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Q9K4Z3 (ASSY_MORPR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase

EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
OrganismMoritella profunda
Taxonomic identifier111291 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesMoritellaceaeMoritella

Protein attributes

Sequence length404 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-citrulline + L-aspartate = AMP + diphosphate + N(omega)-(L-arginino)succinate. HAMAP-Rule MF_00005

Pathway

Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 2/3. HAMAP-Rule MF_00005

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00005

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00005.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148613

Regions

Nucleotide binding13 – 219ATP By similarity

Sites

Binding site411ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site931Citrulline By similarity
Binding site981Citrulline By similarity
Binding site1231ATP; via amide nitrogen By similarity
Binding site1251Aspartate By similarity
Binding site1291Aspartate By similarity
Binding site1291Citrulline By similarity
Binding site1301Aspartate By similarity
Binding site1331Citrulline By similarity
Binding site1821Citrulline By similarity
Binding site1911Citrulline By similarity
Binding site2671Citrulline By similarity
Binding site2791Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K4Z3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: EBE8AFBAB4E87F20

FASTA40444,291
        10         20         30         40         50         60 
MKMTQTVKKV VVAYSGGLDT SVILPWLQEN YDNCEIVAFV ADVGQGAEEL EGIEAKALAS 

        70         80         90        100        110        120 
GASECYVVDL KDELVENYIY PTLKTGAVYE GTYLLGTSMA RPIIAKAQVE IARKVGADAL 

       130        140        150        160        170        180 
CHGCTGKGND QIRFESCFAA LAPELTVIAP WRIWDLTSRE SLLEYLAERD IPTAASATKI 

       190        200        210        220        230        240 
YSRDANAWHI SHEGGELEDP WNQPSKQVWT MTVDPIDAPN EPEFLTISVV KGEITAVNGE 

       250        260        270        280        290        300 
AMSPYNTLMY LNEKAAAHGV GRVDIVENRL VGMKSRGCYE TPGGTVMVEA LRGIEELVLD 

       310        320        330        340        350        360 
KTTRKWKQTV AAEFSHLVYD GRWFTPLCAS LLAAAGTLAE EMNGEVIVKM YKGSVQAIQK 

       370        380        390        400 
KSPNSLYSEE FATFGDDNVY DQSHAEGFIR LYSLSSRIKA LASK 

« Hide

References

[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: 2674.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ252020 Genomic DNA. Translation: CAB95017.1.

3D structure databases

ProteinModelPortalQ9K4Z3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
HAMAPMF_00005. Arg_succ_synth_type1.
InterProIPR001518. 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]
PfamPF00764. Arginosuc_synth. 1 hit.
[Graphical view]
TIGRFAMsTIGR00032. argG. 1 hit.
PROSITEPS00564. ARGININOSUCCIN_SYN_1. 1 hit.
PS00565. ARGININOSUCCIN_SYN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameASSY_MORPR
AccessionPrimary (citable) accession number: Q9K4Z3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways