LYS1_YEAST
ID LYS1_YEAST Reviewed; 373 AA.
AC P38998; D6VVW5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Saccharopine dehydrogenase [NAD(+), L-lysine-forming] {ECO:0000303|PubMed:418069};
DE Short=SDH;
DE EC=1.5.1.7 {ECO:0000269|PubMed:17002315, ECO:0000269|PubMed:4287986, ECO:0000269|PubMed:4318475};
DE AltName: Full=Lysine--2-oxoglutarate reductase;
GN Name=LYS1 {ECO:0000312|SGD:S000001473};
GN OrderedLocusNames=YIR034C {ECO:0000312|SGD:S000001473};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RA Feller A.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP PROTEIN SEQUENCE OF 2-9; 36-65; 132-149; 193-204; 216-225 AND 313-327,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 2-3, CLEAVAGE OF INITIATOR METHIONINE, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=418069; DOI=10.1016/s0021-9258(17)34852-4;
RA Ogawa H., Fujioka M.;
RT "Purification and characterization of saccharopine dehydrogenase from
RT baker's yeast.";
RL J. Biol. Chem. 253:3666-3670(1978).
RN [6]
RP PROTEIN SEQUENCE OF 203-212.
RX PubMed=6769500; DOI=10.1016/0005-2795(80)90024-0;
RA Ogawa H., Hase T., Fujioka M.;
RT "Amino acid sequence of a peptide containing an essential cysteine residue
RT of yeast saccharopine dehydrogenase (L-lysine-forming).";
RL Biochim. Biophys. Acta 623:225-228(1980).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=4287986; DOI=10.1016/s0021-9258(18)96483-5;
RA Saunders P.P., Broquist H.P.;
RT "Saccharopine, an intermediate of the aminoadipic acid pathway of lysine
RT biosynthesis. IV. Saccharopine dehydrogenase.";
RL J. Biol. Chem. 241:3435-3440(1966).
RN [8]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4318475; DOI=10.1111/j.1432-1033.1970.tb01070.x;
RA Fujioka M., Nakatani Y.;
RT "A kinetic study of saccharopine dehydrogenase reaction.";
RL Eur. J. Biochem. 16:180-186(1970).
RN [9]
RP ACTIVITY REGULATION.
RX PubMed=378997; DOI=10.1016/s0021-9258(18)50279-9;
RA Ogawa H., Okamoto M., Fujioka M.;
RT "Chemical modification of the active site sulfhydryl group of saccharopine
RT dehydrogenase (L-lysine-forming).";
RL J. Biol. Chem. 254:7030-7035(1979).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=6985909; DOI=10.1016/s0021-9258(19)86123-9;
RA Fujioka M., Takata Y., Ogawa H., Okamoto M.;
RT "The inactivation of saccharopine dehydrogenase (L-lysine-forming) by
RT diethyl pyrocarbonate.";
RL J. Biol. Chem. 255:937-942(1980).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=6771291; DOI=10.1016/s0021-9258(20)79719-x;
RA Ogawa H., Fujioka M.;
RT "The reaction of pyridoxal 5'-phosphate with an essential lysine residue of
RT saccharopine dehydrogenase (L-lysine-forming).";
RL J. Biol. Chem. 255:7420-7425(1980).
RN [12]
RP INDUCTION.
RX PubMed=3123231; DOI=10.1111/j.1432-1033.1988.tb13773.x;
RA Ramos F., Dubois E., Pierard A.;
RT "Control of enzyme synthesis in the lysine biosynthetic pathway of
RT Saccharomyces cerevisiae. Evidence for a regulatory role of gene LYS14.";
RL Eur. J. Biochem. 171:171-176(1988).
RN [13]
RP RETRACTED PAPER.
RX PubMed=10077615; DOI=10.1073/pnas.96.6.2937;
RA Geraghty M.T., Bassett D., Morrell J.C., Gatto G.J. Jr., Bai J.,
RA Geisbrecht B.V., Hieter P., Gould S.J.;
RT "Detecting patterns of protein distribution and gene expression in
RT silico.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2937-2942(1999).
RN [14]
RP RETRACTION NOTICE OF PUBMED:10077615.
RX PubMed=15696628; DOI=10.1073/pnas.0407487101;
RA Bassett D., Morrell J.C., Gatto G.J. Jr., Bai J., Geisbrecht B.V.,
RA Hieter P., Gould S.J.;
RL Proc. Natl. Acad. Sci. U.S.A. 102:516-516(2005).
RN [15]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17002315; DOI=10.1021/bi0610808;
RA Xu H., West A.H., Cook P.F.;
RT "Overall kinetic mechanism of saccharopine dehydrogenase from Saccharomyces
RT cerevisiae.";
RL Biochemistry 45:12156-12166(2006).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=26928762; DOI=10.1038/nmeth.3795;
RA Yofe I., Weill U., Meurer M., Chuartzman S., Zalckvar E., Goldman O.,
RA Ben-Dor S., Schuetze C., Wiedemann N., Knop M., Khmelinskii A.,
RA Schuldiner M.;
RT "One library to make them all: streamlining the creation of yeast libraries
RT via a SWAp-Tag strategy.";
RL Nat. Methods 13:371-378(2016).
RN [19]
RP SUBCELLULAR LOCATION.
RX PubMed=28928432; DOI=10.1038/s41598-017-11942-2;
RA Al-Saryi N.A., Al-Hejjaj M.Y., van Roermund C.W.T., Hulmes G.E., Ekal L.,
RA Payton C., Wanders R.J.A., Hettema E.H.;
RT "Two NAD-linked redox shuttles maintain the peroxisomal redox balance in
RT Saccharomyces cerevisiae.";
RL Sci. Rep. 7:11868-11868(2017).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-373 IN COMPLEX WITH AMP AND
RP SUBSTRATE ANALOG, AND DISULFIDE BOND.
RX PubMed=17939687; DOI=10.1021/bi701428m;
RA Andi B., Xu H., Cook P.F., West A.H.;
RT "Crystal structures of ligand-bound saccharopine dehydrogenase from
RT Saccharomyces cerevisiae.";
RL Biochemistry 46:12512-12521(2007).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 1-373, AND DISULFIDE BOND.
RX PubMed=17854830; DOI=10.1016/j.jmb.2007.08.044;
RA Burk D.L., Hwang J., Kwok E., Marrone L., Goodfellow V., Dmitrienko G.I.,
RA Berghuis A.M.;
RT "Structural studies of the final enzyme in the alpha-aminoadipate pathway-
RT saccharopine dehydrogenase from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 373:745-754(2007).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 1-373 IN COMPLEX WITH
RP L-SACCHAROPINE AND NAD, ACTIVE SITE, AND MUTAGENESIS OF LYS-77; HIS-96 AND
RP CYS-205.
RX PubMed=22243403; DOI=10.1021/bi201808u;
RA Kumar V.P., Thomas L.M., Bobyk K.D., Andi B., Cook P.F., West A.H.;
RT "Evidence in support of lysine 77 and histidine 96 as acid-base catalytic
RT residues in saccharopine dehydrogenase from Saccharomyces cerevisiae.";
RL Biochemistry 51:857-866(2012).
CC -!- FUNCTION: Catalyzes the NAD(+)-dependent cleavage of saccharopine to L-
CC lysine and 2-oxoglutarate, the final step in the alpha-aminoadipate
CC (AAA) pathway for lysine biosynthesis. {ECO:0000269|PubMed:17002315,
CC ECO:0000269|PubMed:4287986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-saccharopine + NAD(+) = 2-oxoglutarate + H(+) + L-
CC lysine + NADH; Xref=Rhea:RHEA:12440, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16810, ChEBI:CHEBI:32551,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57951; EC=1.5.1.7;
CC Evidence={ECO:0000269|PubMed:17002315, ECO:0000269|PubMed:4287986,
CC ECO:0000269|PubMed:4318475};
CC -!- ACTIVITY REGULATION: Inhibited by p-chloromercuribenzoate and
CC iodoacetate by modification of the active site cysteine residue.
CC Inhibited by diethyl pyrocarbonate by modification of histidine
CC residues. Inhibited by pyridoxal 5'-phosphate by modification of an
CC essential lysine residue. {ECO:0000269|PubMed:378997,
CC ECO:0000269|PubMed:418069, ECO:0000269|PubMed:6771291,
CC ECO:0000269|PubMed:6985909}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.089 mM for NADH (at pH 6.8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:4318475};
CC KM=0.1 mM for NAD(+) (at pH 6.8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:4318475};
CC KM=1.67 mM for saccharopine (at pH 6.8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:4318475};
CC KM=0.55 mM for 2-oxoglutarate (at pH 6.8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:4318475};
CC KM=2.0 mM for L-lysine (at pH 6.8 and 22 degrees Celsius)
CC {ECO:0000269|PubMed:4318475};
CC KM=0.019 mM for NADH (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17002315};
CC KM=0.9 mM for NAD(+) (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17002315};
CC KM=6.7 mM for saccharopine (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17002315};
CC KM=0.11 mM for 2-oxoglutarate (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17002315};
CC KM=1.1 mM for L-lysine (at pH 7 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17002315};
CC pH dependence:
CC Optimum pH is 10 for the forward reaction, and 6.5-7 for the reverse
CC reaction. {ECO:0000269|PubMed:4287986};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA
CC pathway; L-lysine from L-alpha-aminoadipate (fungal route): step 3/3.
CC {ECO:0000305|PubMed:4287986}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:418069}.
CC -!- INTERACTION:
CC P38998; P39940: RSP5; NbExp=3; IntAct=EBI-10264, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:26928762,
CC ECO:0000269|PubMed:28928432}.
CC -!- INDUCTION: Induced by alpha-aminoadipate semialdehyde in a LYS14-
CC dependent manner. Repressed by lysine. {ECO:0000269|PubMed:3123231}.
CC -!- MISCELLANEOUS: Present with 111934 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the AlaDH/PNT family. {ECO:0000305}.
CC -!- CAUTION: PubMed:10077615 shows data confirming the peroxisomal
CC localization of the protein, however this study was later retracted as
CC the images were additionally used in other articles for other proteins.
CC {ECO:0000305|PubMed:15696628}.
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DR EMBL; X77362; CAA54551.1; -; Genomic_DNA.
DR EMBL; Z38061; CAA86194.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08581.1; -; Genomic_DNA.
DR PIR; S48496; S48496.
DR RefSeq; NP_012300.3; NM_001179556.3.
DR PDB; 2Q99; X-ray; 1.64 A; A=1-373.
DR PDB; 2QRJ; X-ray; 1.60 A; A=1-373.
DR PDB; 2QRK; X-ray; 1.75 A; A=1-373.
DR PDB; 2QRL; X-ray; 1.60 A; A=1-373.
DR PDB; 3UGK; X-ray; 2.01 A; A=1-373.
DR PDB; 3UH1; X-ray; 2.17 A; A=1-373.
DR PDB; 3UHA; X-ray; 2.30 A; A/B=1-373.
DR PDBsum; 2Q99; -.
DR PDBsum; 2QRJ; -.
DR PDBsum; 2QRK; -.
DR PDBsum; 2QRL; -.
DR PDBsum; 3UGK; -.
DR PDBsum; 3UH1; -.
DR PDBsum; 3UHA; -.
DR AlphaFoldDB; P38998; -.
DR SMR; P38998; -.
DR BioGRID; 35025; 26.
DR DIP; DIP-5291N; -.
DR IntAct; P38998; 11.
DR MINT; P38998; -.
DR STRING; 4932.YIR034C; -.
DR CarbonylDB; P38998; -.
DR iPTMnet; P38998; -.
DR MaxQB; P38998; -.
DR PaxDb; P38998; -.
DR PRIDE; P38998; -.
DR EnsemblFungi; YIR034C_mRNA; YIR034C; YIR034C.
DR GeneID; 854852; -.
DR KEGG; sce:YIR034C; -.
DR SGD; S000001473; LYS1.
DR VEuPathDB; FungiDB:YIR034C; -.
DR eggNOG; KOG0172; Eukaryota.
DR HOGENOM; CLU_063085_0_0_1; -.
DR InParanoid; P38998; -.
DR OMA; YFFFSHT; -.
DR BioCyc; YEAST:YIR034C-MON; -.
DR BRENDA; 1.5.1.7; 984.
DR SABIO-RK; P38998; -.
DR UniPathway; UPA00033; UER00034.
DR EvolutionaryTrace; P38998; -.
DR PRO; PR:P38998; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P38998; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0004754; F:saccharopine dehydrogenase (NAD+, L-lysine-forming) activity; IDA:SGD.
DR GO; GO:0009085; P:lysine biosynthetic process; IMP:SGD.
DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniPathway.
DR CDD; cd12188; SDH; 1.
DR InterPro; IPR007886; AlaDH/PNT_N.
DR InterPro; IPR007698; AlaDH/PNT_NAD(H)-bd.
DR InterPro; IPR027281; Lys1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF05222; AlaDh_PNT_N; 1.
DR PIRSF; PIRSF018250; Saccharopine_DH_Lys; 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 3D-structure; Acetylation; Amino-acid biosynthesis;
KW Direct protein sequencing; Disulfide bond; Lysine biosynthesis; NAD;
KW Oxidoreductase; Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:418069, ECO:0000269|Ref.4"
FT CHAIN 2..373
FT /note="Saccharopine dehydrogenase [NAD(+), L-lysine-
FT forming]"
FT /id="PRO_0000199016"
FT MOTIF 371..373
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:10077615"
FT ACT_SITE 77
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687"
FT ACT_SITE 96
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687"
FT BINDING 18
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1"
FT BINDING 77
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1"
FT BINDING 101
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0007744|PDB:3UH1"
FT BINDING 130
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:3UHA"
FT BINDING 131
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1"
FT BINDING 135
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0007744|PDB:3UH1"
FT BINDING 203..204
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1,
FT ECO:0007744|PDB:3UHA"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1,
FT ECO:0007744|PDB:3UHA"
FT BINDING 231
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0000305|PubMed:17939687, ECO:0007744|PDB:3UH1,
FT ECO:0007744|PDB:3UHA"
FT BINDING 251
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0007744|PDB:3UH1"
FT BINDING 278
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA"
FT BINDING 279..281
FT /ligand="L-saccharopine"
FT /ligand_id="ChEBI:CHEBI:57951"
FT /evidence="ECO:0007744|PDB:3UH1"
FT BINDING 318..321
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000269|PubMed:22243403,
FT ECO:0007744|PDB:3UH1, ECO:0007744|PDB:3UHA"
FT MOD_RES 2
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000269|Ref.4"
FT DISULFID 205..249
FT /evidence="ECO:0000269|PubMed:17854830,
FT ECO:0000269|PubMed:17939687, ECO:0007744|PDB:2Q99,
FT ECO:0007744|PDB:2QRJ, ECO:0007744|PDB:2QRL"
FT MUTAGEN 77
FT /note="K->M: Decreases the turnover number 145-fold.
FT Decreases the turnover number 700-fold; when associated
FT with GLN-96."
FT /evidence="ECO:0000269|PubMed:22243403"
FT MUTAGEN 96
FT /note="H->Q: Decreases the turnover number 28-fold.
FT Decreases the turnover number 700-fold; when associated
FT with MET-77."
FT /evidence="ECO:0000269|PubMed:22243403"
FT MUTAGEN 205
FT /note="C->S: Prevents disulfide formation."
FT /evidence="ECO:0000269|PubMed:22243403"
FT CONFLICT 209
FT /note="A -> AL (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="A -> V (in Ref. 1; CAA54551)"
FT /evidence="ECO:0000305"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 23..31
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2QRL"
FT HELIX 48..53
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 104..114
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3UHA"
FT HELIX 136..156
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:2QRJ"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2QRJ"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 321..324
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 326..342
FT /evidence="ECO:0007829|PDB:2QRJ"
FT TURN 345..349
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 351..365
FT /evidence="ECO:0007829|PDB:2QRJ"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:2QRL"
SQ SEQUENCE 373 AA; 41465 MW; 7E3A810876C1DC41 CRC64;
MAAVTLHLRA ETKPLEARAA LTPTTVKKLI AKGFKIYVED SPQSTFNINE YRQAGAIIVP
AGSWKTAPRD RIIIGLKEMP ETDTFPLVHE HIQFAHCYKD QAGWQNVLMR FIKGHGTLYD
LEFLENDQGR RVAAFGFYAG FAGAALGVRD WAFKQTHSDD EDLPAVSPYP NEKALVKDVT
KDYKEALATG ARKPTVLIIG ALGRCGSGAI DLLHKVGIPD ANILKWDIKE TSRGGPFDEI
PQADIFINCI YLSKPIAPFT NMEKLNNPNR RLRTVVDVSA DTTNPHNPIP IYTVATVFNK
PTVLVPTTAG PKLSVISIDH LPSLLPREAS EFFSHDLLPS LELLPQRKTA PVWVRAKKLF
DRHCARVKRS SRL
