YSTDSNMLGA
210 220 230 240 250
THEAKDLELL SAGIRIVQPI MGVAFWQDSV QIKAEEVTVR FEEGQPVALN
260 270 280 290 300
GVEYADPVEL LLEANRIGGR HGLGMSDQIE NRIIEAKSRG IYEAPGLALL
310 320 330 340 350
FIAYERLVTG IHNEDTIEQY RENGRKLGRL LYQGRWFDPQ AIMLRETAQR
360 370 380 390 400
WVARAITGEV TLELRRGNDY SLLNTESANL TYAPERLSME KVENAPFTPA
410 420 430 440
DRIGQLTMRN LDIVDTREKL FTYVKTGLLA PSAGSALPQI KDGKK
Length:445
Mass (Da):49,323
Last modified:October 1, 2003 - v1
Checksum:i81278F1EBC07CE61
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640421 Genomic DNA. Translation: CAE43796.1.
RefSeqiNP_882052.1. NC_002929.2.
WP_003820367.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE43796; CAE43796; BP3537.
GeneIDi2664934.
KEGGibpe:BP3537.
PATRICifig|257313.5.peg.3829.

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.

Entry informationi

Entry nameiASSY_BORPE
AccessioniPrimary (citable) accession number: Q7VTJ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: October 1, 2003
Last modified: June 7, 2017
This is version 87 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families