SERB1_ARATH
ID SERB1_ARATH Reviewed; 430 AA.
AC Q96255; Q1EBU1; Q8L7P0; Q8LBA3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Phosphoserine aminotransferase 1, chloroplastic {ECO:0000303|PubMed:16289358, ECO:0000303|PubMed:9881164};
DE Short=AtPSAT1 {ECO:0000303|PubMed:16289358, ECO:0000303|PubMed:9881164};
DE EC=2.6.1.52 {ECO:0000269|PubMed:16289358, ECO:0000269|PubMed:9881164};
DE AltName: Full=Phosphohydroxythreonine aminotransferase {ECO:0000303|PubMed:16289358};
DE Flags: Precursor;
GN Name=PSAT1 {ECO:0000303|PubMed:16289358, ECO:0000303|PubMed:9881164};
GN OrderedLocusNames=At4g35630 {ECO:0000312|Araport:AT4G35630};
GN ORFNames=F8D20.140 {ECO:0000312|EMBL:CAA20033.1};
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND PATHWAY.
RC STRAIN=cv. Columbia;
RX PubMed=9881164; DOI=10.1046/j.1365-313x.1998.00313.x;
RA Ho C.-L., Noji M., Saito M., Yamazaki M., Saito K.;
RT "Molecular characterization of plastidic phosphoserine aminotransferase in
RT serine biosynthesis from Arabidopsis.";
RL Plant J. 16:443-452(1998).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND PATHWAY.
RX PubMed=16289358; DOI=10.1016/j.molbiopara.2005.09.008;
RA Ali V., Nozaki T.;
RT "Biochemical and functional characterization of phosphoserine
RT aminotransferase from Entamoeba histolytica, which possesses both
RT phosphorylated and non-phosphorylated serine metabolic pathways.";
RL Mol. Biochem. Parasitol. 145:71-83(2006).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-52, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER CYS-51, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP INDUCTION BY PATHOGEN.
RC STRAIN=cv. Columbia;
RX PubMed=24368794; DOI=10.1105/tpc.113.118992;
RA Benstein R.M., Ludewig K., Wulfert S., Wittek S., Gigolashvili T.,
RA Frerigmann H., Gierth M., Fluegge U.I., Krueger S.;
RT "Arabidopsis phosphoglycerate dehydrogenase1 of the phosphoserine pathway
RT is essential for development and required for ammonium assimilation and
RT tryptophan biosynthesis.";
RL Plant Cell 25:5011-5029(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.57 ANGSTROMS) OF 72-430 IN COMPLEX WITH PYRIDOXAL
RP PHOSPHATE, SUBUNIT, AND COFACTOR.
RX PubMed=30034403; DOI=10.3389/fpls.2018.00876;
RA Sekula B., Ruszkowski M., Dauter Z.;
RT "Structural Analysis of Phosphoserine Aminotransferase (Isoform 1) From
RT Arabidopsis thaliana- the Enzyme Involved in the Phosphorylated Pathway of
RT Serine Biosynthesis.";
RL Front. Plant Sci. 9:876-876(2018).
CC -!- FUNCTION: Involved in the plastidial phosphorylated pathway of serine
CC biosynthesis (PPSB). Catalyzes the reversible conversion of 3-
CC phosphohydroxypyruvate to phosphoserine. {ECO:0000269|PubMed:16289358,
CC ECO:0000269|PubMed:9881164}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate +
CC L-glutamate; Xref=Rhea:RHEA:14329, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:18110, ChEBI:CHEBI:29985, ChEBI:CHEBI:57524; EC=2.6.1.52;
CC Evidence={ECO:0000269|PubMed:16289358, ECO:0000269|PubMed:9881164};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-(phosphooxy)-L-threonine = (R)-3-hydroxy-2-
CC oxo-4-phosphooxybutanoate + L-glutamate; Xref=Rhea:RHEA:16573,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:58452,
CC ChEBI:CHEBI:58538; EC=2.6.1.52;
CC Evidence={ECO:0000269|PubMed:16289358, ECO:0000269|PubMed:9881164};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:30034403};
CC Note=Binds 1 pyridoxal phosphate per subunit.
CC {ECO:0000269|PubMed:30034403};
CC -!- ACTIVITY REGULATION: Inhibited by high concentration of cysteine and by
CC 3-phosphonooxypyruvate. Not inhibited by serine, threonine, valine,
CC glycine, tryptophan and O-acetyl-L-serine.
CC {ECO:0000269|PubMed:16289358, ECO:0000269|PubMed:9881164}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5050 uM for L-glutamate {ECO:0000269|PubMed:16289358};
CC KM=70 uM for L-glutamate {ECO:0000269|PubMed:9881164};
CC KM=79.7 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:16289358};
CC KM=5 uM for 3-phosphonooxypyruvate {ECO:0000269|PubMed:9881164};
CC KM=22.5 uM for O-phospho-L-serine {ECO:0000269|PubMed:16289358};
CC KM=65.1 uM for 2-oxoglutarate {ECO:0000269|PubMed:16289358};
CC Vmax=9.65 umol/min/mg enzyme toward 3-phosphonooxypyruvate
CC {ECO:0000269|PubMed:16289358};
CC Vmax=21.22 umol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:16289358};
CC Vmax=0.47 umol/min/mg enzyme toward O-phospho-L-serine
CC {ECO:0000269|PubMed:16289358};
CC Vmax=0.74 umol/min/mg enzyme toward 2-oxoglutarate
CC {ECO:0000269|PubMed:16289358};
CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine from
CC 3-phospho-D-glycerate: step 2/3. {ECO:0000269|PubMed:16289358,
CC ECO:0000269|PubMed:9881164}.
CC -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis;
CC pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
CC {ECO:0000269|PubMed:16289358, ECO:0000269|PubMed:9881164}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30034403}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:9881164}.
CC -!- TISSUE SPECIFICITY: Ubiquitous, but expressed preferentially in light-
CC grown roots and shoots. Detected in root meristems and in root tissues
CC surrounding the vascular bundle. {ECO:0000269|PubMed:9881164}.
CC -!- INDUCTION: Up-regulated upon necrotrophic pathogen infection.
CC {ECO:0000269|PubMed:24368794}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. SerC subfamily. {ECO:0000305}.
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DR EMBL; D88541; BAA13640.1; -; mRNA.
DR EMBL; AB010408; BAA24441.1; -; Genomic_DNA.
DR EMBL; AL031135; CAA20033.1; -; Genomic_DNA.
DR EMBL; AL161587; CAB80279.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86542.1; -; Genomic_DNA.
DR EMBL; AY128340; AAM91543.1; -; mRNA.
DR EMBL; BT025993; ABG25082.1; -; mRNA.
DR EMBL; AY087331; AAM64881.1; -; mRNA.
DR PIR; T04668; T04668.
DR RefSeq; NP_195288.1; NM_119728.2.
DR PDB; 6CZX; X-ray; 1.57 A; A/B/C/D=72-430.
DR PDB; 6CZY; X-ray; 1.75 A; A/B/C/D=72-430.
DR PDB; 6CZZ; X-ray; 1.70 A; A/B/C/D=72-430.
DR PDBsum; 6CZX; -.
DR PDBsum; 6CZY; -.
DR PDBsum; 6CZZ; -.
DR AlphaFoldDB; Q96255; -.
DR SMR; Q96255; -.
DR BioGRID; 14997; 13.
DR STRING; 3702.AT4G35630.1; -.
DR iPTMnet; Q96255; -.
DR PaxDb; Q96255; -.
DR PRIDE; Q96255; -.
DR ProMEX; Q96255; -.
DR ProteomicsDB; 234484; -.
DR EnsemblPlants; AT4G35630.1; AT4G35630.1; AT4G35630.
DR GeneID; 829715; -.
DR Gramene; AT4G35630.1; AT4G35630.1; AT4G35630.
DR KEGG; ath:AT4G35630; -.
DR Araport; AT4G35630; -.
DR TAIR; locus:2127963; AT4G35630.
DR eggNOG; KOG2790; Eukaryota.
DR HOGENOM; CLU_034866_0_2_1; -.
DR InParanoid; Q96255; -.
DR OMA; GYRASMY; -.
DR OrthoDB; 1357311at2759; -.
DR PhylomeDB; Q96255; -.
DR BioCyc; ARA:AT4G35630-MON; -.
DR BioCyc; MetaCyc:AT4G35630-MON; -.
DR BRENDA; 2.6.1.52; 399.
DR SABIO-RK; Q96255; -.
DR UniPathway; UPA00135; UER00197.
DR UniPathway; UPA00244; UER00311.
DR PRO; PR:Q96255; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q96255; baseline and differential.
DR Genevisible; Q96255; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central.
DR CDD; cd00611; PSAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00160; SerC_aminotrans_5; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR InterPro; IPR022278; Pser_aminoTfrase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43247; PTHR43247; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR01364; serC_1; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Aminotransferase;
KW Chloroplast; Plastid; Pyridoxal phosphate; Reference proteome;
KW Serine biosynthesis; Transferase; Transit peptide.
FT TRANSIT 1..51
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 52..430
FT /note="Phosphoserine aminotransferase 1, chloroplastic"
FT /id="PRO_0000001282"
FT BINDING 111
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250"
FT BINDING 145..146
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT BINDING 171
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZZ"
FT BINDING 221
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT BINDING 264
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT BINDING 306..307
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT MOD_RES 52
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 265
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:30034403,
FT ECO:0007744|PDB:6CZY, ECO:0007744|PDB:6CZZ"
FT CONFLICT 41
FT /note="V -> A (in Ref. 6; AAM64881)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="Q -> R (in Ref. 4; AAM91543)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="M -> I (in Ref. 6; AAM64881)"
FT /evidence="ECO:0000305"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 113..130
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 136..143
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:6CZZ"
FT STRAND 212..220
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 234..241
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 243..247
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 263..267
FT /evidence="ECO:0007829|PDB:6CZZ"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 295..300
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 301..303
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 310..325
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 329..348
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 349..352
FT /evidence="ECO:0007829|PDB:6CZZ"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 365..374
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 378..387
FT /evidence="ECO:0007829|PDB:6CZX"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:6CZX"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:6CZX"
FT HELIX 412..429
FT /evidence="ECO:0007829|PDB:6CZX"
SQ SEQUENCE 430 AA; 47359 MW; B3225CC8DE78BDE2 CRC64;
MAATTNSFLV GSNNTQIPAL KPKSSSQSFL HLSKPNTVNF VSKTKPVAVR CVASTTQVQD
GVRSGSVGSQ ERVFNFAAGP ATLPENVLLK AQADLYNWRG SGMSVMEMSH RGKEFLSIIQ
KAESDLRQLL EIPQEYSVLF LQGGATTQFA ALPLNLCKSD DTVDFVVTGS WGDKAVKEAK
KYCKTNVIWS GKSEKYTKVP SFEELEQTPD AKYLHICANE TIHGVEFKDY PVPKNGFLVA
DMSSNFCSKP VDVSKFGVIY GGAQKNVGPS GVTIVIIRKD LIGNAQDITP VMLDYKIHDE
NSSLYNTPPC FGIYMCGLVF EDLLEQGGLK EVEKKNQRKA DLLYNAIEES NGFFRCPVEK
SVRSLMNVPF TLEKSELEAE FIKEAAKEKM VQLKGHRSVG GMRASIYNAM PLAGVEKLVA
FMKDFQAKHA
