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Q46I72 (ASSY_PROMT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:PMN2A_1317
OrganismProchlorococcus marinus (strain NATL2A) [Complete proteome] [HAMAP]
Taxonomic identifier59920 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length400 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
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 – 400400Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000263951

Regions

Nucleotide binding10 – 189ATP By similarity

Sites

Binding site381ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site891Citrulline By similarity
Binding site1191ATP; via amide nitrogen By similarity
Binding site1211Aspartate By similarity
Binding site1251Aspartate By similarity
Binding site1251Citrulline By similarity
Binding site1261Aspartate By similarity
Binding site1291Citrulline By similarity
Binding site1771Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2621Citrulline By similarity
Binding site2741Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Q46I72 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 305D70454D2FBCBB

FASTA40044,116
        10         20         30         40         50         60 
MGKANKVVLA YSGGVDTSVC IPYLKEEYGV EHVIAFAADL GQGDELDEIK KKAISAGASQ 

        70         80         90        100        110        120 
SLIGNLVKPF IEDFAFPAIR SNALYQGRYP LSTALARPLI AKKLVEIARE LNADGVAHGC 

       130        140        150        160        170        180 
TGKGNDQVRF DVTIGALAPD LQLLTPAREW GMSREETIAY GEKYGIVPPV SKKNPYSIDL 

       190        200        210        220        230        240 
NLLGRSIEAG PLEDPFQMPS EEVFGITSSI ADSPNEPEIA DILFENGYPV AINGEEMEPV 

       250        260        270        280        290        300 
SLIKKANSLA GKHGFGRLDI IEDRVVGIKS REIYETPGLL LLIKAHQEIE SLTLPADLLD 

       310        320        330        340        350        360 
TKSRLERQWA DLVYKGFWFS PLKEALDGFI NYSQKQVNGT VRVRLFKGNV DVIGRKSKEN 

       370        380        390        400 
SLYISDMSTY GSEDKFNHKS AEGFIYVWGL PSRIWSWINK 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL2A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000095 Genomic DNA. Translation: AAZ58806.1.
RefSeqYP_292509.1. NC_007335.2.

3D structure databases

ProteinModelPortalQ46I72.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING59920.PMN2A_1317.

Proteomic databases

PRIDEQ46I72.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ58806; AAZ58806; PMN2A_1317.
GeneID3606712.
KEGGpmn:PMN2A_1317.
PATRIC23026546. VBIProMar14922_2193.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG6K9QCV.
ProtClustDBPRK00509.

Enzyme and pathway databases

BioCycPMAR59920:GI1O-2217-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_PROMT
AccessionPrimary (citable) accession number: Q46I72
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: September 13, 2005
Last modified: February 19, 2014
This is version 60 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