DAPAT_ARATH
ID DAPAT_ARATH Reviewed; 461 AA.
AC Q93ZN9; O81885;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=LL-diaminopimelate aminotransferase, chloroplastic;
DE Short=AtDAP-AT;
DE Short=DAP-AT;
DE Short=DAP-aminotransferase;
DE Short=LL-DAP-aminotransferase;
DE EC=2.6.1.83 {ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737};
DE AltName: Full=Protein ABERRANT GROWTH AND DEATH 2;
DE Flags: Precursor;
GN Name=DAP; Synonyms=AGD2; OrderedLocusNames=At4g33680; ORFNames=T16L1.170;
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], MUTAGENESIS OF PRO-398, SUBCELLULAR LOCATION,
RP INDUCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14729919; DOI=10.1105/tpc.019372;
RA Song J.T., Lu H., Greenberg J.T.;
RT "Divergent roles in Arabidopsis thaliana development and defense of two
RT homologous genes, aberrant growth and death2 and AGD2-LIKE DEFENSE RESPONSE
RT PROTEIN1, encoding novel aminotransferases.";
RL Plant Cell 16:353-366(2004).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=16361515; DOI=10.1104/pp.105.072629;
RA Hudson A.O., Singh B.K., Leustek T., Gilvarg C.;
RT "An LL-diaminopimelate aminotransferase defines a novel variant of the
RT lysine biosynthesis pathway in plants.";
RL Plant Physiol. 140:292-301(2006).
RN [6]
RP FUNCTION.
RX PubMed=21435399; DOI=10.1016/j.bbapap.2011.03.008;
RA Watanabe N., James M.N.;
RT "Structural insights for the substrate recognition mechanism of LL-
RT diaminopimelate aminotransferase.";
RL Biochim. Biophys. Acta 1814:1528-1533(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 36-461 IN COMPLEX WITH SUBSTRATE
RP ANALOG AND PYRIDOXAL PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBUNIT.
RX PubMed=17583737; DOI=10.1016/j.jmb.2007.05.061;
RA Watanabe N., Cherney M.M., van Belkum M.J., Marcus S.L., Flegel M.D.,
RA Clay M.D., Deyholos M.K., Vederas J.C., James M.N.;
RT "Crystal structure of LL-diaminopimelate aminotransferase from Arabidopsis
RT thaliana: a recently discovered enzyme in the biosynthesis of L-Lysine by
RT plants and Chlamydia.";
RL J. Mol. Biol. 371:685-702(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 36-461 OF MUTANTS AND WILD-TYPE
RP IN COMPLEX WITH SUBSTRATE ANALOG AND PYRIDOXAL PHOSPHATE ANALOG, FUNCTION,
RP MUTAGENESIS OF LYS-305, COFACTOR, AND SUBUNIT.
RX PubMed=18952095; DOI=10.1016/j.jmb.2008.10.022;
RA Watanabe N., Clay M.D., van Belkum M.J., Cherney M.M., Vederas J.C.,
RA James M.N.;
RT "Mechanism of substrate recognition and PLP-induced conformational changes
RT in LL-diaminopimelate aminotransferase from Arabidopsis thaliana.";
RL J. Mol. Biol. 384:1314-1329(2008).
CC -!- FUNCTION: Required for lysine biosynthesis. Catalyzes the direct
CC conversion of tetrahydrodipicolinate to LL-diaminopimelate, a reaction
CC that requires three enzymes in E.coli. Not active with meso-
CC diaminopimelate, lysine or ornithine as substrates.
CC {ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737,
CC ECO:0000269|PubMed:18952095, ECO:0000269|PubMed:21435399}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S,6S)-2,6-diaminoheptanedioate + 2-oxoglutarate = (S)-
CC 2,3,4,5-tetrahydrodipicolinate + H(+) + H2O + L-glutamate;
CC Xref=Rhea:RHEA:23988, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16845, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:57609; EC=2.6.1.83;
CC Evidence={ECO:0000269|PubMed:16361515, ECO:0000269|PubMed:17583737};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17583737, ECO:0000269|PubMed:18952095};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:17583737};
CC KM=67 uM for LL-2,6-diaminopimelate {ECO:0000269|PubMed:16361515};
CC KM=8.7 mM for 2-oxoglutarate {ECO:0000269|PubMed:16361515};
CC KM=38 uM for L-2,3,4,5-tetrahydrodipicolinate
CC {ECO:0000269|PubMed:16361515};
CC KM=1.9 mM for glutamatic acid {ECO:0000269|PubMed:16361515};
CC Vmax=22.3 umol/min/mg enzyme for the forward reaction
CC {ECO:0000269|PubMed:16361515};
CC Vmax=0.38 umol/min/mg enzyme for the reverse reaction
CC {ECO:0000269|PubMed:16361515};
CC pH dependence:
CC Optimum pH is 7.9 in Tris buffer and 7.6 in HEPES buffer.
CC {ECO:0000269|PubMed:16361515};
CC Temperature dependence:
CC Optimum temperature is 36 degrees Celsius.
CC {ECO:0000269|PubMed:16361515};
CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC (aminotransferase route): step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17583737,
CC ECO:0000269|PubMed:18952095}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:14729919}.
CC -!- TISSUE SPECIFICITY: Highly expressed in seedlings, roots, stems,
CC flowers and leaves. Lower expression in siliques.
CC {ECO:0000269|PubMed:14729919}.
CC -!- DEVELOPMENTAL STAGE: Down-regulated during senescence.
CC {ECO:0000269|PubMed:14729919}.
CC -!- INDUCTION: Not induced by pathogen infection, but down-regulated by
CC dark treatment. {ECO:0000269|PubMed:14729919}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality.
CC {ECO:0000269|PubMed:14729919}.
CC -!- MISCELLANEOUS: The expected covalent binding of pyridoxal phosphate by
CC Lys-305 has not been observed in the 3D-structure.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. LL-diaminopimelate aminotransferase subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA20581.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80085.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY518701; AAR99909.1; -; mRNA.
DR EMBL; AL031394; CAA20581.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161584; CAB80085.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86265.1; -; Genomic_DNA.
DR EMBL; AY056423; AAL08279.1; -; mRNA.
DR EMBL; AY065256; AAL38732.1; -; mRNA.
DR EMBL; AY117246; AAM51321.1; -; mRNA.
DR PIR; T04985; T04985.
DR RefSeq; NP_567934.1; NM_119526.4.
DR PDB; 2Z1Z; X-ray; 2.40 A; A/B=36-461.
DR PDB; 2Z20; X-ray; 1.95 A; A/B=36-461.
DR PDB; 3EI5; X-ray; 2.05 A; A/B=36-461.
DR PDB; 3EI6; X-ray; 1.90 A; A/B=36-461.
DR PDB; 3EI7; X-ray; 1.99 A; A/B=36-461.
DR PDB; 3EI8; X-ray; 1.60 A; A/B=36-461.
DR PDB; 3EI9; X-ray; 1.55 A; A/B=36-461.
DR PDB; 3EIA; X-ray; 1.85 A; A/B=36-461.
DR PDB; 3EIB; X-ray; 1.85 A; A/B=36-461.
DR PDBsum; 2Z1Z; -.
DR PDBsum; 2Z20; -.
DR PDBsum; 3EI5; -.
DR PDBsum; 3EI6; -.
DR PDBsum; 3EI7; -.
DR PDBsum; 3EI8; -.
DR PDBsum; 3EI9; -.
DR PDBsum; 3EIA; -.
DR PDBsum; 3EIB; -.
DR AlphaFoldDB; Q93ZN9; -.
DR SMR; Q93ZN9; -.
DR BioGRID; 14792; 16.
DR STRING; 3702.AT4G33680.1; -.
DR BindingDB; Q93ZN9; -.
DR ChEMBL; CHEMBL3308984; -.
DR MetOSite; Q93ZN9; -.
DR PaxDb; Q93ZN9; -.
DR PRIDE; Q93ZN9; -.
DR ProteomicsDB; 224699; -.
DR EnsemblPlants; AT4G33680.1; AT4G33680.1; AT4G33680.
DR GeneID; 829510; -.
DR Gramene; AT4G33680.1; AT4G33680.1; AT4G33680.
DR KEGG; ath:AT4G33680; -.
DR Araport; AT4G33680; -.
DR TAIR; locus:2134243; AT4G33680.
DR eggNOG; KOG0257; Eukaryota.
DR HOGENOM; CLU_051433_0_0_1; -.
DR InParanoid; Q93ZN9; -.
DR OMA; DFQARGC; -.
DR OrthoDB; 683031at2759; -.
DR PhylomeDB; Q93ZN9; -.
DR BioCyc; ARA:AT4G33680-MON; -.
DR BioCyc; MetaCyc:AT4G33680-MON; -.
DR BRENDA; 2.6.1.83; 399.
DR SABIO-RK; Q93ZN9; -.
DR UniPathway; UPA00034; UER00466.
DR EvolutionaryTrace; Q93ZN9; -.
DR PRO; PR:Q93ZN9; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q93ZN9; baseline and differential.
DR Genevisible; Q93ZN9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IDA:TAIR.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
DR GO; GO:0009862; P:systemic acquired resistance, salicylic acid mediated signaling pathway; IMP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_01642; DapL_aminotrans_1; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR019942; DapL/ALD1.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43144; PTHR43144; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR03542; DAPAT_plant; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Chloroplast; Plastid; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..45
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 46..461
FT /note="LL-diaminopimelate aminotransferase, chloroplastic"
FT /id="PRO_0000306914"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:18952095"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 129
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 163..164
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 164
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 187
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 244
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 244
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 275
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 302..304
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 313
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 344
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 344
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT BINDING 439
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17583737,
FT ECO:0000269|PubMed:18952095"
FT MOD_RES 305
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:18952095,
FT ECO:0000305|PubMed:17583737"
FT MUTAGEN 305
FT /note="K->N: Loss of LL-DAP-aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:18952095"
FT MUTAGEN 305
FT /note="K->Q: Loss of LL-DAP-aminotransferase activity."
FT /evidence="ECO:0000269|PubMed:18952095"
FT MUTAGEN 398
FT /note="P->S: In agd2-1; reduced activity and increased
FT resistance to pathogen."
FT /evidence="ECO:0000269|PubMed:14729919"
FT HELIX 63..67
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 73..87
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:3EI9"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 136..147
FT /evidence="ECO:0007829|PDB:3EI9"
FT TURN 148..151
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 163..174
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 189..197
FT /evidence="ECO:0007829|PDB:3EI9"
FT TURN 205..208
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:3EI9"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3EI9"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 331..341
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 348..357
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 360..386
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 395..403
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 409..420
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 427..430
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3EI9"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:3EI9"
FT HELIX 446..460
FT /evidence="ECO:0007829|PDB:3EI9"
SQ SEQUENCE 461 AA; 50396 MW; 9F49DE08EEDCEC3D CRC64;
MSSTHQLVSS MISSSSSTFL APSNFNLRTR NACLPMAKRV NTCKCVATPQ EKIEYKTKVS
RNSNMSKLQA GYLFPEIARR RSAHLLKYPD AQVISLGIGD TTEPIPEVIT SAMAKKAHEL
STIEGYSGYG AEQGAKPLRA AIAKTFYGGL GIGDDDVFVS DGAKCDISRL QVMFGSNVTI
AVQDPSYPAY VDSSVIMGQT GQFNTDVQKY GNIEYMRCTP ENGFFPDLST VGRTDIIFFC
SPNNPTGAAA TREQLTQLVE FAKKNGSIIV YDSAYAMYMS DDNPRSIFEI PGAEEVAMET
ASFSKYAGFT GVRLGWTVIP KKLLYSDGFP VAKDFNRIIC TCFNGASNIS QAGALACLTP
EGLEAMHKVI GFYKENTNII IDTFTSLGYD VYGGKNAPYV WVHFPNQSSW DVFAEILEKT
HVVTTPGSGF GPGGEGFVRV SAFGHRENIL EACRRFKQLY K
