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Q9SZX3 (ASSY_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Argininosuccinate synthase, chloroplastic
EC=6.3.4.5
Alternative name(s):
Citrulline--aspartate ligase
Gene names
Ordered Locus Names:At4g24830
ORF Names:F6I7.40
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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.

Subunit structure

Homotetramer By similarity.

Subcellular location

Plastid › chloroplast Potential.

Sequence similarities

Belongs to the argininosuccinate synthase family. Type 1 subfamily.

Sequence caution

The sequence CAB41123.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB79393.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Arginine biosynthesis
   Cellular componentChloroplast
Plastid
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   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

   Cellular_componentchloroplast stroma

Inferred from direct assay PubMed 18633119PubMed 20061580. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

argininosuccinate synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q9SZX3-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7373Chloroplast Potential
Chain74 – 494421Argininosuccinate synthase, chloroplastic
PRO_0000002412

Regions

Nucleotide binding102 – 1109ATP By similarity

Sites

Binding site1291ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1811Citrulline By similarity
Binding site1861Citrulline By similarity
Binding site2111ATP; via amide nitrogen By similarity
Binding site2131Aspartate By similarity
Binding site2171Aspartate By similarity
Binding site2171Citrulline By similarity
Binding site2181Aspartate By similarity
Binding site2211Citrulline By similarity
Binding site2701Citrulline By similarity
Binding site2791Citrulline By similarity
Binding site3551Citrulline By similarity
Binding site3671Citrulline By similarity

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 25, 2005. Version 3.
Checksum: 926F8D01AF32F052

FASTA49453,846
        10         20         30         40         50         60 
MAEISATSFP SSSSSALVIR SSHNGSLKCQ NVAVPKTTSQ FQELSLKRSQ LVGNAVVTGH 

        70         80         90        100        110        120 
VTGSRSCKNQ AIRAVLSGDG TALTTDSKEA GLRGKLKKVV LAYSGGLDTS VIVPWLKENY 

       130        140        150        160        170        180 
GCEVVCFTAD VGQGIKELEG LEQKAKASGA SQLVVKDLTE EFVKDFIFPC LRAGAIYERK 

       190        200        210        220        230        240 
YLLGTSMARP VIAKAMVDVA AEVGADAVAH GCTGKGNDQV RFELTFFSLN PELKVVAPWR 

       250        260        270        280        290        300 
EWEIQGREDA IEYAKKHNVP VPVTKKSIYS RDRNLWHLSH EGDLLEDPAN EPKKDMYMMS 

       310        320        330        340        350        360 
VDPEDAPDQP EYIEIGIESG LPVALNGKAL SPATLLAELN TIGGKHGIGR IDMVENRLVG 

       370        380        390        400        410        420 
MKSRGVYETP GGTILFAAVQ ELESLTLDRE SIQVKDTLAL KYAEMVYAGR WFDPLRESMD 

       430        440        450        460        470        480 
AFMEKITETT TGSVTLKLYK GSVSVTGRQS PNSLYRQDIS SFEGSEIYNQ ADAAGFIRLY 

       490 
GLPMKIRAML KKIS

« Hide

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. expand/collapse author list , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AL049657 Genomic DNA. Translation: CAB41123.1. Sequence problems.
AL161562 Genomic DNA. Translation: CAB79393.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE84968.1.
AY065252 mRNA. Translation: AAL38728.1.
AY091319 mRNA. Translation: AAM14258.1.
IPIIPI00527702.
PIRT06667.
RefSeqNP_194214.2. NM_118616.4.
UniGeneAt.3133.

3D structure databases

ProteinModelPortalQ9SZX3.
SMRQ9SZX3. Positions 98-492.
ModBaseSearch...

Proteomic databases

PaxDbQ9SZX3.
PRIDEQ9SZX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G24830.1; AT4G24830.1; AT4G24830.
GeneID828586.
KEGGath:AT4G24830.

Organism-specific databases

TAIRAt4g24830.

Phylogenomic databases

eggNOGCOG0137.
HOGENOMHOG000230093.
InParanoidQ9SZX3.
KOK01940.
OMANDQFRFE.
PhylomeDBQ9SZX3.
ProtClustDBPLN00200.

Enzyme and pathway databases

UniPathwayUPA00068; UER00113.

Gene expression databases

ArrayExpressQ9SZX3.
GenevestigatorQ9SZX3.
GermOnlineAT4G24830. Arabidopsis thaliana.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
3.90.1260.10. 1 hit.
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_ARATH
AccessionPrimary (citable) accession number: Q9SZX3
Secondary accession number(s): Q8VZ47
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: October 25, 2005
Last modified: May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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