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Q9SMZ4 (AASS_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-aminoadipic semialdehyde synthase
Alternative name(s):
cAt-LKR/SDH
Short name=LKR/SDH

Including the following 2 domains:

  1. Lysine ketoglutarate reductase
    Short name=LKR
    EC=1.5.1.8
  2. Saccharopine dehydrogenase
    EC=1.5.1.9
    Alternative name(s):
    cAt-SDH
    Short name=SDH
Gene names
Name:LKR/SDH
Synonyms:LKR, SDH
Ordered Locus Names:At4g33150
ORF Names:F4I10.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length1064 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the first two steps in lysine degradation. The N-terminal and the C-terminal contain lysine-oxoglutarate reductase and saccharopine dehydrogenase activity, respectively. Negatively regulates free Lys accumulation in seeds. Ref.1 Ref.2 Ref.9

Catalytic activity

N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP+ + H2O = L-lysine + 2-oxoglutarate + NADPH.

N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD+ + H2O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADH.

Enzyme regulation

The LKR activity is stimulated by NaCl. Ref.10

Pathway

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 1/6.

Amino-acid degradation; L-lysine degradation via saccharopine pathway; glutaryl-CoA from L-lysine: step 2/6.

Subunit structure

Homodimer. Ref.10

Subcellular location

Cytoplasm Ref.8.

Tissue specificity

Ubiquitous, with higher levels in flowers. Isoform Long is mostly present in young leaves, cotyledons, root tips and mature root parts. Whereas isoform Short is mostly expressed in cotyledons and at low levels in all root parts. Ref.1 Ref.12

Developmental stage

In flowers, confined to ovules and vascular tissue of anther filament. In developing and mature seeds, expressed in embryo and the outer layers of the endosperm. Ref.1

Induction

Lysine, Sugar starvation, ABA and MeJA induce isoform Long, but not isoform Short (at protein level). Nitrogen starvation repress isoform Long, but not isoform Short (at protein level). Isoform Long and isoform Short are both slightly induced by NaCl and drought stress, but repressed by sugars. Ref.10 Ref.11 Ref.12

Post-translational modification

Phosphorylation of Ser-458 seems important for the LKR activity.

Sequence similarities

In the N-terminal section; belongs to the AlaDH/PNT family.

In the C-terminal section; belongs to the saccharopine dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=5.180 mM for lysine (isoform Long at pH 7.5 and 30 degrees Celsius) Ref.8

KM=0.272 mM for alpha-ketoglutarate (isoform Long at pH 7.5 and 30 degrees Celsius)

KM=0.044 mM for NADPH (isoform Long at pH 7.5 and 30 degrees Celsius)

KM=0.063 mM for saccharopine (isoform Long at pH 7 and 30 degrees Celsius)

KM=0.035 mM for saccharopine (isoform Long at pH 9 and 30 degrees Celsius)

KM=0.130 mM for saccharopine (isoform Short at pH 7 and 30 degrees Celsius)

KM=0.050 mM for saccharopine (isoform Short at pH 9 and 30 degrees Celsius)

KM=0.374 mM for NAD (isoform Long at pH 7 and 30 degrees Celsius)

KM=0.698 mM for NAD (isoform Long at pH 9 and 30 degrees Celsius)

KM=0.333 mM for NAD (isoform Short at pH 7 and 30 degrees Celsius)

KM=0.759 mM for NAD (isoform Short at pH 9 and 30 degrees Celsius)

pH dependence:

Optimum pH is 7.5 for LKR activity of isoform Long, and 9 for SDH activity of both isoforms Long and Short.

Sequence caution

The sequence AAK64010.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK97099.1 differs from that shown. Reason: Chimeric cDNA. Its C-terminal part is derived from gene At1G61240, which coded for a protein of unknown function. Was originally thought to be an alternative splicing form of At4g33150.

The sequence AAM16268.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative initiation
   LigandNAD
NADP
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processL-lysine catabolic process to acetyl-CoA via saccharopine

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsaccharopine dehydrogenase (NAD+, L-glutamate-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

saccharopine dehydrogenase (NADP+, L-lysine-forming) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]
Isoform Long (identifier: Q9SMZ4-1)

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.
Note: Contains both LKR and SDH activities.
Isoform Short (identifier: Q9SMZ4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-582: Missing.
Note: Contains only SDH activity.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10641064Alpha-aminoadipic semialdehyde synthase
PRO_0000226070

Regions

Region24 – 445422Lysine-ketoglutarate reductase
Region583 – 1064482Saccharopine dehydrogenase

Amino acid modifications

Modified residue2381Phosphothreonine Ref.10
Modified residue4581Phosphoserine Ref.10

Natural variations

Alternative sequence1 – 582582Missing in isoform Short.
VSP_018641

Experimental info

Mutagenesis2381T → A or D: No effect on LKR and SDH activity. Ref.10
Mutagenesis4071S → A: No effect on LKR and SDH activity. Ref.10
Mutagenesis4071S → D: No LKR activity, but no effect on SDH activity. Ref.10
Mutagenesis4581S → A: Reduced LKR activity, but no effect on SDH activity. Ref.10
Mutagenesis4581S → D: No effect on LKR and SDH activity. Ref.10
Mutagenesis551 – 5544NEDY → IEGR: Loss of LKR activity stimulation by NaCl. Ref.10
Sequence conflict167 – 1693KLI → YLS in AAB53975. Ref.1
Sequence conflict167 – 1693KLI → YLS in AAB96825. Ref.2
Sequence conflict167 – 1693KLI → YLS in AAB96826. Ref.2
Sequence conflict167 – 1693KLI → YLS in AAK97099. Ref.3
Sequence conflict3241R → S in AAB53975. Ref.1
Sequence conflict3241R → S in AAK97099. Ref.3
Sequence conflict6211F → V in AAK64010. Ref.6
Sequence conflict6211F → V in AAM16268. Ref.6
Sequence conflict7151K → N in AAB53975. Ref.1
Sequence conflict7151K → N in AAD00700. Ref.1
Sequence conflict7351H → P in AAB53975. Ref.1
Sequence conflict7351H → P in AAD00700. Ref.1
Sequence conflict7391M → K in AAB53975. Ref.1
Sequence conflict7391M → K in AAD00700. Ref.1
Sequence conflict746 – 7483HIK → PIT in AAB53975. Ref.1
Sequence conflict746 – 7483HIK → PIT in AAD00700. Ref.1
Sequence conflict7651P → R in AAB53975. Ref.1
Sequence conflict7651P → R in AAD00700. Ref.1
Sequence conflict8271F → L in AAB96825. Ref.2
Sequence conflict8271F → L in AAB96826. Ref.2
Sequence conflict10401L → F in AAB96825. Ref.2

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 6CA4EBDB22898C7E

FASTA1,064117,149
        10         20         30         40         50         60 
MNSNGHEEEK KLGNGVVGIL AETVNKWERR TPLTPSHCAR LLHGGKDRTG ISRIVVQPSA 

        70         80         90        100        110        120 
KRIHHDALYE DVGCEISDDL SDCGLILGIK QPELEMILPE RAYAFFSHTH KAQKENMPLL 

       130        140        150        160        170        180 
DKILSERVTL CDYELIVGDH GKRLLAFGKY AGRAGLVDFL HGLGQRKLIL GYSTPFLSLG 

       190        200        210        220        230        240 
ASYMYSSLAA AKAAVISVGE EIASQGLPLG ICPLVFVFTG TGNVSLGAQE IFKLLPHTFV 

       250        260        270        280        290        300 
EPSKLPELFV KDKGISQNGI STKRVYQVYG CIITSQDMVE HKDPSKSFDK ADYYAHPEHY 

       310        320        330        340        350        360 
NPVFHEKISP YTSVLVNCMY WEKRFPCLLS TKQLQDLTKK GLPLVGICDI TCDIGGSIEF 

       370        380        390        400        410        420 
VNRATLIDSP FFRFNPSNNS YYDDMDGDGV LCMAVDILPT EFAKEASQHF GDILSGFVGS 

       430        440        450        460        470        480 
LASMTEISDL PAHLKRACIS YRGELTSLYE YIPRMRKSNP EEAQDNIIAN GVSSQRTFNI 

       490        500        510        520        530        540 
LVSLSGHLFD KFLINEALDM IEAAGGSFHL AKCELGQSAD AESYSELEVG ADDKRVLDQI 

       550        560        570        580        590        600 
IDSLTRLANP NEDYISPHRE ANKISLKIGK VQQENEIKEK PEMTKKSGVL ILGAGRVCRP 

       610        620        630        640        650        660 
AADFLASVRT ISSQQWYKTY FGADSEEKTD VHVIVASLYL KDAKETVEGI SDVEAVRLDV 

       670        680        690        700        710        720 
SDSESLLKYV SQVDVVLSLL PASCHAVVAK TCIELKKHLV TASYVDDETS MLHEKAKSAG 

       730        740        750        760        770        780 
ITILGEMGLD PGIDHMMAMK MINDAHIKKG KVKSFTSYCG GLPSPAAANN PLAYKFSWNP 

       790        800        810        820        830        840 
AGAIRAGQNP AKYKSNGDII HVDGKNLYDS AARFRVPNLP AFALECFPNR DSLVYGEHYG 

       850        860        870        880        890        900 
IESEATTIFR GTLRYEGFSM IMATLSKLGF FDSEANQVLS TGKRITFGAL LSNILNKDAD 

       910        920        930        940        950        960 
NESEPLAGEE EISKRIIKLG HSKETAAKAA KTIVFLGFNE EREVPSLCKS VFDATCYLME 

       970        980        990       1000       1010       1020 
EKLAYSGNEQ DMVLLHHEVE VEFLESKRIE KHTATLLEFG DIKNGQTTTA MAKTVGIPAA 

      1030       1040       1050       1060 
IGALLLIEDK IKTRGVLRPL EAEVYLPALD ILQAYGIKLM EKAE 

« Hide

Isoform Short [UniParc].

Checksum: A249E25010D557A3
Show »

FASTA48252,704

References

« Hide 'large scale' references
[1]"Regulation of lysine catabolism through lysine-ketoglutarate reductase and saccharopine dehydrogenase in Arabidopsis."
Tang G., Miron D., Zhu-Shimoni J.X., Galili G.
Plant Cell 9:1305-1316(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: cv. Columbia.
Tissue: Seedling hypocotyl.
[2]"Lysine-ketoglutarate reductase and saccharopine dehydrogenase from Arabidopsis thaliana: nucleotide sequence and characterization."
Epelbaum S., McDevitt R., Falco S.C.
Plant Mol. Biol. 35:735-748(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), FUNCTION.
Strain: cv. Columbia and cv. Landsberg erecta.
[3]"The bifunctional LKR/SDH locus of plants also encodes a highly active monofunctional lysine-ketoglutarate reductase using a polyadenylation signal located within an intron."
Tang G., Zhu X., Gakiere B., Levanony H., Kahana A., Galili G.
Plant Physiol. 130:147-154(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"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.
[5]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[6]"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] OF 529-1064 (ISOFORM LONG).
Strain: cv. Columbia.
[7]"A novel composite locus of Arabidopsis encoding two polypeptides with metabolically related but distinct functions in lysine catabolism."
Tang G., Zhu X., Tang X., Galili G.
Plant J. 23:195-203(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE INITIATION.
[8]"Characterization of the two saccharopine dehydrogenase isozymes of lysine catabolism encoded by the single composite AtLKR/SDH locus of Arabidopsis."
Zhu X., Tang G., Galili G.
Plant Physiol. 124:1363-1371(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"A T-DNA insertion knockout of the bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase gene elevates lysine levels in Arabidopsis seeds."
Zhu X., Tang G., Granier F., Bouchez D., Galili G.
Plant Physiol. 126:1539-1545(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"The activity of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is regulated by functional interaction between its two enzyme domains."
Zhu X., Tang G., Galili G.
J. Biol. Chem. 277:49655-49661(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, SUBUNIT, PHOSPHORYLATION AT THR-238 AND SER-458, MUTAGENESIS OF THR-238; SER-407; SER-458 AND 551-ASN--ARG-554.
[11]"Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals."
Stepansky A., Galili G.
Plant Physiol. 133:1407-1415(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"Regulation of lysine catabolism in Arabidopsis through concertedly regulated synthesis of the two distinct gene products of the composite AtLKR/SDH locus."
Stepansky A., Yao Y., Tang G., Galili G.
J. Exp. Bot. 56:525-536(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U90522 mRNA. Translation: AAB53975.1.
U90523 mRNA. Translation: AAD00700.1.
U95758 Genomic DNA. Translation: AAB96825.1.
U95759 mRNA. Translation: AAB96826.1.
AF295389 mRNA. Translation: AAK97099.1. Sequence problems.
AL035525 Genomic DNA. Translation: CAB36789.1.
AL161583 Genomic DNA. Translation: CAB80032.1.
CP002687 Genomic DNA. Translation: AEE86184.1.
AY039906 mRNA. Translation: AAK64010.1. Different initiation.
AY094007 mRNA. Translation: AAM16268.1. Different initiation.
PIRT05195.
RefSeqNP_001154283.1. NM_001160811.1. [Q9SMZ4-2]
UniGeneAt.20921.

3D structure databases

ProteinModelPortalQ9SMZ4.
SMRQ9SMZ4. Positions 214-239, 589-1062.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ9SMZ4.
PRIDEQ9SMZ4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G33150.1; AT4G33150.1; AT4G33150.
AT4G33150.2; AT4G33150.2; AT4G33150.
GeneID829452.
KEGGath:AT4G33150.

Organism-specific databases

TAIRAT4G33150.

Phylogenomic databases

eggNOGCOG1748.
InParanoidQ9SMZ4.
PhylomeDBQ9SMZ4.

Enzyme and pathway databases

BioCycARA:AT4G33150-MONOMER.
ARA:GQT-806-MONOMER.
ARA:GQT-807-MONOMER.
UniPathwayUPA00868; UER00835.
UPA00868; UER00836.

Gene expression databases

ArrayExpressQ9SMZ4.
GenevestigatorQ9SMZ4.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR007886. AlaDH/PNT_N.
IPR007698. AlaDH/PNT_NAD(H)-bd.
IPR007545. LOR/SDH_bifunc_enz_cons_dom.
IPR016040. NAD(P)-bd_dom.
IPR005097. Saccharopine_DH/HSpermid_syn.
[Graphical view]
PfamPF01262. AlaDh_PNT_C. 1 hit.
PF05222. AlaDh_PNT_N. 1 hit.
PF03435. Saccharop_dh. 1 hit.
PF04455. Saccharop_dh_N. 1 hit.
[Graphical view]
SMARTSM01002. AlaDh_PNT_C. 1 hit.
SM01003. AlaDh_PNT_N. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAASS_ARATH
AccessionPrimary (citable) accession number: Q9SMZ4
Secondary accession number(s): O04155 expand/collapse secondary AC list , O04156, O04884, Q7DM71, Q947M5, Q94BT4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: May 1, 2000
Last modified: June 11, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names