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
Moritella abyssi
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei40 – 401ATP; via amide nitrogen and carbonyl oxygenUniRule annotation
Binding sitei92 – 921CitrullineUniRule annotation
Binding sitei97 – 971CitrullineUniRule annotation
Binding sitei122 – 1221ATP; via amide nitrogenUniRule annotation
Binding sitei124 – 1241AspartateUniRule annotation
Binding sitei128 – 1281AspartateUniRule annotation
Binding sitei128 – 1281CitrullineUniRule annotation
Binding sitei129 – 1291AspartateUniRule annotation
Binding sitei132 – 1321CitrullineUniRule annotation
Binding sitei181 – 1811CitrullineUniRule annotation
Binding sitei190 – 1901CitrullineUniRule annotation
Binding sitei266 – 2661CitrullineUniRule annotation
Binding sitei278 – 2781CitrullineUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 199ATPUniRule annotation

GO - Molecular functioni

  1. argininosuccinate synthase activity Source: UniProtKB-HAMAP
  2. ATP binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. arginine biosynthetic process Source: UniProtKB-HAMAP
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
OrganismiMoritella abyssi
Taxonomic identifieri111292 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

Subcellular locationi

Cytoplasm 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 – 404404Argininosuccinate synthasePRO_0000148612Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ9K4Y8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

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.

Q9K4Y8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQTVKKVVV AYSGGLDTSV ILPWLQENYD NCEIVALFVA DVGQGAEELE
60 70 80 90 100
GIEAKALASG ASECYVVDLK DELVENYIYP TLKTGAVYEG TYLLGTSMAR
110 120 130 140 150
QSIAKAQVEI ARKVGADALC HGCTGKGNDQ IRFESCFAAL APELTVIAPW
160 170 180 190 200
RIWDLTSRES LLEYLAERDI PTAASGTKIY SRDANAWHIS HEGGELEDPW
210 220 230 240 250
NQPSKQVWTM TVDPIDAPNE PEFLTISVVK GEITAVNGEE MYLIIRYTYL
260 270 280 290 300
NEKAAAHGVG RVDIVENRLV GMKSRGCYET PGGTVMVEAL RGIEELVLDK
310 320 330 340 350
ITRKWKHTVA AEFSHLVYDG RWFTPLCASL LAAAGTLAEE MNGEVIVKMY
360 370 380 390 400
KGSVQAVQKQ SPNSLYSEEF ATFGDDNVYD DQSHAEGFIR LYSLSSRIKA

LASK
Length:404
Mass (Da):44,432
Last modified:October 1, 2000 - v1
Checksum:i9E1C4D037AF5923F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252021 Genomic DNA. Translation: CAB95023.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ252021 Genomic DNA. Translation: CAB95023.1.

3D structure databases

ProteinModelPortaliQ9K4Y8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00068; UER00113.

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

  1. "Evolution of arginine biosynthesis in the bacterial domain: novel gene-enzyme relationships from psychrophilic Moritella strains (Vibrionaceae) and evolutionary significance of N-alpha-acetyl ornithinase."
    Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.
    J. Bacteriol. 182:1609-1615(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 2693.

Entry informationi

Entry nameiASSY_MORAB
AccessioniPrimary (citable) accession number: Q9K4Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 68 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

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.