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Protein

Argininosuccinate lyase, chloroplastic

Gene

At5g10920

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

2-(N(omega)-L-arginino)succinate = fumarate + L-arginine.

Pathwayi: L-arginine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Argininosuccinate synthase, chloroplastic (At4g24830)
  3. Argininosuccinate lyase, chloroplastic (At5g10920)
This subpathway is part of the pathway L-arginine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-arginine from L-ornithine and carbamoyl phosphate, the pathway L-arginine biosynthesis and in Amino-acid biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Amino-acid biosynthesis, Arginine biosynthesis

Enzyme and pathway databases

BioCyciARA:AT5G10920-MONOMER.
ReactomeiR-ATH-70635. Urea cycle.
UniPathwayiUPA00068; UER00114.

Names & Taxonomyi

Protein namesi
Recommended name:
Argininosuccinate lyase, chloroplastic (EC:4.3.2.1)
Alternative name(s):
Arginosuccinase
Gene namesi
Ordered Locus Names:At5g10920
ORF Names:T30N20.190
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G10920.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545ChloroplastSequence analysisAdd
BLAST
Chaini46 – 517472Argininosuccinate lyase, chloroplasticPRO_0000423421Add
BLAST

Proteomic databases

PaxDbiQ9LEU8.
PRIDEiQ9LEU8.
ProMEXiQ9LEU8.

Expressioni

Gene expression databases

GenevisibleiQ9LEU8. AT.

Interactioni

Protein-protein interaction databases

BioGridi16237. 2 interactions.
IntActiQ9LEU8. 1 interaction.
STRINGi3702.AT5G10920.1.

Structurei

3D structure databases

ProteinModelPortaliQ9LEU8.
SMRiQ9LEU8. Positions 75-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1316. Eukaryota.
COG0165. LUCA.
HOGENOMiHOG000242744.
InParanoidiQ9LEU8.
KOiK01755.
OMAiGRGKMER.
PhylomeDBiQ9LEU8.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9LEU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGAIDLSFSQ SLLFSSSRSN LSSSTHRSVS FLPPGSKSRC LPPLRSMSHD
60 70 80 90 100
DDTASKEVKL WGGRFEESVT EKVEKFTESI SFDKVLYKQD IMGSKAHASM
110 120 130 140 150
LAHQGLITDS DKDSILRGLD DIERQIEANK FEWRTDREDV HMNIEAALTD
160 170 180 190 200
LIGEPAKKLH TARSRNDQVA TDFRLWCRDA IDTIIVKIRN LQRALVELAL
210 220 230 240 250
KNEALIVPGY THLQRAQPVL LPHVLLTFVE QLERDAGRYV DCRARLNFSP
260 270 280 290 300
LGACALAGTG LPIDRFMTAN ALGFTEPMRN SIDAVSDRDF VLEFLYTNAN
310 320 330 340 350
TGIHLSRLGE EWVLWASEEF GFMTPSDSVS TGSSIMPQKK NPDPMELVRG
360 370 380 390 400
KSARVIGDLV TVLTLCKGLP LAYNRDFQED KEPMFDSTKT IMGMIDVSAE
410 420 430 440 450
FAQNVTFNED RIKKSLPAGH LDATTLADYL VKKGMPFRSS HDIVGKLVGV
460 470 480 490 500
CVSKGCELQN LSLEEMKKLS PVFEEDVFGF LGVENSVNKF SSYGSTGSNC
510
VAEQLGYWVN KLNITST
Length:517
Mass (Da):57,512
Last modified:October 1, 2000 - v1
Checksum:iBA40F4E8109984C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411H → L in AAK76572 (PubMed:14593172).Curated
Sequence conflicti516 – 5161S → T in CAB10698 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97558 mRNA. Translation: CAB10698.1.
AL365234 Genomic DNA. Translation: CAB96847.1.
CP002688 Genomic DNA. Translation: AED91609.1.
AY045898 mRNA. Translation: AAK76572.1.
BT000891 mRNA. Translation: AAN41291.1.
PIRiT50801.
RefSeqiNP_196653.1. NM_121130.2.
UniGeneiAt.24301.

Genome annotation databases

EnsemblPlantsiAT5G10920.1; AT5G10920.1; AT5G10920.
GeneIDi830959.
GrameneiAT5G10920.1; AT5G10920.1; AT5G10920.
KEGGiath:AT5G10920.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z97558 mRNA. Translation: CAB10698.1.
AL365234 Genomic DNA. Translation: CAB96847.1.
CP002688 Genomic DNA. Translation: AED91609.1.
AY045898 mRNA. Translation: AAK76572.1.
BT000891 mRNA. Translation: AAN41291.1.
PIRiT50801.
RefSeqiNP_196653.1. NM_121130.2.
UniGeneiAt.24301.

3D structure databases

ProteinModelPortaliQ9LEU8.
SMRiQ9LEU8. Positions 75-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi16237. 2 interactions.
IntActiQ9LEU8. 1 interaction.
STRINGi3702.AT5G10920.1.

Proteomic databases

PaxDbiQ9LEU8.
PRIDEiQ9LEU8.
ProMEXiQ9LEU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G10920.1; AT5G10920.1; AT5G10920.
GeneIDi830959.
GrameneiAT5G10920.1; AT5G10920.1; AT5G10920.
KEGGiath:AT5G10920.

Organism-specific databases

TAIRiAT5G10920.

Phylogenomic databases

eggNOGiKOG1316. Eukaryota.
COG0165. LUCA.
HOGENOMiHOG000242744.
InParanoidiQ9LEU8.
KOiK01755.
OMAiGRGKMER.
PhylomeDBiQ9LEU8.

Enzyme and pathway databases

UniPathwayiUPA00068; UER00114.
BioCyciARA:AT5G10920-MONOMER.
ReactomeiR-ATH-70635. Urea cycle.

Miscellaneous databases

PROiQ9LEU8.

Gene expression databases

GenevisibleiQ9LEU8. AT.

Family and domain databases

Gene3Di1.10.275.10. 1 hit.
HAMAPiMF_00006. Arg_succ_lyase.
InterProiIPR029419. Arg_succ_lyase_C.
IPR009049. Argininosuccinate_lyase.
IPR024083. Fumarase/histidase_N.
IPR020557. Fumarate_lyase_CS.
IPR000362. Fumarate_lyase_fam.
IPR022761. Fumarate_lyase_N.
IPR008948. L-Aspartase-like.
[Graphical view]
PANTHERiPTHR11444. PTHR11444. 1 hit.
PTHR11444:SF3. PTHR11444:SF3. 1 hit.
PfamiPF14698. ASL_C2. 1 hit.
PF00206. Lyase_1. 1 hit.
[Graphical view]
PRINTSiPR00149. FUMRATELYASE.
SUPFAMiSSF48557. SSF48557. 1 hit.
TIGRFAMsiTIGR00838. argH. 1 hit.
PROSITEiPS00163. FUMARATE_LYASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a cDNA encoding argininosuccinate lyase from Arabidopsis thaliana by functional expression in yeast."
    Hansen A., Rognes S.E.
    Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Landsberg erecta.
  2. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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.
    , 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.

Entry informationi

Entry nameiARLY_ARATH
AccessioniPrimary (citable) accession number: Q9LEU8
Secondary accession number(s): O23637, Q94AP1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 18, 2013
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.