DHQSD_ARATH
ID DHQSD_ARATH Reviewed; 603 AA.
AC Q9SQT8; Q3ZLP7; Q56ZH7; Q6NLY1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic {ECO:0000303|PubMed:16784230};
DE Short=DHQ-SDH protein {ECO:0000303|PubMed:16784230};
DE AltName: Full=DHQase-SORase {ECO:0000305};
DE AltName: Full=Protein EMBRYO DEFECTIVE 3004 {ECO:0000305};
DE Includes:
DE RecName: Full=Dehydroquinate dehydratase {ECO:0000303|PubMed:16784230};
DE Short=DHQ {ECO:0000303|PubMed:16784230};
DE EC=4.2.1.10 {ECO:0000269|PubMed:16784230};
DE Includes:
DE RecName: Full=Shikimate dehydrogenase {ECO:0000303|PubMed:16784230};
DE Short=SDH {ECO:0000303|PubMed:16784230};
DE EC=1.1.1.25 {ECO:0000269|PubMed:16784230};
DE Flags: Precursor;
GN Name=EMB3004 {ECO:0000305};
GN OrderedLocusNames=At3g06350 {ECO:0000312|Araport:AT3G06350};
GN ORFNames=F24P17.18 {ECO:0000312|EMBL:AAF08579.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Carninci P., Hayashizaki Y.,
RA Ishida J., Kamiya A., Kawai J., Narusaka M., Sakurai T., Satou M., Seki M.,
RA Shinozaki K., Ecker J.R.;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-603.
RA Muir R.M., Ingham E., Uratsu S.L., Leslie C.A., McGranahan G.H.,
RA Dandekar A.M.;
RT "Shikimate dehydrogenase: a bi-functional enzyme with a novel role in plant
RT and microbial secondary metabolism.";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-603.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 90-603 IN COMPLEX WITH SHIKIMATE,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE,
RP SUBUNIT, AND MUTAGENESIS OF SER-336; SER-338; LYS-385; ASP-423 AND TYR-550.
RX PubMed=16784230; DOI=10.1021/bi060366+;
RA Singh S.A., Christendat D.;
RT "Structure of Arabidopsis dehydroquinate dehydratase-shikimate
RT dehydrogenase and implications for metabolic channeling in the shikimate
RT pathway.";
RL Biochemistry 45:7787-7796(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 90-603 IN COMPLEX WITH
RP 3-DEHYDROSHIKIMATE AND NADP.
RX DOI=10.1021/cg7007107;
RA Singh S.A., Christendat D.;
RT "The DHQ-dehydroshikimate-SDH-shikimate-NADP(H) complex: Insights into
RT metabolite transfer in the shikimate pathway.";
RL Cryst. Growth Des. 7:2153-2160(2007).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 90-603 IN COMPLEX WITH SHIKIMATE.
RX PubMed=29890023; DOI=10.1111/tpj.13989;
RA Gritsunov A., Peek J., Diaz Caballero J., Guttman D., Christendat D.;
RT "Structural and biochemical approaches uncover multiple evolutionary
RT trajectories of plant quinate dehydrogenases.";
RL Plant J. 0:0-0(2018).
CC -!- FUNCTION: Bifunctional dehydroquinate dehydratase-shikimate
CC dehydrogenase enzyme that catalyzes two steps in the chorismate
CC biosynthesis pathway. {ECO:0000269|PubMed:16784230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O;
CC Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:32364; EC=4.2.1.10;
CC Evidence={ECO:0000269|PubMed:16784230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21097;
CC Evidence={ECO:0000269|PubMed:16784230};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH;
CC Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630,
CC ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25;
CC Evidence={ECO:0000269|PubMed:16784230};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:17739;
CC Evidence={ECO:0000269|PubMed:16784230};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=685 uM for shikimate {ECO:0000269|PubMed:16784230};
CC KM=131 uM for NADP {ECO:0000269|PubMed:16784230};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 3/7. {ECO:0000305}.
CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC 4/7. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16784230}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the type-I 3-
CC dehydroquinase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the shikimate
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AC011623; AAF08579.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74381.1; -; Genomic_DNA.
DR EMBL; BT012197; AAS76684.1; -; mRNA.
DR EMBL; AY736474; AAW63134.1; -; mRNA.
DR EMBL; AK220988; BAD94599.1; -; mRNA.
DR RefSeq; NP_187286.1; NM_111510.4.
DR PDB; 2GPT; X-ray; 1.95 A; A=90-603.
DR PDB; 2O7Q; X-ray; 2.20 A; A=90-603.
DR PDB; 2O7S; X-ray; 1.78 A; A=90-603.
DR PDB; 6BMB; X-ray; 2.08 A; A=90-603.
DR PDB; 6BMQ; X-ray; 2.08 A; A=90-603.
DR PDBsum; 2GPT; -.
DR PDBsum; 2O7Q; -.
DR PDBsum; 2O7S; -.
DR PDBsum; 6BMB; -.
DR PDBsum; 6BMQ; -.
DR AlphaFoldDB; Q9SQT8; -.
DR SMR; Q9SQT8; -.
DR BioGRID; 5144; 2.
DR STRING; 3702.AT3G06350.1; -.
DR iPTMnet; Q9SQT8; -.
DR PaxDb; Q9SQT8; -.
DR PRIDE; Q9SQT8; -.
DR ProteomicsDB; 224103; -.
DR EnsemblPlants; AT3G06350.1; AT3G06350.1; AT3G06350.
DR GeneID; 819809; -.
DR Gramene; AT3G06350.1; AT3G06350.1; AT3G06350.
DR KEGG; ath:AT3G06350; -.
DR Araport; AT3G06350; -.
DR TAIR; locus:2081036; AT3G06350.
DR eggNOG; KOG0692; Eukaryota.
DR HOGENOM; CLU_019120_0_0_1; -.
DR InParanoid; Q9SQT8; -.
DR OMA; RSMEPSN; -.
DR OrthoDB; 187464at2759; -.
DR PhylomeDB; Q9SQT8; -.
DR BioCyc; ARA:AT3G06350-MON; -.
DR BioCyc; MetaCyc:AT3G06350-MON; -.
DR BRENDA; 1.1.1.25; 399.
DR BRENDA; 4.2.1.10; 399.
DR SABIO-RK; Q9SQT8; -.
DR UniPathway; UPA00053; UER00086.
DR UniPathway; UPA00053; UER00087.
DR EvolutionaryTrace; Q9SQT8; -.
DR PRO; PR:Q9SQT8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SQT8; baseline and differential.
DR Genevisible; Q9SQT8; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IDA:TAIR.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0019632; P:shikimate metabolic process; IDA:TAIR.
DR CDD; cd00502; DHQase_I; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_00214; AroD; 1.
DR HAMAP; MF_00222; Shikimate_DH_AroE; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR001381; DHquinase_I.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR041121; SDH_C.
DR InterPro; IPR011342; Shikimate_DH.
DR InterPro; IPR013708; Shikimate_DH-bd_N.
DR InterPro; IPR022893; Shikimate_DH_fam.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR PANTHER; PTHR21089; PTHR21089; 1.
DR Pfam; PF01487; DHquinase_I; 1.
DR Pfam; PF18317; SDH_C; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR Pfam; PF08501; Shikimate_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR TIGRFAMs; TIGR01093; aroD; 1.
DR TIGRFAMs; TIGR00507; aroE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Chloroplast; Lyase; Multifunctional enzyme; NADP; Oxidoreductase; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..603
FT /note="Bifunctional 3-dehydroquinate dehydratase/shikimate
FT dehydrogenase, chloroplastic"
FT /id="PRO_0000250645"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..313
FT /note="3-dehydroquinate dehydratase"
FT REGION 328..558
FT /note="Shikimate dehydrogenase"
FT ACT_SITE 214
FT /note="Proton acceptor; for 3-dehydroquinate dehydratase
FT activity"
FT /evidence="ECO:0000305|PubMed:16784230"
FT ACT_SITE 241
FT /note="Schiff-base intermediate with substrate; for 3-
FT dehydroquinate dehydratase activity"
FT /evidence="ECO:0000305|PubMed:16784230"
FT ACT_SITE 385
FT /note="For shikimate dehydrogenase activity"
FT /evidence="ECO:0000305|PubMed:16784230"
FT ACT_SITE 423
FT /note="For shikimate dehydrogenase activity"
FT /evidence="ECO:0000305|PubMed:16784230"
FT BINDING 124
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 126
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 155
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 241
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 279
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 300
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 304
FT /ligand="3-dehydroshikimate"
FT /ligand_id="ChEBI:CHEBI:16630"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7Q"
FT BINDING 336
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 338
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 381
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 385
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 406
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 423
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 461
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 463
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 464
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 483
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 485
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 488
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 525
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 548
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 550
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 571
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PDB:2O7S"
FT BINDING 578
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT BINDING 582
FT /ligand="shikimate"
FT /ligand_id="ChEBI:CHEBI:36208"
FT /evidence="ECO:0000269|PubMed:16784230,
FT ECO:0007744|PDB:2GPT"
FT MUTAGEN 336
FT /note="S->A: 13-fold decrease in substrate affinity but
FT almost no change in activity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 338
FT /note="S->A: 10-fold decrease in activity, and 9-fold
FT decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 385
FT /note="K->A: Strongly reduced shikimate dehydrogenase
FT activity, but minor change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 385
FT /note="K->N: Strongly reduced shikimate dehydrogenase
FT activity, but no change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 423
FT /note="D->A: Loss of shikimate dehydrogenase activity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 423
FT /note="D->N: Reduced shikimate dehydrogenase activity, but
FT no change in substrate affinity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT MUTAGEN 550
FT /note="Y->F,A: 100-fold decrease in activity, and 2-fold
FT decrease in substrate affinity."
FT /evidence="ECO:0000269|PubMed:16784230"
FT CONFLICT 491
FT /note="E -> K (in Ref. 5; BAD94599)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="L -> Q (in Ref. 3; AAS76684)"
FT /evidence="ECO:0000305"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 105..118
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 135..145
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 167..180
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 189..198
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 222..233
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 282..286
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 338..348
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 352..359
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 363..369
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 397..402
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 412..414
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 423..434
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 456..459
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 486..495
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:2O7Q"
FT TURN 503..508
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 514..519
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 536..538
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 539..541
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 542..547
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 551..554
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 556..562
FT /evidence="ECO:0007829|PDB:2O7S"
FT TURN 563..565
FT /evidence="ECO:0007829|PDB:2O7S"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 571..587
FT /evidence="ECO:0007829|PDB:2O7S"
FT HELIX 593..603
FT /evidence="ECO:0007829|PDB:2O7S"
SQ SEQUENCE 603 AA; 65796 MW; 4DAAB35F594E7CB6 CRC64;
MAASSTNARL TNPPRLLSKP RLSPTSVANL RFPAADFSTR FFADSSSPRL RSVPFPVVFS
DQRRRRSMEP SNVYVASNST EMEIGSHDIV KNPSLICAPV MADSIDKMVI ETSKAHELGA
DLVEIRLDWL KDFNPLEDLK TIIKKSPLPT LFTYRPKWEG GQYEGDENER RDVLRLAMEL
GADYIDVELQ VASEFIKSID GKKPGKFKVI VSSHNYQNTP SVEDLDGLVA RIQQTGADIV
KIATTAVDIA DVARMFHITS KAQVPTIGLV MGERGLMSRI LCSKFGGYLT FGTLDSSKVS
APGQPTIKDL LDLYNFRRIG PDTKVYGIIG KPVSHSKSPI VHNQAFKSVD FNGVYVHLLV
DNLVSFLQAY SSSDFAGFSC TIPHKEAALQ CCDEVDPLAK SIGAVNTILR RKSDGKLLGY
NTDCIGSISA IEDGLRSSGD PSSVPSSSSP LASKTVVVIG AGGAGKALAY GAKEKGAKVV
IANRTYERAL ELAEAIGGKA LSLTDLDNYH PEDGMVLANT TSMGMQPNVE ETPISKDALK
HYALVFDAVY TPRITRLLRE AEESGAITVS GSEMFVRQAY EQFEIFTGLP APKELYWQIM
SKY
