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Reviewed, UniProtKB/Swiss-Prot B0CCQ2 (ASSY_ACAM1)

Last modified November 3, 2009. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
Ordered Locus Names: AM1_4234
OrganismAcaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]
Taxonomic identifier329726 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Acaryochloris

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Protein attributes

Sequence length399 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 399399Argininosuccinate synthase HAMAP MF_00005
PRO_1000073810

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

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Sequences

Sequence LengthMass (Da)Tools
B0CCQ2-1 [UniParc].

Last modified February 26, 2008. Version 1.
Checksum: 27D3B5979F81A7B1

FASTA39943,644
        10         20         30         40         50         60 
MGRAKKVVLA YSGGVDTSVC IPYLKHEWGV EEVITLAADL GQGDELEPIR KKALDAGAAQ 

        70         80         90        100        110        120 
SLIADGTESF IADYAFPAIQ ANALYENRYP LSTALARPLI AKLLVEAAEI HGADAVAHGC 

       130        140        150        160        170        180 
TGKGNDQVRF DVSITALNPD IKVLAPAREW GMSREETIAY GEKYGVQSPV KKSSPYSIDR 

       190        200        210        220        230        240 
NLLGRSVEAG PLEDPWVEPL EEVYDLTKAI ADTPDQPEYV DIDFAQGLPT QLNGQALSPV 

       250        260        270        280        290        300 
ALVEQLNQIV GNHGVGRIDM VENRLVGIKS REIYEAPALL VLIQAHRELE SLALTADVTH 

       310        320        330        340        350        360 
YKRGIEETYS QLVYNGLWFS PLKDALDAFI QQTQKQVTGT VRVKLFKGAA TVVGRQSPHS 

       370        380        390 
LYTPDLATYG AEDAFDHKAA EGFIYVWGLP TRVWSQQQR

« Hide

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References

[1]"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina."
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. expand/collapse author list , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000828 Genomic DNA. Translation: ABW29214.1.
RefSeqYP_001518531.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5683037.
GenomeReviewsGene locus AM1_4234 in contig CP000828_GR.
KEGGamr:AM1_4234.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIAPVREW.

Family and domain databases

HAMAPMF_00005.
[Tree]
InterProIPR001518. Arginosuc_synth.
IPR018223. Arginosuc_synth_CS.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR11587. Arginosuc_synth. 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...

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Entry information

Entry nameASSY_ACAM1
AccessionPrimary (citable) accession number: B0CCQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 26, 2008
Last modified: November 3, 2009
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents