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O97069 (ASSY_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
ORF Names:CG1315
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-UniPathway

urea cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Argininosuccinate synthase HAMAP-Rule MF_00005
PRO_0000148557

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 site2701Citrulline By similarity
Binding site2821Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
O97069 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 0566A10A329BE513

FASTA41946,595
        10         20         30         40         50         60 
MPKETVILAY SGGLDTSCVL KWLLDKQYEV ICVLADVGQK EDFTAAEKKA LKIGAKKVIV 

        70         80         90        100        110        120 
ADVKQSFVED YIWPAVQMGL VYEERYLLGT SLARPCISVA LMEVAREYGA KYLAHGATGK 

       130        140        150        160        170        180 
GNDQVRFELC AYALKPDLKI IAPWRDVEFC CQFQGRQDLI AYAQQHGIEV SAKPATPWST 

       190        200        210        220        230        240 
DANILHISYE SGILEDPNTV APENLYEMTV DPLTRAPRDP VHLVIQFDRG LPSSVEDLPG 

       250        260        270        280        290        300 
GRVYTKPLEM LDFLNKLGGS YGIGRIDIVE NRFVGLKSRG VYETPGGTIL FAAHQDLEVF 

       310        320        330        340        350        360 
ALDREVLRTK QVLRDRMADY VYNGFWFSPE AIYARKCIEL AEQRVSGKVT VELAPGYCRA 

       370        380        390        400        410 
IARKAAKDVG ALYNEQLVSM DVHGGYVPQD AGGFIAINAV RIREHVRAFG AYDVPTKKN 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence of the Antennapedia complex of Drosophila."
Celniker S.E., Pfeiffer B., Knafels J., Martin C.H., Mayeda C.A., Palazzolo M.J.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Berkeley.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]Carlson J.W., Booth B., Frise E., Sandler J., Wan K.H., Yu C., Celniker S.E.
Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE001572 Genomic DNA. Translation: AAD19816.1.
AE014297 Genomic DNA. Translation: AAF54103.2.
BT060440 mRNA. Translation: ACN22205.1.
RefSeqNP_001262324.1. NM_001275395.1.
NP_649674.1. NM_141417.3.
UniGeneDm.20149.

3D structure databases

ProteinModelPortalO97069.
SMRO97069. Positions 3-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66010. 1 interaction.
DIPDIP-21101N.
IntActO97069. 1 interaction.
MINTMINT-958605.
STRING7227.FBpp0081197.

Proteomic databases

PRIDEO97069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081699; FBpp0081197; FBgn0026565.
GeneID40812.
KEGGdme:Dmel_CG1315.

Organism-specific databases

FlyBaseFBgn0026565. CG1315.

Phylogenomic databases

eggNOGCOG0137.
GeneTreeENSGT00390000004524.
InParanoidO97069.
KOK01940.
OMAIYNGYWW.
OrthoDBEOG7PVWPB.
PhylomeDBO97069.

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.
UPA00158; UER00272.

Gene expression databases

BgeeO97069.

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...

Other

GenomeRNAi40812.
NextBio820710.
PROO97069.

Entry information

Entry nameASSY_DROME
AccessionPrimary (citable) accession number: O97069
Secondary accession number(s): C0HDN4, Q9VI41
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: February 19, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase