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Protein

Argininosuccinate synthase

Gene

argG

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei34 – 341ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei85 – 851CitrullineUniRule annotation
Binding sitei115 – 1151ATP; via amide nitrogenUniRule annotation
Binding sitei117 – 1171AspartateUniRule annotation
Binding sitei121 – 1211AspartateUniRule annotation
Binding sitei121 – 1211CitrullineUniRule annotation
Binding sitei122 – 1221AspartateUniRule annotation
Binding sitei125 – 1251CitrullineUniRule annotation
Binding sitei178 – 1781CitrullineUniRule annotation
Binding sitei187 – 1871CitrullineUniRule annotation
Binding sitei268 – 2681CitrullineUniRule annotation
Binding sitei280 – 2801CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi8 – 169ATPUniRule annotation

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:TM_1780
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 409409Argininosuccinate synthasePRO_0000148656Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi243274.TM1780.

Structurei

Secondary structure

1
409
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 85Combined sources
Helixi13 – 2412Combined sources
Beta strandi28 – 3710Combined sources
Helixi42 – 5211Combined sources
Beta strandi55 – 617Combined sources
Helixi63 – 697Combined sources
Helixi71 – 755Combined sources
Turni76 – 783Combined sources
Turni82 – 843Combined sources
Helixi88 – 10720Combined sources
Beta strandi110 – 1134Combined sources
Helixi122 – 13312Combined sources
Beta strandi137 – 1404Combined sources
Helixi142 – 1443Combined sources
Helixi146 – 1516Combined sources
Helixi157 – 1659Combined sources
Beta strandi176 – 1816Combined sources
Beta strandi186 – 1905Combined sources
Helixi191 – 1944Combined sources
Helixi202 – 2043Combined sources
Turni211 – 2133Combined sources
Beta strandi219 – 2268Combined sources
Beta strandi229 – 2357Combined sources
Turni236 – 2383Combined sources
Helixi245 – 25814Combined sources
Beta strandi263 – 2697Combined sources
Beta strandi271 – 28111Combined sources
Helixi283 – 29917Combined sources
Helixi302 – 32120Combined sources
Helixi327 – 34014Combined sources
Beta strandi345 – 3528Combined sources
Beta strandi355 – 3628Combined sources
Beta strandi364 – 3663Combined sources
Helixi383 – 40422Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VL2X-ray1.65A/B/C/D1-409[»]
ProteinModelPortaliQ9X2A1.
SMRiQ9X2A1. Positions 2-409.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9X2A1.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0137.
InParanoidiQ9X2A1.
KOiK01940.
OMAiPAREWGM.
OrthoDBiEOG6K9QCV.

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: Complete.

Q9X2A1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKEKVVLAYS GGLDTSVILK WLCEKGFDVI AYVANVGQKD DFVAIKEKAL
60 70 80 90 100
KTGASKVYVE DLRREFVTDY IFTALLGNAM YEGRYLLGTA IARPLIAKRQ
110 120 130 140 150
VEIAEKEGAQ YVAHGATGKG NDQVRFELTY AALNPNLKVI SPWKDPEFLA
160 170 180 190 200
KFKGRTDLIN YAMEKGIPIK VSKKRPYSED ENLMHISHEA GKLEDPAHIP
210 220 230 240 250
DEDVFTWTVS PKDAPDEETL LEIHFENGIP VKVVNLKDGT EKTDPLELFE
260 270 280 290 300
YLNEVGAKNG VGRLDMVENR FIGIKSRGVY ETPGATILWI AHRDLEGITM
310 320 330 340 350
DKEVMHLRDM LAPKFAELIY NGFWFSPEME FLLAAFRKAQ ENVTGKVTVS
360 370 380 390 400
IYKGNVMPVA RYSPYSLYNP ELSSMDVEGG FDATDSKGFI NIHALRLKVH

QLVKKGYQR
Length:409
Mass (Da):46,054
Last modified:November 1, 1999 - v1
Checksum:iECCDC8575E962482
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36844.1.
PIRiH72210.
RefSeqiNP_229577.1. NC_000853.1.
WP_004082326.1. NC_023151.1.
YP_007978138.1. NC_021214.1.
YP_008991121.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD36844; AAD36844; TM_1780.
GeneIDi897844.
KEGGitma:TM1780.
tmi:THEMA_05300.
tmm:Tmari_1789.
PATRICi23938542. VBITheMar51294_1799.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD36844.1.
PIRiH72210.
RefSeqiNP_229577.1. NC_000853.1.
WP_004082326.1. NC_023151.1.
YP_007978138.1. NC_021214.1.
YP_008991121.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VL2X-ray1.65A/B/C/D1-409[»]
ProteinModelPortaliQ9X2A1.
SMRiQ9X2A1. Positions 2-409.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM1780.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD36844; AAD36844; TM_1780.
GeneIDi897844.
KEGGitma:TM1780.
tmi:THEMA_05300.
tmm:Tmari_1789.
PATRICi23938542. VBITheMar51294_1799.

Phylogenomic databases

eggNOGiCOG0137.
InParanoidiQ9X2A1.
KOiK01940.
OMAiPAREWGM.
OrthoDBiEOG6K9QCV.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

Miscellaneous databases

EvolutionaryTraceiQ9X2A1.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. "Crystal structure of argininosuccinate synthase (TM1780) from Thermotoga maritima at 1.65 A resolution."
    Joint center for structural genomics (JCSG)
    Submitted (MAR-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), SUBUNIT.

Entry informationi

Entry nameiASSY_THEMA
AccessioniPrimary (citable) accession number: Q9X2A1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1999
Last modified: May 27, 2015
This is version 105 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.