Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0QHA8 (ASSY_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 44. 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
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:MAV_3112
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) ›

Protein attributes

Sequence length398 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
   Technical termComplete proteome
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 – 398398Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_1000000406

Regions

Nucleotide binding8 – 169ATP By similarity

Sites

Binding site871Citrulline By similarity
Binding site1171ATP; via amide nitrogen By similarity
Binding site1191Aspartate By similarity
Binding site1231Aspartate By similarity
Binding site1231Citrulline By similarity
Binding site1241Aspartate By similarity
Binding site1271Citrulline By similarity
Binding site1751Citrulline By similarity
Binding site2601Citrulline By similarity
Binding site2721Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QHA8 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 815A2952E4C8F2A2

FASTA39843,780
        10         20         30         40         50         60 
MSERVILAYS GGLDTSVAIS WIGKETGREV VAVAIDLGQG GEDMEVIRQR ALDCGAVEAV 

        70         80         90        100        110        120 
VVDARDEFAE GYCLPTIRNN ALYMDRYPLV SAISRPLIVK HLVAAAREHG GSIVAHGCTG 

       130        140        150        160        170        180 
KGNDQVRFEV GFASLAPDLE VLAPVRDYAW TREKAIAFAE ENAIPINVTK RSPFSIDQNV 

       190        200        210        220        230        240 
WGRAVETGFL EHLWNAPTKD VYAYTEDPTL NWSTPDEVIV GFERGVPVSI DGKPVSVLGA 

       250        260        270        280        290        300 
IEELNARAGA QGVGRLDVVE DRLVGIKSRE IYEAPGAMVL ITAHTELEHV TLERELGRFK 

       310        320        330        340        350        360 
RHTDQRWAEL VYDGLWYSPL KAALESFVDK TQEHVTGEIR MVLHGGHIAV NGRRSAESLY 

       370        380        390 
DFNLATYDEG DSFDQSAAKG FVYVHGLSSK IASRRDQR

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000479 Genomic DNA. Translation: ABK67697.1.
RefSeqYP_882296.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QHA8.
ModBaseSearch...

Protein-protein interaction databases

STRING243243.MAV_3112.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK67697; ABK67697; MAV_3112.
GeneID4528930.
KEGGmav:MAV_3112.
PATRIC17987915. VBIMycAvi38287_3043.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMANDQFRFE.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycMAVI243243:GH3Y-3127-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]
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_MYCA1
AccessionPrimary (citable) accession number: A0QHA8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: May 1, 2013
This is version 44 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents