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O81852

- AKH2_ARATH

UniProt

O81852 - AKH2_ARATH

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Protein

Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic

Gene

AKHSDH2

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

Functioni

Catalytic activityi

L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H.
ATP + L-aspartate = ADP + 4-phospho-L-aspartate.

Enzyme regulationi

Threonine interaction with Gln-443 leads to inhibition of aspartate kinase activity and facilitates the binding of a second threonine on Gln-524, leading to a partial inhibition of homoserine dehydrogenase activity (25% of activity remaining at saturation with threonine). Homoserine dehydrogenase activity is also partially inhibited by cysteine (15% of activity remaining at saturation with cysteine). No synergy between threonine and cysteine for the inhibition. 13-fold activation of aspartate kinase activity by cysteine, isoleucine, valine, serine and alanine at 2.5 mM and 4-fold activation by leucine at 2.5 mM, but no activation of homoserine dehydrogenase activity.2 Publications

Kineticsi

  1. KM=11.6 mM for aspartate for the aspartokinase activity (in the presence of 40 mM ATP)2 Publications
  2. KM=6.15 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH and 20 mM ATP)2 Publications
  3. KM=1.5 mM for aspartate for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH, 20 mM ATP and a saturating concentration of alanine)2 Publications
  4. KM=26.4 mM for aspartate for the aspartokinase activity (in the presence of 100 mM ATP and 0.5 mM threonine)2 Publications
  5. KM=5.5 mM for ATP for the aspartokinase activity (in the presence of 50 mM aspartate)2 Publications
  6. KM=2.2 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH and 50 mM aspartate)2 Publications
  7. KM=0.42 mM for ATP for the aspartokinase activity (at pH 8.0, in the presence of 200 µM NADPH, 50 mM aspartate and a saturating concentration of alanine)2 Publications
  8. KM=5.2 mM for homoserine for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 1 mM NADP)2 Publications
  9. KM=1.4 mM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (in the presence of NADPH)2 Publications
  10. KM=311 µM for aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity (at pH 8.0, in the presence of 150 mM KCl and 200 µM NADPH)2 Publications
  11. KM=24.5 mM for homoserine for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 1 mM NADP and 60 mM threonine)2 Publications
  12. KM=166.1 µM for NADP for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 50 mM homoserine)2 Publications
  13. KM=676.1 µM for NADP for the reverse reaction of the homoserine dehydrogenase activity (in the presence of 100 mM homoserine and 60 mM threonine)2 Publications

Vmax=5.4 µmol/min/mg enzyme toward aspartylhydroxamate for the aspartokinase activity2 Publications

Vmax=165 µmol/min/mg enzyme toward aspartate semialdehyde for the forward reaction of the homoserine dehydrogenase activity2 Publications

Vmax=18.8 µmol/min/mg enzyme toward NADPH for the reverse reaction of the homoserine dehydrogenase activity2 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi564 – 5696NADPSequence Analysis

GO - Molecular functioni

  1. amino acid binding Source: InterPro
  2. aspartate kinase activity Source: TAIR
  3. ATP binding Source: UniProtKB-KW
  4. homoserine dehydrogenase activity Source: TAIR
  5. NADP binding Source: InterPro

GO - Biological processi

  1. lysine biosynthetic process via diaminopimelate Source: UniProtKB-UniPathway
  2. methionine biosynthetic process Source: UniProtKB-KW
  3. threonine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Methionine biosynthesis

Keywords - Ligandi

ATP-binding, NADP, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:GQT-2291-MONOMER.
BRENDAi1.1.1.3. 399.
SABIO-RKO81852.
UniPathwayiUPA00034; UER00015.
UPA00050; UER00063.
UPA00050; UER00461.
UPA00051; UER00462.
UPA00051; UER00465.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
Short name:
AK-HD 2
Short name:
AK-HSDH 2
Alternative name(s):
Beta-aspartyl phosphate homoserine 2
Including the following 2 domains:
Aspartokinase (EC:2.7.2.4)
Homoserine dehydrogenase (EC:1.1.1.3)
Gene namesi
Name:AKHSDH2
Synonyms:AK-HSDH II
Ordered Locus Names:At4g19710
ORF Names:T16H5.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G19710.

Subcellular locationi

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast stroma Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi441 – 4411I → A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
Mutagenesisi443 – 4431Q → A: Loss of threonine sensitivity for the aspartokinase activity and decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
Mutagenesisi522 – 5221I → A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication
Mutagenesisi524 – 5241Q → A: No effect on the inhibition of aspartokinase activity by threonine, but decreased inhibition of homoserine dehydrogenase activity by threonine. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 8787ChloroplastSequence AnalysisAdd
BLAST
Chaini88 – 916829Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplasticPRO_0000245845Add
BLAST

Proteomic databases

PaxDbiO81852.
PRIDEiO81852.

Expressioni

Gene expression databases

ExpressionAtlasiO81852. baseline and differential.
GenevestigatoriO81852.

Interactioni

Subunit structurei

Homo- or heterodimer.Curated

Structurei

3D structure databases

ProteinModelPortaliO81852.
SMRiO81852. Positions 90-551, 554-912.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini412 – 48776ACT 1PROSITE-ProRule annotationAdd
BLAST
Domaini493 – 57078ACT 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 336249AspartokinaseBy similarityAdd
BLAST
Regioni337 – 562226InterfaceBy similarityAdd
BLAST
Regioni563 – 916354Homoserine dehydrogenaseBy similarityAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the aspartokinase family.Curated
In the C-terminal section; belongs to the homoserine dehydrogenase family.Curated
Contains 2 ACT domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transit peptide

Phylogenomic databases

eggNOGiCOG0527.
HOGENOMiHOG000271593.
InParanoidiO81852.
KOiK12524.
OMAiYIFGMLD.
PhylomeDBiO81852.

Family and domain databases

Gene3Di3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR011147. Bifunc_aspartokin/hSer_DH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF000727. ThrA. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR00657. asp_kinases. 1 hit.
PROSITEiPS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O81852-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATLKPSFTV SPPNSNPIRF GSFPPQCFLR VPKPRRLILP RFRKTTGGGG
60 70 80 90 100
GLIRCELPDF HLSATATTVS GVSTVNLVDQ VQIPKGEMWS VHKFGGTCVG
110 120 130 140 150
NSQRIRNVAE VIINDNSERK LVVVSAMSKV TDMMYDLIRK AQSRDDSYLS
160 170 180 190 200
ALEAVLEKHR LTARDLLDGD DLASFLSHLH NDISNLKAML RAIYIAGHAS
210 220 230 240 250
ESFSDFVAGH GELWSAQMLS YVVRKTGLEC KWMDTRDVLI VNPTSSNQVD
260 270 280 290 300
PDFGESEKRL DKWFSLNPSK IIIATGFIAS TPQNIPTTLK RDGSDFSAAI
310 320 330 340 350
MGALLRARQV TIWTDVDGVY SADPRKVNEA VILQTLSYQE AWEMSYFGAN
360 370 380 390 400
VLHPRTIIPV MRYNIPIVIR NIFNLSAPGT IICQPPEDDY DLKLTTPVKG
410 420 430 440 450
FATIDNLALI NVEGTGMAGV PGTASDIFGC VKDVGANVIM ISQASSEHSV
460 470 480 490 500
CFAVPEKEVN AVSEALRSRF SEALQAGRLS QIEVIPNCSI LAAVGQKMAS
510 520 530 540 550
TPGVSCTLFS ALAKANINVR AISQGCSEYN VTVVIKREDS VKALRAVHSR
560 570 580 590 600
FFLSRTTLAM GIVGPGLIGA TLLDQLRDQA AVLKQEFNID LRVLGITGSK
610 620 630 640 650
KMLLSDIGID LSRWRELLNE KGTEADLDKF TQQVHGNHFI PNSVVVDCTA
660 670 680 690 700
DSAIASRYYD WLRKGIHVIT PNKKANSGPL DQYLKLRDLQ RKSYTHYFYE
710 720 730 740 750
ATVGAGLPII STLRGLLETG DKILRIEGIC SGTLSYLFNN FVGDRSFSEV
760 770 780 790 800
VTEAKNAGFT EPDPRDDLSG TDVARKVIIL ARESGLKLDL ADLPIRSLVP
810 820 830 840 850
EPLKGCTSVE EFMEKLPQYD GDLAKERLDA ENSGEVLRYV GVVDAVNQKG
860 870 880 890 900
TVELRRYKKE HPFAQLAGSD NIIAFTTTRY KDHPLIVRGP GAGAQVTAGG
910
IFSDILRLAS YLGAPS
Length:916
Mass (Da):100,250
Last modified:November 1, 1998 - v1
Checksum:i7ECD984DAFC97C4F
GO
Isoform 2 (identifier: O81852-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     837-916: LRYVGVVDAV...RLASYLGAPS → RLFTTNVFPFDQCDHILTIYICM

Note: Derived from EST data. No experimental confirmation available.

Show »
Length:859
Mass (Da):94,426
Checksum:i1785CFCBF23709C7
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei837 – 91680LRYVG…LGAPS → RLFTTNVFPFDQCDHILTIY ICM in isoform 2. CuratedVSP_019798Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL024486 Genomic DNA. Translation: CAA19688.1.
AL161551 Genomic DNA. Translation: CAB78973.1.
CP002687 Genomic DNA. Translation: AEE84219.1.
CP002687 Genomic DNA. Translation: AEE84220.1.
BX827863 mRNA. No translation available.
PIRiT04752.
RefSeqiNP_193706.2. NM_118091.3. [O81852-2]
NP_974576.1. NM_202847.2. [O81852-1]
UniGeneiAt.32787.

Genome annotation databases

EnsemblPlantsiAT4G19710.2; AT4G19710.2; AT4G19710. [O81852-1]
GeneIDi827715.
KEGGiath:AT4G19710.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL024486 Genomic DNA. Translation: CAA19688.1 .
AL161551 Genomic DNA. Translation: CAB78973.1 .
CP002687 Genomic DNA. Translation: AEE84219.1 .
CP002687 Genomic DNA. Translation: AEE84220.1 .
BX827863 mRNA. No translation available.
PIRi T04752.
RefSeqi NP_193706.2. NM_118091.3. [O81852-2 ]
NP_974576.1. NM_202847.2. [O81852-1 ]
UniGenei At.32787.

3D structure databases

ProteinModelPortali O81852.
SMRi O81852. Positions 90-551, 554-912.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi O81852.
PRIDEi O81852.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G19710.2 ; AT4G19710.2 ; AT4G19710 . [O81852-1 ]
GeneIDi 827715.
KEGGi ath:AT4G19710.

Organism-specific databases

TAIRi AT4G19710.

Phylogenomic databases

eggNOGi COG0527.
HOGENOMi HOG000271593.
InParanoidi O81852.
KOi K12524.
OMAi YIFGMLD.
PhylomeDBi O81852.

Enzyme and pathway databases

UniPathwayi UPA00034 ; UER00015 .
UPA00050 ; UER00063 .
UPA00050 ; UER00461 .
UPA00051 ; UER00462 .
UPA00051 ; UER00465 .
BioCyci ARA:GQT-2291-MONOMER.
BRENDAi 1.1.1.3. 399.
SABIO-RK O81852.

Gene expression databases

ExpressionAtlasi O81852. baseline and differential.
Genevestigatori O81852.

Family and domain databases

Gene3Di 3.40.1160.10. 2 hits.
3.40.50.720. 1 hit.
InterProi IPR002912. ACT_dom.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR005106. Asp/hSer_DH_NAD-bd.
IPR001341. Asp_kinase_dom.
IPR018042. Aspartate_kinase_CS.
IPR011147. Bifunc_aspartokin/hSer_DH.
IPR001342. HDH_cat.
IPR019811. HDH_CS.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF01842. ACT. 2 hits.
PF00742. Homoserine_dh. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF000727. ThrA. 1 hit.
SUPFAMi SSF53633. SSF53633. 1 hit.
TIGRFAMsi TIGR00657. asp_kinases. 1 hit.
PROSITEi PS51671. ACT. 2 hits.
PS00324. ASPARTOKINASE. 1 hit.
PS01042. HOMOSER_DHGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana."
    Paris S., Wessel P.M., Dumas R.
    Protein Expr. Purif. 24:105-110(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES.
  4. "Whole genome sequence comparisons and 'full-length' cDNA sequences: a combined approach to evaluate and improve Arabidopsis genome annotation."
    Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M., Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M., Weissenbach J., Salanoubat M.
    Genome Res. 14:406-413(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  5. "Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine."
    Paris S., Viemon C., Curien G., Dumas R.
    J. Biol. Chem. 278:5361-5366(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, MUTAGENESIS OF ILE-441; GLN-443; ILE-522 AND GLN-524.
  6. "Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity."
    Curien G., Ravanel S., Robert M., Dumas R.
    J. Biol. Chem. 280:41178-41183(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiAKH2_ARATH
AccessioniPrimary (citable) accession number: O81852
Secondary accession number(s): Q3E9Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 112 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, Multifunctional enzyme, 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

External Data

Dasty 3