PPDK1_MAIZE
ID PPDK1_MAIZE Reviewed; 947 AA.
AC P11155; C5IHE0; Q41846; Q41847; Q42367; Q7DMU6; Q9XGW9;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Pyruvate, phosphate dikinase 1, chloroplastic {ECO:0000303|PubMed:1668653};
DE EC=2.7.9.1 {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960, ECO:0000269|PubMed:9038349, ECO:0000269|PubMed:9287137};
DE AltName: Full=Pyruvate, orthophosphate dikinase 1;
DE Flags: Precursor;
GN Name=PPDK1 {ECO:0000303|PubMed:1668653};
GN Synonyms=C4PPDKZM1 {ECO:0000303|PubMed:1668653},
GN CYPPDKZM1 {ECO:0000303|PubMed:1668653}, PPDK2 {ECO:0000303|PubMed:2158100};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C4PPDKZM1), AND PROTEIN SEQUENCE OF
RP 71-89.
RX PubMed=2841317; DOI=10.1016/s0021-9258(18)37924-9;
RA Matsuoka M., Ozeki Y., Yamamoto N., Hirano H., Kano-Murakami Y., Tanaka Y.;
RT "Primary structure of maize pyruvate, orthophosphate dikinase as deduced
RT from cDNA sequence.";
RL J. Biol. Chem. 263:11080-11083(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2170354; DOI=10.1016/s0021-9258(17)44827-7;
RA Matsuoka M.;
RT "Structure, genetic mapping, and expression of the gene for pyruvate,
RT orthophosphate dikinase from maize.";
RL J. Biol. Chem. 265:16772-16777(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM CYPPDKZM1).
RC STRAIN=cv. LH52;
RX PubMed=19329568; DOI=10.1104/pp.108.131888;
RA Manicacci D., Camus-Kulandaivelu L., Fourmann M., Arar C., Barrault S.,
RA Rousselet A., Feminias N., Consoli L., Frances L., Mechin V., Murigneux A.,
RA Prioul J.L., Charcosset A., Damerval C.;
RT "Epistatic interactions between Opaque2 transcriptional activator and its
RT target gene CyPPDK1 control kernel trait variation in maize.";
RL Plant Physiol. 150:506-520(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-75 (ISOFORM C4PPDKZM1), ALTERNATIVE
RP PROMOTER USAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. B73;
RX PubMed=2158100; DOI=10.1073/pnas.87.8.3004;
RA Glackin C.A., Grula J.W.;
RT "Organ-specific transcripts of different size and abundance derive from the
RT same pyruvate, orthophosphate dikinase gene in maize.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:3004-3008(1990).
RN [5]
RP PROTEIN SEQUENCE OF 521-535, AND PHOSPHORYLATION AT THR-527.
RX PubMed=2834385; DOI=10.1016/s0021-9258(18)68696-x;
RA Roeske C.A., Kutny R.M., Budde R.J.A., Chollet R.;
RT "Sequence of the phosphothreonyl regulatory site peptide from inactive
RT maize leaf pyruvate, orthophosphate dikinase.";
RL J. Biol. Chem. 263:6683-6687(1988).
RN [6]
RP PROTEIN SEQUENCE OF 524-535, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT
RP THR-527.
RC STRAIN=cv. Olenka; TISSUE=Bundle sheath cell, and Mesophyll cell;
RX PubMed=22833285; DOI=10.1002/pmic.201200196;
RA Fristedt R., Wasilewska W., Romanowska E., Vener A.V.;
RT "Differential phosphorylation of thylakoid proteins in mesophyll and bundle
RT sheath chloroplasts from maize plants grown under low or high light.";
RL Proteomics 12:2852-2861(2012).
RN [7]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C4PPDKZM1 AND CYPPDKZM1),
RP MUTAGENESIS OF GLY-525 AND SER-528, ALTERNATIVE PROMOTER USAGE, FUNCTION,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=1668653; DOI=10.2307/3869364;
RA Sheen J.;
RT "Molecular mechanisms underlying the differential expression of maize
RT pyruvate, orthophosphate dikinase genes.";
RL Plant Cell 3:225-245(1991).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 868-947.
RC STRAIN=cv. B73;
RA Stapleton A.E., Walbot V.;
RT "Maize clones with putative DNA-binding activity.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP PROTEIN SEQUENCE OF 63-74, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT THR-309; SER-506; THR-527 AND SER-528, TISSUE
RP SPECIFICITY, INDUCTION BY LIGHT, ACETYLATION AT ALA-63, AND CLEAVAGE OF
RP INITIATOR METHIONINE (ISOFORM CYPPDKZM1).
RX PubMed=24710069; DOI=10.1104/pp.113.231993;
RA Chen Y.B., Lu T.C., Wang H.X., Shen J., Bu T.T., Chao Q., Gao Z.F.,
RA Zhu X.G., Wang Y.F., Wang B.C.;
RT "Posttranslational modification of maize chloroplast pyruvate
RT orthophosphate dikinase reveals the precise regulatory mechanism of its
RT enzymatic activity.";
RL Plant Physiol. 165:534-549(2014).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=16660615; DOI=10.1104/pp.62.5.826;
RA Shirahashi K., Hayakawa S., Sugiyama T.;
RT "Cold lability of pyruvate, orthophosphate dikinase in the Maize Leaf.";
RL Plant Physiol. 62:826-830(1978).
RN [11]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP MUTAGENESIS OF LEU-946.
RX PubMed=9038349; DOI=10.1016/s0014-5793(97)00015-x;
RA Ohta S., Usami S., Ueki J., Kumashiro T., Komari T., Burnell J.N.;
RT "Identification of the amino acid residues responsible for cold tolerance
RT in Flaveria brownii pyruvate,orthophosphate dikinase.";
RL FEBS Lett. 403:5-9(1997).
RN [12]
RP CATALYTIC ACTIVITY, MUTAGENESIS OF THR-527, AND COFACTOR.
RX PubMed=9287137; DOI=10.1016/s0014-5793(97)00884-3;
RA Chastain C.J., Lee M.E., Moorman M.A., Shameekumar P., Chollet R.;
RT "Site-directed mutagenesis of maize recombinant C4-pyruvate,orthophosphate
RT dikinase at the phosphorylatable target threonine residue.";
RL FEBS Lett. 413:169-173(1997).
RN [13]
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, ACTIVE SITE HIS-529, AND
RP MUTAGENESIS OF THR-527 AND HIS-529.
RX PubMed=10683263; DOI=10.1006/abbi.1999.1651;
RA Chastain C.J., Botschner M., Harrington G.E., Thompson B.J., Mills S.E.,
RA Sarath G., Chollet R.;
RT "Further analysis of maize C(4) pyruvate,orthophosphate dikinase
RT phosphorylation by its bifunctional regulatory protein using selective
RT substitutions of the regulatory Thr-456 and catalytic His-458 residues.";
RL Arch. Biochem. Biophys. 375:165-170(2000).
RN [14]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21414960; DOI=10.1093/jxb/err058;
RA Chastain C.J., Failing C.J., Manandhar L., Zimmerman M.A., Lakner M.M.,
RA Nguyen T.H.;
RT "Functional evolution of C(4) pyruvate, orthophosphate dikinase.";
RL J. Exp. Bot. 62:3083-3091(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 72-947 IN APOPROTEIN AND IN
RP COMPLEX WITH SUBSTRATE, ACTIVE SITE CYS-907, METAL BINDING AT GLU-821 AND
RP ASP-845, AND SUBSTRATE BINDING AT ARG-635; ARG-692; ASN-844 AND ASP-845.
RX PubMed=15667207; DOI=10.1021/bi0484522;
RA Nakanishi T., Nakatsu T., Matsuoka M., Sakata K., Kato H.;
RT "Crystal structures of pyruvate phosphate dikinase from maize revealed an
RT alternative conformation in the swiveling-domain motion.";
RL Biochemistry 44:1136-1144(2005).
CC -!- FUNCTION: Formation of phosphoenolpyruvate, which is the primary
CC acceptor of CO(2) in C4 and some Crassulacean acid metabolism plants.
CC {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:21414960}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC Evidence={ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:21414960,
CC ECO:0000269|PubMed:9038349};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15667207, ECO:0000305|PubMed:9287137};
CC -!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
CC Inhibited by dark-induced phosphorylation. Both reactions are catalyzed
CC by PDRP1. Inactivated by cold due to the dissociation of the
CC homotetramer. Independent of circadian regulation (PubMed:24710069).
CC {ECO:0000269|PubMed:10683263, ECO:0000269|PubMed:16660615,
CC ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:9038349}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=158 uM for pyruvate {ECO:0000269|PubMed:9038349};
CC KM=178 uM for pyruvate {ECO:0000269|PubMed:21414960};
CC KM=95 uM for ATP {ECO:0000269|PubMed:9038349};
CC KM=194 uM for phosphoenolpyruvate {ECO:0000269|PubMed:21414960};
CC KM=408 uM for phosphate {ECO:0000269|PubMed:9038349};
CC Temperature dependence:
CC Loss of activity below 10 degrees Celsius.
CC {ECO:0000269|PubMed:9038349};
CC -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:15667207}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000269|PubMed:1668653,
CC ECO:0000269|PubMed:22833285}. Cytoplasm {ECO:0000269|PubMed:1668653}.
CC Note=Isoform C4PPDKZM1 is targeted to the chloroplast while isoform
CC CYPPDKZM1 is found in the cytoplasm. Can be found associated with the
CC thylakoid membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage; Named isoforms=2;
CC Name=C4PPDKZM1 {ECO:0000303|PubMed:1668653}; Synonyms=C4PPDK
CC {ECO:0000303|PubMed:24710069};
CC IsoId=P11155-1; Sequence=Displayed;
CC Name=CYPPDKZM1 {ECO:0000303|PubMed:1668653,
CC ECO:0000303|PubMed:24710069};
CC IsoId=P11155-2; Sequence=VSP_057373;
CC -!- TISSUE SPECIFICITY: Isoform C4PPDKZM1 mainly localized in mesophyll
CC cells and only a low level is found in bundle sheath cells. Isoform
CC CYPPDKZM1 expressed in roots, stems and etiolated leaves.
CC {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:2158100,
CC ECO:0000269|PubMed:24710069}.
CC -!- INDUCTION: Isoform C4ppdkZm1 is light-inducible.
CC {ECO:0000269|PubMed:1668653, ECO:0000269|PubMed:24710069}.
CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site.
CC -!- PTM: Phosphorylation of Thr-527 in the dark inactivates the enzyme,
CC dephosphorylation upon light stimulation reactivates the enzyme
CC (PubMed:2834385). More highly phosphorylated when grown under high
CC rather than low light regimes (70 vs 900 umol photons/m-2/s). the
CC degree of phosphorylation is strictly regulated by light intensity and
CC the light/dark transition has no influence (PubMed:24710069).
CC Phosphorylated in both mesophyll and bundle sheath cells
CC (PubMed:22833285). The phosphorylation at Ser-528 may be important for
CC the phosphorylation at Thr-527 and may also be regulated by light
CC intensity (PubMed:24710069). {ECO:0000269|PubMed:22833285,
CC ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385}.
CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a
CC phosphocarrier histidine residue located on the surface of the central
CC domain. The two first partial reactions are catalyzed at an active site
CC located on the N-terminal domain, and the third partial reaction is
CC catalyzed at an active site located on the C-terminal domain. For
CC catalytic turnover, the central domain swivels from the concave surface
CC of the N-terminal domain to that of the C-terminal domain.
CC -!- MISCELLANEOUS: PubMed:1668653 shows the existence of a second gene
CC coding only for the short cytoplasmic isoform of PPDK.
CC -!- MISCELLANEOUS: [Isoform CYPPDKZM1]: Produced by alternative promoter
CC usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1
CC is removed (PubMed:24710069). {ECO:0000269|PubMed:1668653,
CC ECO:0000269|PubMed:24710069}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33495.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; J03901; AAA33495.1; ALT_FRAME; mRNA.
DR EMBL; M58656; AAA33498.1; -; Genomic_DNA.
DR EMBL; M58655; AAA33498.1; JOINED; Genomic_DNA.
DR EMBL; S46966; AAB23731.1; -; Genomic_DNA.
DR EMBL; S46965; AAB23730.1; -; Genomic_DNA.
DR EMBL; S46964; AAB23730.1; JOINED; Genomic_DNA.
DR EMBL; X14927; CAA33054.1; -; Genomic_DNA.
DR EMBL; FJ935764; ACR78549.1; -; Genomic_DNA.
DR EMBL; AF152599; AAD45281.1; -; mRNA.
DR PIR; A29225; KIZMPO.
DR PIR; PQ0190; PQ0190.
DR PDB; 1VBG; X-ray; 2.30 A; A=72-947.
DR PDB; 1VBH; X-ray; 2.30 A; A=72-947.
DR PDBsum; 1VBG; -.
DR PDBsum; 1VBH; -.
DR AlphaFoldDB; P11155; -.
DR SMR; P11155; -.
DR iPTMnet; P11155; -.
DR PaxDb; P11155; -.
DR PRIDE; P11155; -.
DR MaizeGDB; 25385; -.
DR BRENDA; 2.7.9.1; 6752.
DR SABIO-RK; P11155; -.
DR UniPathway; UPA00322; -.
DR EvolutionaryTrace; P11155; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; P11155; baseline and differential.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR018274; PEP_util_AS.
DR InterPro; IPR000121; PEP_util_C.
DR InterPro; IPR023151; PEP_util_CS.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR22931; PTHR22931; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 3.
DR PIRSF; PIRSF000853; PPDK; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
DR TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative promoter usage; ATP-binding;
KW Chloroplast; Cytoplasm; Direct protein sequencing; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Photosynthesis; Plastid;
KW Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..62
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:24710069"
FT CHAIN 63..947
FT /note="Pyruvate, phosphate dikinase 1, chloroplastic"
FT /id="PRO_0000431714"
FT REGION 21..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 529
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000269|PubMed:10683263"
FT ACT_SITE 907
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:15667207"
FT BINDING 635
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 692
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 821
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 821
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 842
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 843
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 844
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 845
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:15667207"
FT BINDING 845
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:15667207"
FT MOD_RES 63
FT /note="N-acetylalanine; partial"
FT /evidence="ECO:0000269|PubMed:24710069"
FT MOD_RES 309
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:24710069"
FT MOD_RES 506
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:24710069"
FT MOD_RES 527
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000269|PubMed:22833285,
FT ECO:0000269|PubMed:24710069, ECO:0000269|PubMed:2834385"
FT MOD_RES 528
FT /note="Phosphoserine; by PDRP1"
FT /evidence="ECO:0000269|PubMed:24710069"
FT VAR_SEQ 1..75
FT /note="MAASVSRAICVQKPGSKCTRDREATSFARRSVAAPRPPHAKAAGVIRSDSGA
FT GRGQHCSPLRAVVDAAPIQTTKK -> MAPVQCARSQ (in isoform
FT CYPPDKZM1)"
FT /id="VSP_057373"
FT MUTAGEN 525
FT /note="G->A,P: Greatly reduced activity. Strongly reduced
FT or lack of phosphorylation by PDRP1 in vitro."
FT /evidence="ECO:0000269|PubMed:24710069"
FT MUTAGEN 527
FT /note="T->D,E: Abolished activity."
FT /evidence="ECO:0000269|PubMed:10683263,
FT ECO:0000269|PubMed:9287137"
FT MUTAGEN 527
FT /note="T->N: Greatly reduced activity."
FT /evidence="ECO:0000269|PubMed:10683263,
FT ECO:0000269|PubMed:9287137"
FT MUTAGEN 527
FT /note="T->S,V: No effect on activity."
FT /evidence="ECO:0000269|PubMed:10683263,
FT ECO:0000269|PubMed:9287137"
FT MUTAGEN 527
FT /note="T->Y: Greatly reduced activity. No tyrosine
FT phosphorylation by PDRP1 in vitro."
FT /evidence="ECO:0000269|PubMed:10683263,
FT ECO:0000269|PubMed:9287137"
FT MUTAGEN 528
FT /note="S->C: No effect on activity or phosphorylation by
FT PDRP1 in vitro."
FT /evidence="ECO:0000269|PubMed:24710069"
FT MUTAGEN 528
FT /note="S->Y,T: Greatly reduced activity. Strongly reduced
FT or lack of phosphorylation by PDRP1 in vitro."
FT /evidence="ECO:0000269|PubMed:24710069"
FT MUTAGEN 529
FT /note="H->N: Abolished activity. No phosphorylation on T-
FT 527 by PDRP1 in vitro."
FT /evidence="ECO:0000269|PubMed:10683263"
FT MUTAGEN 946
FT /note="L->V: No decrease of the cold sensitivity."
FT /evidence="ECO:0000269|PubMed:9038349"
FT CONFLICT 2
FT /note="A -> T (in Ref. 2; AAA33498 and 7; AAB23730)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="Missing (in Ref. 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="R -> G (in Ref. 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="W -> G (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="S -> G (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 671
FT /note="T -> P (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..699
FT /note="HPSY -> PPLH (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="A -> V (in Ref. 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 865
FT /note="H -> Y (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 869..873
FT /note="GILQH -> EFGTS (in Ref. 8; AAD45281)"
FT /evidence="ECO:0000305"
FT CONFLICT 878
FT /note="V -> I (in Ref. 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 890
FT /note="F -> L (in Ref. 2; AAA33498 and 3; ACR78549)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="F -> Y (in Ref. 2; AAA33498, 8; AAD45281 and 3;
FT ACR78549)"
FT /evidence="ECO:0000305"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 96..107
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:1VBH"
FT HELIX 137..152
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 224..238
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 248..266
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 335..337
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 366..371
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 373..390
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 404..412
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 417..429
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 444..449
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 462..464
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 465..468
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 475..484
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 485..493
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:1VBH"
FT HELIX 510..515
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 529..536
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 552..555
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 556..559
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 562..565
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 574..577
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 594..605
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 608..613
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 617..625
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 630..635
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 636..640
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 644..655
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 659..683
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 687..692
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 707..718
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 722..732
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 737..739
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 744..749
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 751..769
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 776..781
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 787..808
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 815..820
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 823..827
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 829..832
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 833..835
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 837..841
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 843..851
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 855..857
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 858..860
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 862..867
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 875..877
FT /evidence="ECO:0007829|PDB:1VBG"
FT TURN 881..883
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 884..898
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 903..908
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 909..912
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 914..922
FT /evidence="ECO:0007829|PDB:1VBG"
FT STRAND 926..930
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:1VBG"
FT HELIX 935..944
FT /evidence="ECO:0007829|PDB:1VBG"
SQ SEQUENCE 947 AA; 102674 MW; 6D11F51D150ACFD1 CRC64;
MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KAAGVIRSDS GAGRGQHCSP
LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA NLAEMASIGL SVPPGFTVST
EACQQYQDAG CALPAGLWAE IVDGLQWVEE YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD
TVLNLGLNDE VAAGLAAKSG ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL
KNDTDLTASD LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI
NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA QGEDVVAGIR
TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV QENRLWMLQC RTGKRTGKSA
VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL LHPQFENPSA YKDQVIATGL PASPGAAVGQ
VVFTAEDAEA WHSQGKAAIL VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC
CVSGCSGIRV NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA
WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV RQMIMAPTLE
LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE FLPEGNIEDI VSELCAETGA
NQEDALARIE KLSEVNPMLG FRGCRLGISY PELTEMQARA IFEAAIAMTN QGVQVFPEIM
VPLVGTPQEL GHQVTLIRQV AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS
FGTNDLTQMT FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP
NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV
