AASS_ARATH
ID AASS_ARATH Reviewed; 1064 AA.
AC Q9SMZ4; O04155; O04156; O04884; Q7DM71; Q947M5; Q94BT4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Alpha-aminoadipic semialdehyde synthase;
DE AltName: Full=cAt-LKR/SDH;
DE Short=LKR/SDH;
DE Includes:
DE RecName: Full=Lysine ketoglutarate reductase;
DE Short=LKR;
DE EC=1.5.1.8;
DE Includes:
DE RecName: Full=Saccharopine dehydrogenase;
DE EC=1.5.1.9;
DE AltName: Full=cAt-SDH;
DE Short=SDH;
GN Name=LKR/SDH; Synonyms=LKR, SDH; OrderedLocusNames=At4g33150;
GN ORFNames=F4I10.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), FUNCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=9286108; DOI=10.2307/3870383;
RA Tang G., Miron D., Zhu-Shimoni J.X., Galili G.;
RT "Regulation of lysine catabolism through lysine-ketoglutarate reductase and
RT saccharopine dehydrogenase in Arabidopsis.";
RL Plant Cell 9:1305-1316(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM LONG), AND FUNCTION.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=9426595; DOI=10.1023/a:1005808923191;
RA Epelbaum S., McDevitt R., Falco S.C.;
RT "Lysine-ketoglutarate reductase and saccharopine dehydrogenase from
RT Arabidopsis thaliana: nucleotide sequence and characterization.";
RL Plant Mol. Biol. 35:735-748(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12226495; DOI=10.1104/pp.005660;
RA Tang G., Zhu X., Gakiere B., Levanony H., Kahana A., Galili G.;
RT "The bifunctional LKR/SDH locus of plants also encodes a highly active
RT monofunctional lysine-ketoglutarate reductase using a polyadenylation
RT signal located within an intron.";
RL Plant Physiol. 130:147-154(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 529-1064 (ISOFORM LONG).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP ALTERNATIVE INITIATION.
RX PubMed=10929113; DOI=10.1046/j.1365-313x.2000.00770.x;
RA Tang G., Zhu X., Tang X., Galili G.;
RT "A novel composite locus of Arabidopsis encoding two polypeptides with
RT metabolically related but distinct functions in lysine catabolism.";
RL Plant J. 23:195-203(2000).
RN [8]
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11080311; DOI=10.1104/pp.124.3.1363;
RA Zhu X., Tang G., Galili G.;
RT "Characterization of the two saccharopine dehydrogenase isozymes of lysine
RT catabolism encoded by the single composite AtLKR/SDH locus of
RT Arabidopsis.";
RL Plant Physiol. 124:1363-1371(2000).
RN [9]
RP FUNCTION.
RX PubMed=11500552; DOI=10.1104/pp.126.4.1539;
RA Zhu X., Tang G., Granier F., Bouchez D., Galili G.;
RT "A T-DNA insertion knockout of the bifunctional lysine-ketoglutarate
RT reductase/saccharopine dehydrogenase gene elevates lysine levels in
RT Arabidopsis seeds.";
RL Plant Physiol. 126:1539-1545(2001).
RN [10]
RP ACTIVITY REGULATION, SUBUNIT, PHOSPHORYLATION AT THR-238 AND SER-458, AND
RP MUTAGENESIS OF THR-238; SER-407; SER-458 AND 551-ASN--ARG-554.
RX PubMed=12393892; DOI=10.1074/jbc.m205466200;
RA Zhu X., Tang G., Galili G.;
RT "The activity of the Arabidopsis bifunctional lysine-ketoglutarate
RT reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
RT regulated by functional interaction between its two enzyme domains.";
RL J. Biol. Chem. 277:49655-49661(2002).
RN [11]
RP INDUCTION.
RX PubMed=14576281; DOI=10.1104/pp.103.026294;
RA Stepansky A., Galili G.;
RT "Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate
RT reductase/saccharopine dehydrogenase enzyme of lysine catabolism is
RT concertedly regulated by metabolic and stress-associated signals.";
RL Plant Physiol. 133:1407-1415(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15569707; DOI=10.1093/jxb/eri031;
RA Stepansky A., Yao Y., Tang G., Galili G.;
RT "Regulation of lysine catabolism in Arabidopsis through concertedly
RT regulated synthesis of the two distinct gene products of the composite
RT AtLKR/SDH locus.";
RL J. Exp. Bot. 56:525-536(2005).
CC -!- FUNCTION: Bifunctional enzyme that catalyzes the first two steps in
CC lysine degradation. The N-terminal and the C-terminal contain lysine-
CC oxoglutarate reductase and saccharopine dehydrogenase activity,
CC respectively. Negatively regulates free Lys accumulation in seeds.
CC {ECO:0000269|PubMed:11500552, ECO:0000269|PubMed:9286108,
CC ECO:0000269|PubMed:9426595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NADP(+) = 2-oxoglutarate + H(+) + L-
CC lysine + NADPH; Xref=Rhea:RHEA:19373, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:57951, ChEBI:CHEBI:58349; EC=1.5.1.8;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NAD(+) = (S)-2-amino-6-oxohexanoate +
CC H(+) + L-glutamate + NADH; Xref=Rhea:RHEA:24520, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:57951, ChEBI:CHEBI:58321; EC=1.5.1.9;
CC -!- ACTIVITY REGULATION: The LKR activity is stimulated by NaCl.
CC {ECO:0000269|PubMed:12393892}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.180 mM for lysine (isoform Long at pH 7.5 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.272 mM for alpha-ketoglutarate (isoform Long at pH 7.5 and 30
CC degrees Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.044 mM for NADPH (isoform Long at pH 7.5 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11080311};
CC KM=0.063 mM for saccharopine (isoform Long at pH 7 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.035 mM for saccharopine (isoform Long at pH 9 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.130 mM for saccharopine (isoform Short at pH 7 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.050 mM for saccharopine (isoform Short at pH 9 and 30 degrees
CC Celsius) {ECO:0000269|PubMed:11080311};
CC KM=0.374 mM for NAD (isoform Long at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11080311};
CC KM=0.698 mM for NAD (isoform Long at pH 9 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11080311};
CC KM=0.333 mM for NAD (isoform Short at pH 7 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11080311};
CC KM=0.759 mM for NAD (isoform Short at pH 9 and 30 degrees Celsius)
CC {ECO:0000269|PubMed:11080311};
CC pH dependence:
CC Optimum pH is 7.5 for LKR activity of isoform Long, and 9 for SDH
CC activity of both isoforms Long and Short.
CC {ECO:0000269|PubMed:11080311};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 1/6.
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 2/6.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12393892}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11080311}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Name=Long;
CC IsoId=Q9SMZ4-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q9SMZ4-2; Sequence=VSP_018641;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in flowers. Isoform
CC Long is mostly present in young leaves, cotyledons, root tips and
CC mature root parts. Whereas isoform Short is mostly expressed in
CC cotyledons and at low levels in all root parts.
CC {ECO:0000269|PubMed:15569707, ECO:0000269|PubMed:9286108}.
CC -!- DEVELOPMENTAL STAGE: In flowers, confined to ovules and vascular tissue
CC of anther filament. In developing and mature seeds, expressed in embryo
CC and the outer layers of the endosperm. {ECO:0000269|PubMed:9286108}.
CC -!- INDUCTION: Lysine, Sugar starvation, ABA and MeJA induce isoform Long,
CC but not isoform Short (at protein level). Nitrogen starvation repress
CC isoform Long, but not isoform Short (at protein level). Isoform Long
CC and isoform Short are both slightly induced by NaCl and drought stress,
CC but repressed by sugars. {ECO:0000269|PubMed:14576281,
CC ECO:0000269|PubMed:15569707}.
CC -!- PTM: Phosphorylation of Ser-458 seems important for the LKR activity.
CC {ECO:0000269|PubMed:12393892}.
CC -!- MISCELLANEOUS: [Isoform Long]: Contains both LKR and SDH activities.
CC -!- MISCELLANEOUS: [Isoform Short]: Contains only SDH activity.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AlaDH/PNT family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the saccharopine
CC dehydrogenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK64010.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK97099.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Its C-terminal part is derived from gene At1G61240 whose function is unknown. Originally thought to be an alternative splicing form of At4g33150.; Evidence={ECO:0000305};
CC Sequence=AAM16268.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U90522; AAB53975.1; -; mRNA.
DR EMBL; U90523; AAD00700.1; -; mRNA.
DR EMBL; U95758; AAB96825.1; -; Genomic_DNA.
DR EMBL; U95759; AAB96826.1; -; mRNA.
DR EMBL; AF295389; AAK97099.1; ALT_SEQ; mRNA.
DR EMBL; AL035525; CAB36789.1; -; Genomic_DNA.
DR EMBL; AL161583; CAB80032.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86184.1; -; Genomic_DNA.
DR EMBL; AY039906; AAK64010.1; ALT_INIT; mRNA.
DR EMBL; AY094007; AAM16268.1; ALT_INIT; mRNA.
DR PIR; T05195; T05195.
DR RefSeq; NP_001154283.1; NM_001160811.2. [Q9SMZ4-2]
DR AlphaFoldDB; Q9SMZ4; -.
DR SMR; Q9SMZ4; -.
DR STRING; 3702.AT4G33150.2; -.
DR iPTMnet; Q9SMZ4; -.
DR PaxDb; Q9SMZ4; -.
DR EnsemblPlants; AT4G33150.3; AT4G33150.3; AT4G33150. [Q9SMZ4-2]
DR GeneID; 829452; -.
DR Gramene; AT4G33150.3; AT4G33150.3; AT4G33150. [Q9SMZ4-2]
DR KEGG; ath:AT4G33150; -.
DR Araport; AT4G33150; -.
DR eggNOG; KOG0172; Eukaryota.
DR InParanoid; Q9SMZ4; -.
DR OMA; KMEGRSE; -.
DR PhylomeDB; Q9SMZ4; -.
DR BioCyc; ARA:AT4G33150-MON; -.
DR SABIO-RK; Q9SMZ4; -.
DR UniPathway; UPA00868; UER00835.
DR UniPathway; UPA00868; UER00836.
DR PRO; PR:Q9SMZ4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SMZ4; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047131; F:saccharopine dehydrogenase (NAD+, L-glutamate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0047130; F:saccharopine dehydrogenase (NADP+, L-lysine-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004753; F:saccharopine dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IBA:GO_Central.
DR CDD; cd12144; SDH_N_domain; 1.
DR Gene3D; 3.30.70.2690; -; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR007545; LOR/SDH_bifunc_enz_cons_dom.
DR InterPro; IPR043009; LOR/SDH_bifunc_enz_cons_dom_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032095; Sacchrp_dh-like_C.
DR InterPro; IPR005097; Sacchrp_dh_NADP.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR Pfam; PF04455; Saccharop_dh_N; 1.
DR Pfam; PF16653; Sacchrp_dh_C; 1.
DR Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR SMART; SM01002; AlaDh_PNT_C; 1.
DR SMART; SM01003; AlaDh_PNT_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Cytoplasm; Multifunctional enzyme; NAD; NADP;
KW Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..1064
FT /note="Alpha-aminoadipic semialdehyde synthase"
FT /id="PRO_0000226070"
FT REGION 24..445
FT /note="Lysine-ketoglutarate reductase"
FT REGION 583..1064
FT /note="Saccharopine dehydrogenase"
FT BINDING 703..704
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 729..731
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 730
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 830
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT BINDING 852..854
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R4"
FT MOD_RES 238
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:12393892"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12393892"
FT VAR_SEQ 1..582
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:9286108"
FT /id="VSP_018641"
FT MUTAGEN 238
FT /note="T->A,D: No effect on LKR and SDH activity."
FT /evidence="ECO:0000269|PubMed:12393892"
FT MUTAGEN 407
FT /note="S->A: No effect on LKR and SDH activity."
FT /evidence="ECO:0000269|PubMed:12393892"
FT MUTAGEN 407
FT /note="S->D: No LKR activity, but no effect on SDH
FT activity."
FT /evidence="ECO:0000269|PubMed:12393892"
FT MUTAGEN 458
FT /note="S->A: Reduced LKR activity, but no effect on SDH
FT activity."
FT /evidence="ECO:0000269|PubMed:12393892"
FT MUTAGEN 458
FT /note="S->D: No effect on LKR and SDH activity."
FT /evidence="ECO:0000269|PubMed:12393892"
FT MUTAGEN 551..554
FT /note="NEDY->IEGR: Loss of LKR activity stimulation by
FT NaCl."
FT /evidence="ECO:0000269|PubMed:12393892"
FT CONFLICT 167..169
FT /note="KLI -> YLS (in Ref. 1; AAB53975, 2; AAB96825/
FT AAB96826 and 3; AAK97099)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="R -> S (in Ref. 1; AAB53975 and 3; AAK97099)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="F -> V (in Ref. 6; AAK64010/AAM16268)"
FT /evidence="ECO:0000305"
FT CONFLICT 715
FT /note="K -> N (in Ref. 1; AAB53975/AAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 735
FT /note="H -> P (in Ref. 1; AAB53975/AAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="M -> K (in Ref. 1; AAB53975/AAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 746..748
FT /note="HIK -> PIT (in Ref. 1; AAB53975/AAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 765
FT /note="P -> R (in Ref. 1; AAB53975/AAD00700)"
FT /evidence="ECO:0000305"
FT CONFLICT 827
FT /note="F -> L (in Ref. 2; AAB96825/AAB96826)"
FT /evidence="ECO:0000305"
FT CONFLICT 1040
FT /note="L -> F (in Ref. 2; AAB96825)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1064 AA; 117149 MW; 6CA4EBDB22898C7E CRC64;
MNSNGHEEEK KLGNGVVGIL AETVNKWERR TPLTPSHCAR LLHGGKDRTG ISRIVVQPSA
KRIHHDALYE DVGCEISDDL SDCGLILGIK QPELEMILPE RAYAFFSHTH KAQKENMPLL
DKILSERVTL CDYELIVGDH GKRLLAFGKY AGRAGLVDFL HGLGQRKLIL GYSTPFLSLG
ASYMYSSLAA AKAAVISVGE EIASQGLPLG ICPLVFVFTG TGNVSLGAQE IFKLLPHTFV
EPSKLPELFV KDKGISQNGI STKRVYQVYG CIITSQDMVE HKDPSKSFDK ADYYAHPEHY
NPVFHEKISP YTSVLVNCMY WEKRFPCLLS TKQLQDLTKK GLPLVGICDI TCDIGGSIEF
VNRATLIDSP FFRFNPSNNS YYDDMDGDGV LCMAVDILPT EFAKEASQHF GDILSGFVGS
LASMTEISDL PAHLKRACIS YRGELTSLYE YIPRMRKSNP EEAQDNIIAN GVSSQRTFNI
LVSLSGHLFD KFLINEALDM IEAAGGSFHL AKCELGQSAD AESYSELEVG ADDKRVLDQI
IDSLTRLANP NEDYISPHRE ANKISLKIGK VQQENEIKEK PEMTKKSGVL ILGAGRVCRP
AADFLASVRT ISSQQWYKTY FGADSEEKTD VHVIVASLYL KDAKETVEGI SDVEAVRLDV
SDSESLLKYV SQVDVVLSLL PASCHAVVAK TCIELKKHLV TASYVDDETS MLHEKAKSAG
ITILGEMGLD PGIDHMMAMK MINDAHIKKG KVKSFTSYCG GLPSPAAANN PLAYKFSWNP
AGAIRAGQNP AKYKSNGDII HVDGKNLYDS AARFRVPNLP AFALECFPNR DSLVYGEHYG
IESEATTIFR GTLRYEGFSM IMATLSKLGF FDSEANQVLS TGKRITFGAL LSNILNKDAD
NESEPLAGEE EISKRIIKLG HSKETAAKAA KTIVFLGFNE EREVPSLCKS VFDATCYLME
EKLAYSGNEQ DMVLLHHEVE VEFLESKRIE KHTATLLEFG DIKNGQTTTA MAKTVGIPAA
IGALLLIEDK IKTRGVLRPL EAEVYLPALD ILQAYGIKLM EKAE
