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Q9K4Y8 (ASSY_MORAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Argininosuccinate synthase
EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Name:argG
OrganismMoritella abyssi
Taxonomic identifier111292 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Moritellaceae › Moritella

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.

Subcellular location

Cytoplasm By similarity.

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: HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: HAMAP

argininosuccinate synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148612

Regions

Nucleotide binding11 – 199ATP By similarity

Sites

Binding site401ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site921Citrulline By similarity
Binding site971Citrulline By similarity
Binding site1221ATP; via amide nitrogen By similarity
Binding site1241Aspartate By similarity
Binding site1281Aspartate By similarity
Binding site1281Citrulline By similarity
Binding site1291Aspartate By similarity
Binding site1321Citrulline By similarity
Binding site1811Citrulline By similarity
Binding site1901Citrulline By similarity
Binding site2661Citrulline By similarity
Binding site2781Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9K4Y8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9E1C4D037AF5923F

FASTA40444,432
        10         20         30         40         50         60 
MTQTVKKVVV AYSGGLDTSV ILPWLQENYD NCEIVALFVA DVGQGAEELE GIEAKALASG 

        70         80         90        100        110        120 
ASECYVVDLK DELVENYIYP TLKTGAVYEG TYLLGTSMAR QSIAKAQVEI ARKVGADALC 

       130        140        150        160        170        180 
HGCTGKGNDQ IRFESCFAAL APELTVIAPW RIWDLTSRES LLEYLAERDI PTAASGTKIY 

       190        200        210        220        230        240 
SRDANAWHIS HEGGELEDPW NQPSKQVWTM TVDPIDAPNE PEFLTISVVK GEITAVNGEE 

       250        260        270        280        290        300 
MYLIIRYTYL NEKAAAHGVG RVDIVENRLV GMKSRGCYET PGGTVMVEAL RGIEELVLDK 

       310        320        330        340        350        360 
ITRKWKHTVA AEFSHLVYDG RWFTPLCASL LAAAGTLAEE MNGEVIVKMY KGSVQAVQKQ 

       370        380        390        400 
SPNSLYSEEF ATFGDDNVYD 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: 2693.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ252021 Genomic DNA. Translation: CAB95023.1.

3D structure databases

ProteinModelPortalQ9K4Y8.
ModBaseSearch...

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]
PANTHERPTHR11587. PTHR11587. 1 hit.
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_MORAB
AccessionPrimary (citable) accession number: Q9K4Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 25, 2003
Last sequence update: October 1, 2000
Last modified: April 3, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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