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Q9KNT8 (ASSY_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. 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
Ordered Locus Names:VC_2642
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine biosynthetic process

Inferred from sequence or structural similarity Ref.1. Source: TIGR

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

argininosuccinate synthase activity

Inferred from sequence or structural similarity Ref.1. Source: TIGR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 404404Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148660

Regions

Nucleotide binding12 – 209ATP By similarity

Sites

Binding site391ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site911Citrulline By similarity
Binding site961Citrulline By similarity
Binding site1211ATP; via amide nitrogen By similarity
Binding site1231Aspartate By similarity
Binding site1271Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1281Aspartate By similarity
Binding site1311Citrulline By similarity
Binding site1801Citrulline By similarity
Binding site1891Citrulline By similarity
Binding site2651Citrulline By similarity
Binding site2771Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KNT8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: A65C73B442B5AF82

FASTA40444,465
        10         20         30         40         50         60 
MSKVQVKKVV VAYSGGLDTS VIIPWLKENY DCEVVAFVAD VGQGDEELKG VEAKALSSGA 

        70         80         90        100        110        120 
SECYIVDLKE EFVKEYIYPT LKTGAYYEGK YLLGTSMARP VIAKAQVEIA RKVGADALAH 

       130        140        150        160        170        180 
GCTGKGNDQV RFEGAFAALA PDLHVIAPWR EWDLRSREAC LDYLAERNIP CAASLTKIYS 

       190        200        210        220        230        240 
RDANAWHVST EGGVLESTWN APNEDCWVWT VDPEQAPNEA EYVTLQVAHG EVVAVDGEAM 

       250        260        270        280        290        300 
TPYNALLYLN QKGAKHGVGR IDIVENRLVG MKSRGCYETP GGTIIMEALR AVEQLVLDKT 

       310        320        330        340        350        360 
SFEFREELGI KASHLVYDGR WFTPLRQAVF AAADELAKDV NGEVVIKLYK GQAVATQKRS 

       370        380        390        400 
ANSLYSEDFA TFGADEVYDH SHAGGFIRLY SLSSRIRALS QNKQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF95783.1.
PIRA82052.
RefSeqNP_232270.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KNT8.
SMRQ9KNT8. Positions 8-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC2642.

Protocols and materials databases

DNASU2615659.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF95783; AAF95783; VC_2642.
GeneID2615659.
KEGGvch:VC2642.
PATRIC20084308. VBIVibCho83274_2520.

Phylogenomic databases

eggNOGCOG0137.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycVCHO:VC2642-MONOMER.
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_VIBCH
AccessionPrimary (citable) accession number: Q9KNT8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 81 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