Q9SMZ4 (AASS_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1064 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Coding sequence diversity	Alternative initiation
Ligand	NAD NADP
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	L-lysine catabolic process to acetyl-CoA via saccharopine Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity Inferred from electronic annotation. Source: EC saccharopine dehydrogenase (NADP+, L-lysine-forming) activity Inferred from electronic annotation. Source: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1064	1064	Alpha-aminoadipic semialdehyde synthase		PRO_0000226070
Regions
	Region	24 – 445	422	Lysine-ketoglutarate reductase
	Region	583 – 1064	482	Saccharopine dehydrogenase
Amino acid modifications
	Modified residue	238	1	Phosphothreonine Ref.10
	Modified residue	458	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	1 – 582	582	Missing in isoform Short.		VSP_018641
Experimental info
	Mutagenesis	238	1	T → A or D: No effect on LKR and SDH activity. Ref.10
	Mutagenesis	407	1	S → A: No effect on LKR and SDH activity. Ref.10
	Mutagenesis	407	1	S → D: No LKR activity, but no effect on SDH activity. Ref.10
	Mutagenesis	458	1	S → A: Reduced LKR activity, but no effect on SDH activity. Ref.10
	Mutagenesis	458	1	S → D: No effect on LKR and SDH activity. Ref.10
	Mutagenesis	551 – 554	4	NEDY → IEGR: Loss of LKR activity stimulation by NaCl. Ref.10
	Sequence conflict	167 – 169	3	KLI → YLS in AAB53975. Ref.1
	Sequence conflict	167 – 169	3	KLI → YLS in AAB96825. Ref.2
	Sequence conflict	167 – 169	3	KLI → YLS in AAB96826. Ref.2
	Sequence conflict	167 – 169	3	KLI → YLS in AAK97099. Ref.3
	Sequence conflict	324	1	R → S in AAB53975. Ref.1
	Sequence conflict	324	1	R → S in AAK97099. Ref.3
	Sequence conflict	621	1	F → V in AAK64010. Ref.6
	Sequence conflict	621	1	F → V in AAM16268. Ref.6
	Sequence conflict	715	1	K → N in AAB53975. Ref.1
	Sequence conflict	715	1	K → N in AAD00700. Ref.1
	Sequence conflict	735	1	H → P in AAB53975. Ref.1
	Sequence conflict	735	1	H → P in AAD00700. Ref.1
	Sequence conflict	739	1	M → K in AAB53975. Ref.1
	Sequence conflict	739	1	M → K in AAD00700. Ref.1
	Sequence conflict	746 – 748	3	HIK → PIT in AAB53975. Ref.1
	Sequence conflict	746 – 748	3	HIK → PIT in AAD00700. Ref.1
	Sequence conflict	765	1	P → R in AAB53975. Ref.1
	Sequence conflict	765	1	P → R in AAD00700. Ref.1
	Sequence conflict	827	1	F → L in AAB96825. Ref.2
	Sequence conflict	827	1	F → L in AAB96826. Ref.2
	Sequence conflict	1040	1	L → F in AAB96825. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6CA4EBDB22898C7E	FASTA	1,064	117,149
	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
	Isoform Short [UniParc]. Checksum: A249E25010D557A3	FASTA	482	52,704
	10 20 30 40 50 60 MTKKSGVLIL GAGRVCRPAA DFLASVRTIS SQQWYKTYFG ADSEEKTDVH VIVASLYLKD 70 80 90 100 110 120 AKETVEGISD VEAVRLDVSD SESLLKYVSQ VDVVLSLLPA SCHAVVAKTC IELKKHLVTA 130 140 150 160 170 180 SYVDDETSML HEKAKSAGIT ILGEMGLDPG IDHMMAMKMI NDAHIKKGKV KSFTSYCGGL 190 200 210 220 230 240 PSPAAANNPL AYKFSWNPAG AIRAGQNPAK YKSNGDIIHV DGKNLYDSAA RFRVPNLPAF 250 260 270 280 290 300 ALECFPNRDS LVYGEHYGIE SEATTIFRGT LRYEGFSMIM ATLSKLGFFD SEANQVLSTG 310 320 330 340 350 360 KRITFGALLS NILNKDADNE SEPLAGEEEI SKRIIKLGHS KETAAKAAKT IVFLGFNEER 370 380 390 400 410 420 EVPSLCKSVF DATCYLMEEK LAYSGNEQDM VLLHHEVEVE FLESKRIEKH TATLLEFGDI 430 440 450 460 470 480 KNGQTTTAMA KTVGIPAAIG ALLLIEDKIK TRGVLRPLEA EVYLPALDIL QAYGIKLMEK AE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00517041. IPI00760342.
PIR	T05195.
RefSeq	NP_001154283.1. NM_001160811.1.
UniGene	At.20921.
3D structure databases
ProteinModelPortal	Q9SMZ4.
SMR	Q9SMZ4. Positions 214-239, 589-1062.
ModBase	Search...
Proteomic databases
PaxDb	Q9SMZ4.
PRIDE	Q9SMZ4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	829452.
KEGG	ath:AT4G33150.
Organism-specific databases
TAIR	At4g33150.
Phylogenomic databases
eggNOG	COG1748.
InParanoid	Q9SMZ4.
PhylomeDB	Q9SMZ4.
Enzyme and pathway databases
UniPathway	UPA00868; UER00835. UPA00868; UER00836.
Gene expression databases
ArrayExpress	Q9SMZ4.
Genevestigator	Q9SMZ4.
GermOnline	AT4G33150. Arabidopsis thaliana.
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
InterPro	IPR007886. 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]
Pfam	PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. PF03435. Saccharop_dh. 1 hit. PF04455. Saccharop_dh_N. 1 hit. [Graphical view]
SMART	SM01002. AlaDh_PNT_C. 1 hit. SM01003. AlaDh_PNT_N. 1 hit. [Graphical view]
PROSITE	PS00836. ALADH_PNT_1. False negative. PS00837. ALADH_PNT_2. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AASS_ARATH

Accession

Primary (citable) accession number: Q9SMZ4
Secondary accession number(s): O04155 , O04156, O04884, Q7DM71, Q947M5, Q94BT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program