RBSK_ECOLI
ID RBSK_ECOLI Reviewed; 309 AA.
AC P0A9J6; P05054; Q2M870;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Ribokinase {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000303|PubMed:3011794};
DE Short=RK {ECO:0000255|HAMAP-Rule:MF_01987};
DE EC=2.7.1.15 {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:11563694, ECO:0000269|PubMed:3011794};
GN Name=rbsK {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000303|PubMed:3011794};
GN OrderedLocusNames=b3752, JW3731;
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 1-21 AND 297-309,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12;
RX PubMed=3011794; DOI=10.1016/s0021-9258(19)57450-6;
RA Hope J.N., Bell A.W., Hermodson M.A., Groarke J.M.;
RT "Ribokinase from Escherichia coli K12. Nucleotide sequence and
RT overexpression of the rbsK gene and purification of ribokinase.";
RL J. Biol. Chem. 261:7663-7668(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [3]
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 [4]
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 [5]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=9385653; DOI=10.1002/pro.5560061124;
RA Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L.;
RT "Purification, characterization, and crystallization of Escherichia coli
RT ribokinase.";
RL Protein Sci. 6:2474-2476(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11563694; DOI=10.1023/a:1011081508171;
RA Maj M.C., Gupta R.S.;
RT "The effect of inorganic phosphate on the activity of bacterial
RT ribokinase.";
RL J. Protein Chem. 20:139-144(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND
RP ACTIVITY REGULATION.
RX PubMed=16784868; DOI=10.1016/j.bmc.2006.05.057;
RA Chuvikovsky D.V., Esipov R.S., Skoblov Y.S., Chupova L.A., Muravyova T.I.,
RA Miroshnikov A.I., Lapinjoki S., Mikhailopulo I.A.;
RT "Ribokinase from E. coli: expression, purification, and substrate
RT specificity.";
RL Bioorg. Med. Chem. 14:6327-6332(2006).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH AMP-PNP AND RIBOSE.
RC STRAIN=K12;
RX PubMed=9519409; DOI=10.1016/s0969-2126(98)00020-3;
RA Sigrell J.A., Cameron A.D., Jones T.A., Mowbray S.L.;
RT "Structure of Escherichia coli ribokinase in complex with ribose and
RT dinucleotide determined to 1.8-A resolution: insights into a new family of
RT kinase structures.";
RL Structure 6:183-193(1998).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH ADP; MAGNESIUM AND
RP RIBOSE.
RX PubMed=10438599; DOI=10.1006/jmbi.1999.2938;
RA Sigrell J.A., Cameron A.D., Mowbray S.L.;
RT "Induced fit on sugar binding activates ribokinase.";
RL J. Mol. Biol. 290:1009-1018(1999).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.34 ANGSTROMS) IN COMPLEX WITH ATP ANALOG; CESIUM
RP AND RIBOSE, AND ACTIVITY REGULATION.
RX PubMed=11786021; DOI=10.1006/jmbi.2001.5248;
RA Andersson C.E., Mowbray S.L.;
RT "Activation of ribokinase by monovalent cations.";
RL J. Mol. Biol. 315:409-419(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction
CC requiring ATP and magnesium. The resulting D-ribose-5-phosphate can
CC then be used either for sythesis of nucleotides, histidine, and
CC tryptophan, or as a component of the pentose phosphate pathway.
CC {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:11563694,
CC ECO:0000269|PubMed:3011794}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribose = ADP + D-ribose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:13697, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:47013, ChEBI:CHEBI:78346, ChEBI:CHEBI:456216;
CC EC=2.7.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01987,
CC ECO:0000269|PubMed:11563694, ECO:0000269|PubMed:16784868,
CC ECO:0000269|PubMed:3011794};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01987,
CC ECO:0000269|PubMed:16784868, ECO:0000305|PubMed:11786021};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:16784868};
CC Note=Requires a divalent cation, most likely magnesium in vivo, as an
CC electrophilic catalyst to aid phosphoryl group transfer. It is the
CC chelate of the metal and the nucleotide that is the actual substrate
CC (Probable). Also active with manganase (PubMed:16784868).
CC {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:16784868,
CC ECO:0000305|PubMed:11786021};
CC -!- ACTIVITY REGULATION: Activated by a monovalent cation that binds near,
CC but not in, the active site (PubMed:11786021). The most likely occupant
CC of the site in vivo is potassium (PubMed:16784868, PubMed:11786021).
CC Also activated by ammonium ion (PubMed:16784868). Ion binding induces a
CC conformational change that may alter substrate affinity (Probable).
CC {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:11786021,
CC ECO:0000269|PubMed:16784868, ECO:0000305|PubMed:11786021}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.213 mM for ATP {ECO:0000269|PubMed:16784868};
CC KM=0.279 mM for D-ribose {ECO:0000269|PubMed:16784868};
CC KM=1.41 mM for 2-deoxy-D-ribose {ECO:0000269|PubMed:16784868};
CC KM=32 mM for D-arabinose {ECO:0000269|PubMed:16784868};
CC KM=31.6 mM for D-xylose {ECO:0000269|PubMed:16784868};
CC KM=8.2 mM for D-fructose {ECO:0000269|PubMed:16784868};
CC KM=0.65 mM for ribose (at pH 6.2 in the presence of 0 mM inorganic
CC phosphate) {ECO:0000269|PubMed:11563694};
CC KM=0.43 mM for ribose (at pH 6.2 in the presence of 0.5 mM inorganic
CC phosphate) {ECO:0000269|PubMed:11563694};
CC KM=0.27 mM for ribose (at pH 6.2 in the presence of 1 mM inorganic
CC phosphate) {ECO:0000269|PubMed:11563694};
CC KM=0.23 mM for ribose (at pH 6.2 in the presence of 5 mM inorganic
CC phosphate) {ECO:0000269|PubMed:11563694};
CC KM=0.21 mM for ribose (at pH 6.2 in the presence of 20 mM inorganic
CC phosphate) {ECO:0000269|PubMed:11563694};
CC Vmax=122 umol/min/mg enzyme toward ATP {ECO:0000269|PubMed:16784868};
CC Vmax=81 umol/min/mg enzyme toward D-ribose
CC {ECO:0000269|PubMed:16784868};
CC Vmax=25 umol/min/mg enzyme toward 2-deoxy-D-ribose
CC {ECO:0000269|PubMed:16784868};
CC Vmax=0.6 umol/min/mg enzyme toward D-arabinose
CC {ECO:0000269|PubMed:16784868};
CC Vmax=0.86 umol/min/mg enzyme toward D-xylose
CC {ECO:0000269|PubMed:16784868};
CC Vmax=0.226 umol/min/mg enzyme toward D-fructose
CC {ECO:0000269|PubMed:16784868};
CC Vmax=7.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 0 mM
CC inorganic phosphate) {ECO:0000269|PubMed:11563694};
CC Vmax=32.0 pmol/min/mg enzyme (at pH 6.2 in the presence of 0.5 mM
CC inorganic phosphate) {ECO:0000269|PubMed:11563694};
CC Vmax=59.6 pmol/min/mg enzyme (at pH 6.2 in the presence of 1 mM
CC inorganic phosphate) {ECO:0000269|PubMed:11563694};
CC Vmax=139.4 pmol/min/mg enzyme (at pH 6.2 in the presence of 5 mM
CC inorganic phosphate) {ECO:0000269|PubMed:11563694};
CC Vmax=172.4 pmol/min/mg enzyme (at pH 6.2 in the presence of 20 mM
CC inorganic phosphate) {ECO:0000269|PubMed:11563694};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:16784868};
CC Temperature dependence:
CC Optimum temperature is 30-50 degrees Celsius.
CC {ECO:0000269|PubMed:16784868};
CC -!- PATHWAY: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-
CC phosphate from beta-D-ribopyranose: step 2/2. {ECO:0000255|HAMAP-
CC Rule:MF_01987, ECO:0000305|PubMed:3011794}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01987,
CC ECO:0000269|PubMed:9385653}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01987,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. Ribokinase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01987}.
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DR EMBL; M13169; AAA51476.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62105.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76775.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77536.1; -; Genomic_DNA.
DR PIR; A26305; KIECRB.
DR RefSeq; NP_418208.1; NC_000913.3.
DR RefSeq; WP_001300603.1; NZ_STEB01000015.1.
DR PDB; 1GQT; X-ray; 2.34 A; A/B/C/D=1-309.
DR PDB; 1RK2; X-ray; 2.25 A; A/B/C/D=1-309.
DR PDB; 1RKA; X-ray; 2.30 A; A=1-309.
DR PDB; 1RKD; X-ray; 1.84 A; A=1-309.
DR PDB; 1RKS; X-ray; 2.40 A; A=1-309.
DR PDBsum; 1GQT; -.
DR PDBsum; 1RK2; -.
DR PDBsum; 1RKA; -.
DR PDBsum; 1RKD; -.
DR PDBsum; 1RKS; -.
DR AlphaFoldDB; P0A9J6; -.
DR SMR; P0A9J6; -.
DR BioGRID; 4259582; 11.
DR DIP; DIP-36178N; -.
DR IntAct; P0A9J6; 3.
DR STRING; 511145.b3752; -.
DR BindingDB; P0A9J6; -.
DR ChEMBL; CHEMBL5093; -.
DR DrugBank; DB03909; Adenosine-5'-[Beta, Gamma-Methylene]Triphosphate.
DR DrugBank; DB01936; alpha-D-arabinofuranose.
DR DrugBank; DB04444; Tetrafluoroaluminate Ion.
DR jPOST; P0A9J6; -.
DR PaxDb; P0A9J6; -.
DR PRIDE; P0A9J6; -.
DR DNASU; 948260; -.
DR EnsemblBacteria; AAC76775; AAC76775; b3752.
DR EnsemblBacteria; BAE77536; BAE77536; BAE77536.
DR GeneID; 66672344; -.
DR GeneID; 948260; -.
DR KEGG; ecj:JW3731; -.
DR KEGG; eco:b3752; -.
DR PATRIC; fig|1411691.4.peg.2948; -.
DR EchoBASE; EB0811; -.
DR eggNOG; COG0524; Bacteria.
DR HOGENOM; CLU_027634_2_0_6; -.
DR InParanoid; P0A9J6; -.
DR OMA; IPWRDEL; -.
DR PhylomeDB; P0A9J6; -.
DR BioCyc; EcoCyc:RIBOKIN-MON; -.
DR BioCyc; MetaCyc:RIBOKIN-MON; -.
DR BRENDA; 2.7.1.15; 2026.
DR UniPathway; UPA00916; UER00889.
DR EvolutionaryTrace; P0A9J6; -.
DR PRO; PR:P0A9J6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0004747; F:ribokinase activity; IDA:EcoCyc.
DR GO; GO:0019303; P:D-ribose catabolic process; IMP:EcoCyc.
DR CDD; cd01174; ribokinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_01987; Ribokinase; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011877; D_ribokin.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR002139; Ribo/fructo_kinase.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR PRINTS; PR00990; RIBOKINASE.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02152; D_ribokin_bact; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Cytoplasm;
KW Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Potassium; Reference proteome; Transferase.
FT CHAIN 1..309
FT /note="Ribokinase"
FT /id="PRO_0000080097"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 14..16
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 42..46
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 223..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 249
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 251
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 254..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000269|PubMed:10438599, ECO:0000269|PubMed:11786021,
FT ECO:0000269|PubMed:9519409"
FT BINDING 285
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 288
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 290
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT BINDING 294
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01987,
FT ECO:0000305|PubMed:11786021"
FT STRAND 6..10
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1RK2"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:1RKD"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 129..134
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 202..214
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 253..266
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 271..286
FT /evidence="ECO:0007829|PDB:1RKD"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 292..294
FT /evidence="ECO:0007829|PDB:1RKD"
FT HELIX 298..306
FT /evidence="ECO:0007829|PDB:1RKD"
SQ SEQUENCE 309 AA; 32291 MW; 753729B41E64060E CRC64;
MQNAGSLVVL GSINADHILN LQSFPTPGET VTGNHYQVAF GGKGANQAVA AGRSGANIAF
IACTGDDSIG ESVRQQLATD NIDITPVSVI KGESTGVALI FVNGEGENVI GIHAGANAAL
SPALVEAQRE RIANASALLM QLESPLESVM AAAKIAHQNK TIVALNPAPA RELPDELLAL
VDIITPNETE AEKLTGIRVE NDEDAAKAAQ VLHEKGIRTV LITLGSRGVW ASVNGEGQRV
PGFRVQAVDT IAAGDTFNGA LITALLEEKP LPEAIRFAHA AAAIAVTRKG AQPSVPWREE
IDAFLDRQR
