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Reviewed, UniProtKB/Swiss-Prot Q7PR38 (ASSY_ANOGA)

Last modified June 16, 2009. Version 43. 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
ORF Names: AGAP003015
OrganismAnopheles gambiae (African malaria mosquito) [Complete proteome]
Taxonomic identifier7165 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles

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Protein attributes

Sequence length424 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.

Pathway

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

Nitrogen metabolism; urea cycle; N(omega)-(L-arginino)succinic acid from L-aspartate and L-citrulline: step 1/1.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the argininosuccinate synthase family.

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Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
Urea cycle
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processarginine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

urea cycle

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 424424Argininosuccinate synthase
PRO_0000321327

Regions

Nucleotide binding9 – 179ATP By similarity
Nucleotide binding114 – 1229ATP By similarity

Sites

Binding site351ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site861Citrulline By similarity
Binding site911Citrulline By similarity
Binding site1181Aspartate By similarity
Binding site1221Aspartate By similarity
Binding site1221Citrulline By similarity
Binding site1231Aspartate By similarity
Binding site1261Citrulline By similarity
Binding site1791Citrulline By similarity
Binding site1881Citrulline By similarity
Binding site2691Citrulline By similarity
Binding site2811Citrulline By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q7PR38-1 [UniParc].

Last modified January 9, 2007. Version 3.
Checksum: 133485FD4A9CC4B3

FASTA42447,807
        10         20         30         40         50         60 
MSKEKVLLAY SGGLDTSCIL KWLLEQDYEV ICFMADVGQT EDFAAAREKA LKIGAADVVV 

        70         80         90        100        110        120 
KDMKDFFVEK FVWPAVQMGL IYEDRYLLGT SLARPCISKG LMDVAVQRGC SYISHGATGK 

       130        140        150        160        170        180 
GNDQIRFELS CYALSPTIRV IAPWRMETFC QRFQGRSDLL EYAKRSNIPV SATTKAPWSM 

       190        200        210        220        230        240 
DANIMHISYE SGILEDPSVA APEELYQLTQ SPTRAPDTPT VAEIVFKAGL PVRVTELVSG 

       250        260        270        280        290        300 
RTMERPVDIL AFLNKAGGEH GVGRIDIVEN RYIGLKSRGV YETPGVTVLH CAHRDLEIYC 

       310        320        330        340        350        360 
LDREVLRVKK YLADRMADYV YNGYWYAPEA EYVRKCILES QKHVSGKVVV EMFKGHVMVT 

       370        380        390        400        410        420 
SRESMHSLYN QELASMEVHG NFSPYSSTGF IEINAVRLRE HHRVFGTANM TKHFSRTESD 


MKLI

« Hide

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References

[1]"The genome sequence of the malaria mosquito Anopheles gambiae."
Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R., Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R., Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z., Kraft C.L., Abril J.F. expand/collapse author list , Anthouard V., Arensburger P., Atkinson P.W., Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C., Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K., Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V., Dana A., Delcher A., Dew I., Evans C.A., Flanigan M., Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R., Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J., Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I., Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A., McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D., O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H., Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J., Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B., Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M., Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I., Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J., Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M., Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C., Collins F.H., Hoffman S.L.
Science 298:129-149(2002) [PubMed: 12364791] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PEST.

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Cross-references

Sequence databases

AAAB01008859 Genomic DNA. Translation: EAA07894.4.
RefSeqXP_311863.3.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1272938.
KEGGaga:AgaP_AGAP003015.
VectorBaseAGAP003015. Anopheles gambiae.

Phylogenomic databases

OMAQ7PR38. IAPVREW.

Enzyme and pathway databases

BRENDA6.3.4.5. 165157.

Family and domain databases

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_ANOGA
AccessionPrimary (citable) accession number: Q7PR38
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 9, 2007
Last modified: June 16, 2009
This is version 43 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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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