KPRS_ECOLI
ID KPRS_ECOLI Reviewed; 315 AA.
AC P0A717; P08330; P76828; P78058;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:6290219};
DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:6290219};
DE EC=2.7.6.1 {ECO:0000269|PubMed:2542328, ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:6290219, ECO:0000269|PubMed:8679571, ECO:0000305|PubMed:10954724, ECO:0000305|PubMed:7657655, ECO:0000305|PubMed:9125530};
DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:6290219};
DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583};
DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583};
GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:6290219};
GN Synonyms=prsA; OrderedLocusNames=b1207, JW1198;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND
RP COFACTOR.
RX PubMed=3009477; DOI=10.1016/s0021-9258(19)62682-7;
RA Hove-Jensen B., Harlow K.W., King C.J., Switzer R.L.;
RT "Phosphoribosylpyrophosphate synthetase of Escherichia coli. Properties of
RT the purified enzyme and primary structure of the prs gene.";
RL J. Biol. Chem. 261:6765-6771(1986).
RN [2]
RP SEQUENCE REVISION TO 127, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, ACTIVITY REGULATION, AND MUTANT PRSA1.
RX PubMed=2542328; DOI=10.1016/s0021-9258(18)81798-7;
RA Bower S.G., Harlow K.W., Switzer R.L., Hove-Jensen B.;
RT "Characterization of the Escherichia coli prsA1-encoded mutant
RT phosphoribosylpyrophosphate synthetase identifies a divalent cation-
RT nucleotide binding site.";
RL J. Biol. Chem. 264:10287-10291(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, ACTIVITY REGULATION,
RP AND NOMENCLATURE.
RX PubMed=6290219; DOI=10.1111/j.1432-1033.1982.tb06782.x;
RA Hove-Jensen B., Nygaard P.;
RT "Phosphoribosylpyrophosphate synthetase of Escherichia coli, Identification
RT of a mutant enzyme.";
RL Eur. J. Biochem. 126:327-332(1982).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND ACTIVE SITE.
RX PubMed=7657655; DOI=10.1074/jbc.270.35.20730;
RA Hilden I., Hove-Jensen B., Harlow K.W.;
RT "Inactivation of Escherichia coli phosphoribosylpyrophosphate synthetase by
RT the 2',3'-dialdehyde derivative of ATP. Identification of active site
RT lysines.";
RL J. Biol. Chem. 270:20730-20736(1995).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-220; ASP-221 AND ASP-224,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=8679571; DOI=10.1021/bi9528560;
RA Willemoes M., Nilsson D., Hove-Jensen B.;
RT "Effects of mutagenesis of aspartic acid residues in the putative
RT phosphoribosyl diphosphate binding site of Escherichia coli phosphoribosyl
RT diphosphate synthetase on metal ion specificity and ribose 5-phosphate
RT binding.";
RL Biochemistry 35:8181-8186(1996).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=9125530; DOI=10.1021/bi962610a;
RA Willemoes M., Hove-Jensen B.;
RT "Binding of divalent magnesium by Escherichia coli phosphoribosyl
RT diphosphate synthetase.";
RL Biochemistry 36:5078-5083(1997).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=10954724; DOI=10.1074/jbc.m006346200;
RA Willemoes M., Hove-Jensen B., Larsen S.;
RT "Steady state kinetic model for the binding of substrates and allosteric
RT effectors to Escherichia coli phosphoribosyl-diphosphate synthase.";
RL J. Biol. Chem. 275:35408-35412(2000).
RN [12]
RP REVIEW, AND COFACTOR.
RX PubMed=28031352; DOI=10.1128/mmbr.00040-16;
RA Hove-Jensen B., Andersen K.R., Kilstrup M., Martinussen J., Switzer R.L.,
RA Willemoes M.;
RT "Phosphoribosyl diphosphate (PRPP): biosynthesis, enzymology, utilization,
RT and metabolic significance.";
RL Microbiol. Mol. Biol. Rev. 81:E00040-E00040(2017).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 2-315 IN COMPLEX WITH MAGNESIUM
RP IONS, AND COFACTOR.
RA Timofeev V.I., Abramchik Y.A., Muravieva T.I., Iaroslavtceva A.K.,
RA Stepanenko V.N., Zhukhlistova N.E., Esipov R.S., Kuranova I.P.;
RT "Crystal structure of the phosphoribosylpyrophosphate synthetase from E.
RT Coli.";
RL Submitted (JAN-2015) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of the central metabolite
CC phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of
CC pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-
CC 5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10954724,
CC ECO:0000269|PubMed:2542328, ECO:0000269|PubMed:3009477,
CC ECO:0000269|PubMed:6290219, ECO:0000269|PubMed:7657655,
CC ECO:0000269|PubMed:8679571, ECO:0000269|PubMed:9125530}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose 5-phosphate = 5-phospho-alpha-D-ribose 1-
CC diphosphate + AMP + H(+); Xref=Rhea:RHEA:15609, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58017, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:456215; EC=2.7.6.1; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00583, ECO:0000269|PubMed:2542328,
CC ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:6290219,
CC ECO:0000269|PubMed:8679571, ECO:0000305|PubMed:10954724,
CC ECO:0000305|PubMed:7657655, ECO:0000305|PubMed:9125530};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328,
CC ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:8679571,
CC ECO:0000269|PubMed:9125530, ECO:0000305|Ref.13};
CC Note=Binds 2 Mg(2+) ions per subunit (Probable). Mn(2+), Co(2+) and
CC Cd(2+) are also accepted (PubMed:3009477, PubMed:2542328,
CC PubMed:8679571, PubMed:9125530, PubMed:10954724).
CC {ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328,
CC ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:8679571,
CC ECO:0000269|PubMed:9125530, ECO:0000303|PubMed:28031352};
CC -!- ACTIVITY REGULATION: Activated by inorganic phosphate (PubMed:3009477,
CC PubMed:10954724). In addition to form a complex with ATP, Mg(2+) also
CC acts as a cofactor (PubMed:9125530). Strongly inhibited by ADP through
CC competitive binding at the activation site and at a specific allosteric
CC site (PubMed:3009477, PubMed:6290219,PubMed:9125530). Competitively
CC inhibited by Ca(2+) and ribose 1,5-bisphosphate (Rib-1,5-P2)
CC (PubMed:2542328, PubMed:9125530). Less strongly inhibited by AMP,
CC alpha,beta-methylene ATP (mATP), (2',3'-dialdehyde)-ATP (oATP) and 1-
CC alpha,2-alpha,3-alpha-trihydroxy-4-beta-cyclopentanemethanol 5-
CC phosphate (cRib-5-P) (PubMed:2542328, PubMed:7657655, PubMed:9125530).
CC {ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328,
CC ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:6290219,
CC ECO:0000269|PubMed:7657655, ECO:0000269|PubMed:9125530}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=138 uM for Rib-5-P (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:3009477};
CC KM=230 uM for ATP (at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2542328};
CC KM=280 uM for Rib-5-P (at pH 8.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:8679571};
CC KM=300 uM for Rib-5-P (with 20 mM ATP at pH 8 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:2542328};
CC Vmax=129 umol/min/mg enzyme toward Rib-5-P (at pH 8.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:8679571};
CC Vmax=143 umol/min/mg enzyme toward ATP (at pH 8.5 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:8679571};
CC pH dependence:
CC Optimum pH is 9.7-9.8. {ECO:0000269|PubMed:3009477};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route I): step 1/1. {ECO:0000255|HAMAP-
CC Rule:MF_00583, ECO:0000305|PubMed:8679571}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- INTERACTION:
CC P0A717; P0A6F5: groEL; NbExp=2; IntAct=EBI-906827, EBI-543750;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to grow on
CC nucleosides as purine source. {ECO:0000269|PubMed:6290219}.
CC -!- MISCELLANEOUS: This enzyme uses a steady state ordered mechanism, where
CC Mg(2+) binds first, followed by Mg-ATP and lastly, ribose 5-phosphate.
CC {ECO:0000269|PubMed:10954724}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC Class I subfamily. {ECO:0000255|HAMAP-Rule:MF_00583,
CC ECO:0000303|PubMed:28031352}.
CC -!- CAUTION: Although Mg(2+) has been found in crystallography study, the
CC positions do not correspond to the correct residues.
CC {ECO:0000303|PubMed:28031352, ECO:0000305|Ref.13}.
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DR EMBL; M13174; AAA24431.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74291.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36065.1; -; Genomic_DNA.
DR PIR; D64867; KIECRY.
DR RefSeq; NP_415725.1; NC_000913.3.
DR RefSeq; WP_001298109.1; NZ_STEB01000023.1.
DR PDB; 4S2U; X-ray; 2.71 A; A=2-315.
DR PDBsum; 4S2U; -.
DR AlphaFoldDB; P0A717; -.
DR SMR; P0A717; -.
DR BioGRID; 4260813; 58.
DR DIP; DIP-35839N; -.
DR IntAct; P0A717; 155.
DR STRING; 511145.b1207; -.
DR jPOST; P0A717; -.
DR PaxDb; P0A717; -.
DR PRIDE; P0A717; -.
DR EnsemblBacteria; AAC74291; AAC74291; b1207.
DR EnsemblBacteria; BAA36065; BAA36065; BAA36065.
DR GeneID; 67417475; -.
DR GeneID; 945772; -.
DR KEGG; ecj:JW1198; -.
DR KEGG; eco:b1207; -.
DR PATRIC; fig|511145.12.peg.1255; -.
DR EchoBASE; EB0767; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_2_0_6; -.
DR InParanoid; P0A717; -.
DR OMA; FGWARQD; -.
DR PhylomeDB; P0A717; -.
DR BioCyc; EcoCyc:PRPPSYN-MON; -.
DR BioCyc; MetaCyc:PRPPSYN-MON; -.
DR BRENDA; 2.7.6.1; 2026.
DR UniPathway; UPA00087; UER00172.
DR PRO; PR:P0A717; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0042301; F:phosphate ion binding; IDA:EcoCyc.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IDA:EcoCyc.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IMP:EcoCyc.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034214; P:protein hexamerization; IDA:EcoCyc.
DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central.
DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR HAMAP; MF_00583_B; RibP_PPkinase_B; 1.
DR InterPro; IPR000842; PRib_PP_synth_CS.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR InterPro; IPR037515; Rib-P_diPkinase_bac.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
DR PROSITE; PS00114; PRPP_SYNTHASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Manganese; Metal-binding;
KW Nucleotide biosynthesis; Nucleotide-binding; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3009477,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 2..315
FT /note="Ribose-phosphate pyrophosphokinase"
FT /id="PRO_0000141134"
FT ACT_SITE 194
FT /evidence="ECO:0000305|PubMed:7657655"
FT BINDING 37..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 96..97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 170
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 196
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 220
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT BINDING 224..228
FT /ligand="D-ribose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:78346"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00583"
FT VARIANT 129
FT /note="D -> A (in mutant PRSA1; alters the binding of
FT divalent cations, especially magnesium. Little alteration
FT in the affinity for ribose 5-phosphate and 27-fold decrease
FT of the affinity for ATP. Absence of inhibition by AMP)"
FT /evidence="ECO:0000269|PubMed:2542328"
FT MUTAGEN 220
FT /note="D->E: 4-fold decrease in the affinity binding for
FT Rib-5-P in the presence of magnesium ions. In the presence
FT of cobalt ions, it shows a 15-fold decrease in the affinity
FT binding for Rib-5-P."
FT /evidence="ECO:0000269|PubMed:8679571"
FT MUTAGEN 220
FT /note="D->F: With magnesium or manganese ions, the affinity
FT binding values for ATP and Rib-5-P are comparable to those
FT of the wild-type."
FT /evidence="ECO:0000269|PubMed:8679571"
FT MUTAGEN 221
FT /note="D->A: The affinity binding for ATP is comparable to
FT those of the wild-type, apart from a slight decrease in the
FT presence of manganese ions. The affinity binding for Rib-5-
FT P is greatly decreased in the presence of both manganese
FT and cobalt ions but only about 2-fold in the presence of
FT magnesium ions."
FT /evidence="ECO:0000269|PubMed:8679571"
FT MUTAGEN 224
FT /note="D->A: With magnesium or manganese ions, the affinity
FT binding values for ATP and Rib-5-P are comparable to those
FT of the wild-type."
FT /evidence="ECO:0000269|PubMed:8679571"
FT MUTAGEN 224
FT /note="D->S: With magnesium or manganese ions, the affinity
FT binding values for ATP and Rib-5-P are comparable to those
FT of the wild-type."
FT /evidence="ECO:0000269|PubMed:8679571"
FT CONFLICT 127
FT /note="T -> I (in Ref. 1; AAA24431)"
FT /evidence="ECO:0000305"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 13..22
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 63..78
FT /evidence="ECO:0007829|PDB:4S2U"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 124..129
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 174..183
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 216..226
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 227..238
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 257..262
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 267..275
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:4S2U"
FT STRAND 285..290
FT /evidence="ECO:0007829|PDB:4S2U"
FT HELIX 293..302
FT /evidence="ECO:0007829|PDB:4S2U"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:4S2U"
SQ SEQUENCE 315 AA; 34218 MW; 4D69B7D118F93720 CRC64;
MPDMKLFAGN ATPELAQRIA NRLYTSLGDA AVGRFSDGEV SVQINENVRG GDIFIIQSTC
APTNDNLMEL VVMVDALRRA SAGRITAVIP YFGYARQDRR VRSARVPITA KVVADFLSSV
GVDRVLTVDL HAEQIQGFFD VPVDNVFGSP ILLEDMLQLN LDNPIVVSPD IGGVVRARAI
AKLLNDTDMA IIDKRRPRAN VSQVMHIIGD VAGRDCVLVD DMIDTGGTLC KAAEALKERG
AKRVFAYATH PIFSGNAANN LRNSVIDEVV VCDTIPLSDE IKSLPNVRTL TLSGMLAEAI
RRISNEESIS AMFEH
