GLGC_ECOLI
ID GLGC_ECOLI Reviewed; 431 AA.
AC P0A6V1; P00584; Q2M794;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glucose-1-phosphate adenylyltransferase {ECO:0000305};
DE EC=2.7.7.27 {ECO:0000269|PubMed:1648099};
DE AltName: Full=ADP-glucose pyrophosphorylase {ECO:0000303|PubMed:826540};
DE Short=ADPGlc PPase {ECO:0000303|PubMed:21741429};
DE AltName: Full=ADP-glucose synthase {ECO:0000303|PubMed:2162151};
GN Name=glgC; OrderedLocusNames=b3430, JW3393;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=6300111; DOI=10.1016/s0021-9258(18)32541-9;
RA Baecker P.A., Furlong C.E., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli
RT ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C
RT gene.";
RL J. Biol. Chem. 258:5084-5088(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT CL1136.
RC STRAIN=B;
RX PubMed=1339262; DOI=10.1016/0003-9861(92)90553-9;
RA Ghosh P., Meyer C., Remy E., Peterson D., Preiss J.;
RT "Cloning, expression, and nucleotide sequence of glgC gene from an
RT allosteric mutant of Escherichia coli B.";
RL Arch. Biochem. Biophys. 296:122-128(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT SG5.
RC STRAIN=B;
RX PubMed=1320612; DOI=10.1128/jb.174.13.4509-4512.1992;
RA Meyer C.R., Ghosh P., Remy E., Preiss J.;
RT "Cloning, expression, and nucleotide sequence of a mutant glgC gene from
RT Escherichia coli B.";
RL J. Bacteriol. 174:4509-4512(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT SG14, AND SEQUENCE REVISION TO
RP 295.
RC STRAIN=B;
RX PubMed=8385906; DOI=10.1006/abbi.1993.1181;
RA Meyer C.R., Ghosh P., Nadler S., Preiss J.;
RT "Cloning, expression, and sequence of an allosteric mutant ADPglucose
RT pyrophosphorylase from Escherichia coli B.";
RL Arch. Biochem. Biophys. 302:64-71(1993).
RN [5]
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 [6]
RP SEQUENCE REVISION TO 161; 166 AND 189, AND MUTANT 618.
RX PubMed=2543670; DOI=10.1016/s0021-9258(18)81644-1;
RA Kumar A., Ghosh P., Lee Y.M., Hill M.A., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Determination of the amino acid
RT changes that alter the regulatory properties of a mutant Escherichia coli
RT ADP-glucose synthetase.";
RL J. Biol. Chem. 264:10464-10471(1989).
RN [7]
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 [8]
RP PROTEIN SEQUENCE OF 2-28, AND SUBUNIT.
RX PubMed=826540; DOI=10.1016/s0021-9258(19)57016-8;
RA Haugen T.H., Ishaque A., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Characterization of the subunit
RT structure of Escherichia coli B glucose-1-phosphate adenylyltransferase (EC
RT 2.7.7.27).";
RL J. Biol. Chem. 251:7880-7885(1976).
RN [9]
RP PROTEIN SEQUENCE OF 2-49 AND 183-201.
RX PubMed=359552; DOI=10.1016/s0021-9258(17)34418-6;
RA Parsons T.F., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Isolation and characterization of the
RT pyridoxal-P allosteric activator site and the ADP-glucose-protected
RT pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase.";
RL J. Biol. Chem. 253:7638-7645(1978).
RN [10]
RP MUTAGENESIS OF TYR-114.
RX PubMed=2844780; DOI=10.1016/s0021-9258(18)68084-6;
RA Kumar A., Tanaka T., Lee Y.M., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis to
RT probe the role of tyrosine 114 in the catalytic mechanism of ADP-glucose
RT synthetase from Escherichia coli.";
RL J. Biol. Chem. 263:14634-14639(1988).
RN [11]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-39.
RX PubMed=2162151; DOI=10.1016/0003-9861(90)90533-5;
RA Gardiol A., Preiss J.;
RT "Escherichia coli E-39 ADPglucose synthetase has different activation
RT kinetics from the wild-type allosteric enzyme.";
RL Arch. Biochem. Biophys. 280:175-180(1990).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP LYS-195, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=1648099; DOI=10.1016/s0021-9258(18)98920-9;
RA Hill M.A., Kaufmann K., Otero J., Preiss J.;
RT "Biosynthesis of bacterial glycogen. Mutagenesis of a catalytic site
RT residue of ADP-glucose pyrophosphorylase from Escherichia coli.";
RL J. Biol. Chem. 266:12455-12460(1991).
RN [13]
RP INDUCTION.
RC STRAIN=K12 / BW3414;
RX PubMed=7751274; DOI=10.1128/jb.177.10.2663-2672.1995;
RA Liu M.Y., Yang H., Romeo T.;
RT "The product of the pleiotropic Escherichia coli gene csrA modulates
RT glycogen biosynthesis via effects on mRNA stability.";
RL J. Bacteriol. 177:2663-2672(1995).
RN [14]
RP ACTIVITY REGULATION, AND MUTAGENESIS OF GLN-74 AND TRP-113.
RX PubMed=21741429; DOI=10.1016/j.biochi.2011.06.029;
RA Figueroa C.M., Esper M.C., Bertolo A., Demonte A.M., Aleanzi M.,
RA Iglesias A.A., Ballicora M.A.;
RT "Understanding the allosteric trigger for the fructose-1,6-bisphosphate
RT regulation of the ADP-glucose pyrophosphorylase from Escherichia coli.";
RL Biochimie 93:1816-1823(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEX WITH
RP FRUCTOSE-1,6-BISPHOSPHATE; AMP AND SUBSTRATE ANALOG, SUBUNIT, AND REACTION
RP MECHANISM.
RX PubMed=27545622; DOI=10.1016/j.str.2016.06.023;
RA Cifuente J.O., Comino N., Madariaga-Marcos J., Lopez-Fernandez S.,
RA Garcia-Alija M., Agirre J., Albesa-Jove D., Guerin M.E.;
RT "Structural basis of glycogen biosynthesis regulation in bacteria.";
RL Structure 24:1613-1622(2016).
CC -!- FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block
CC required for the elongation reactions to produce glycogen. Catalyzes
CC the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to
CC produce pyrophosphate and ADP-Glc. {ECO:0000269|PubMed:1648099}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose
CC + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498,
CC ChEBI:CHEBI:58601; EC=2.7.7.27;
CC Evidence={ECO:0000269|PubMed:1648099};
CC -!- ACTIVITY REGULATION: Allosterically activated by fructose-1,6-
CC bisphosphate (F16BP), hexanediol 1,6-bisphosphate, NADPH and pyridoxal
CC phosphate. Inhibited by AMP and by high concentrations of MgCl(2).
CC {ECO:0000269|PubMed:1648099, ECO:0000269|PubMed:2162151,
CC ECO:0000269|PubMed:21741429}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:1648099};
CC KM=120 uM for diphosphate {ECO:0000269|PubMed:1648099};
CC Vmax=133 umol/min/mg enzyme toward alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:1648099};
CC Vmax=97 umol/min/mg enzyme toward diphosphate
CC {ECO:0000269|PubMed:1648099};
CC Note=kcat is 111 sec(-1) for adenylyltransferase activity. kcat is 81
CC sec(-1) for pyrophosphorylase activity. {ECO:0000269|PubMed:1648099};
CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:27545622,
CC ECO:0000269|PubMed:826540}.
CC -!- INDUCTION: mRNA stability is at least partially under the control of
CC CsrA; loss of csrA leads to higher transcript levels, possibly mediated
CC by protein binding to the mRNA (PubMed:7751274).
CC {ECO:0000269|PubMed:7751274}.
CC -!- MISCELLANEOUS: Displays cooperative behavior and a bibi mechanism with
CC sequential binding of ATP and G1P, followed by ordered release of
CC pyrophosphate and ADP-Glc. {ECO:0000269|PubMed:27545622}.
CC -!- SIMILARITY: Belongs to the bacterial/plant glucose-1-phosphate
CC adenylyltransferase family. {ECO:0000305}.
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DR EMBL; V00281; CAA23544.1; -; Genomic_DNA.
DR EMBL; J01616; AAA98736.1; -; Genomic_DNA.
DR EMBL; M97226; AAA23873.1; -; Genomic_DNA.
DR EMBL; S58224; AAB26162.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58228.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76455.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77862.1; -; Genomic_DNA.
DR PIR; A00721; YUEC.
DR RefSeq; NP_417888.1; NC_000913.3.
DR RefSeq; WP_000253975.1; NZ_STEB01000004.1.
DR PDB; 5L6S; X-ray; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-431.
DR PDB; 5L6V; X-ray; 2.67 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-431.
DR PDB; 5MNI; X-ray; 3.09 A; A/B/C/D/E/F/G/H=1-431.
DR PDB; 6R8B; EM; 3.10 A; A/B/C/D=1-431.
DR PDB; 6R8U; EM; 3.00 A; A/B/C/D=1-431.
DR PDB; 6SHJ; EM; 3.20 A; A/B/C/D=1-431.
DR PDB; 6SHN; EM; 3.30 A; A/B/C/D=1-431.
DR PDB; 6SHQ; EM; 3.20 A; A/B/C/D=1-431.
DR PDB; 6SI8; EM; 3.40 A; A/B/C/D=1-431.
DR PDBsum; 5L6S; -.
DR PDBsum; 5L6V; -.
DR PDBsum; 5MNI; -.
DR PDBsum; 6R8B; -.
DR PDBsum; 6R8U; -.
DR PDBsum; 6SHJ; -.
DR PDBsum; 6SHN; -.
DR PDBsum; 6SHQ; -.
DR PDBsum; 6SI8; -.
DR AlphaFoldDB; P0A6V1; -.
DR SMR; P0A6V1; -.
DR BioGRID; 4262502; 297.
DR BioGRID; 852251; 1.
DR DIP; DIP-48147N; -.
DR IntAct; P0A6V1; 6.
DR STRING; 511145.b3430; -.
DR jPOST; P0A6V1; -.
DR PaxDb; P0A6V1; -.
DR PRIDE; P0A6V1; -.
DR EnsemblBacteria; AAC76455; AAC76455; b3430.
DR EnsemblBacteria; BAE77862; BAE77862; BAE77862.
DR GeneID; 66672686; -.
DR GeneID; 947942; -.
DR KEGG; ecj:JW3393; -.
DR KEGG; eco:b3430; -.
DR PATRIC; fig|511145.12.peg.3527; -.
DR EchoBASE; EB0374; -.
DR eggNOG; COG0448; Bacteria.
DR HOGENOM; CLU_029499_14_1_6; -.
DR InParanoid; P0A6V1; -.
DR OMA; QEWDVDE; -.
DR PhylomeDB; P0A6V1; -.
DR BioCyc; EcoCyc:GLUC1PADENYLTRANS-MON; -.
DR BioCyc; MetaCyc:GLUC1PADENYLTRANS-MON; -.
DR BRENDA; 2.7.7.27; 2026.
DR UniPathway; UPA00164; -.
DR PRO; PR:P0A6V1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0010170; C:glucose-1-phosphate adenylyltransferase complex; IDA:EcoCyc.
DR GO; GO:0016208; F:AMP binding; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008878; F:glucose-1-phosphate adenylyltransferase activity; IDA:EcoCyc.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0005978; P:glycogen biosynthetic process; IMP:EcoCyc.
DR Gene3D; 3.90.550.10; -; 1.
DR HAMAP; MF_00624; GlgC; 1.
DR InterPro; IPR011831; ADP-Glc_PPase.
DR InterPro; IPR005836; ADP_Glu_pyroP_CS.
DR InterPro; IPR023049; GlgC_bac.
DR InterPro; IPR005835; NTP_transferase_dom.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR PANTHER; PTHR43523; PTHR43523; 1.
DR Pfam; PF00483; NTP_transferase; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR TIGRFAMs; TIGR02091; glgC; 1.
DR PROSITE; PS00808; ADP_GLC_PYROPHOSPH_1; 1.
DR PROSITE; PS00809; ADP_GLC_PYROPHOSPH_2; 1.
DR PROSITE; PS00810; ADP_GLC_PYROPHOSPH_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; ATP-binding; Carbohydrate metabolism;
KW Direct protein sequencing; Glycogen biosynthesis; Glycogen metabolism;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:359552,
FT ECO:0000269|PubMed:826540"
FT CHAIN 2..431
FT /note="Glucose-1-phosphate adenylyltransferase"
FT /id="PRO_0000195294"
FT BINDING 39
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /evidence="ECO:0000269|PubMed:27545622,
FT ECO:0000305|PubMed:2162151"
FT BINDING 40
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 46
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 52
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 114
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000305|PubMed:2844780"
FT BINDING 130
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 179
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000305|PubMed:27545622"
FT BINDING 194..195
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000305|PubMed:1648099,
FT ECO:0000305|PubMed:27545622"
FT BINDING 212
FT /ligand="alpha-D-glucose 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:58601"
FT /evidence="ECO:0000305|PubMed:27545622"
FT BINDING 370
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 386
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 419..423
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /evidence="ECO:0000269|PubMed:27545622"
FT BINDING 429..431
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /evidence="ECO:0000269|PubMed:27545622"
FT SITE 74
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000305|PubMed:21741429"
FT SITE 113
FT /note="Could play a key role in the communication between
FT the regulatory and the substrate sites"
FT /evidence="ECO:0000305|PubMed:21741429"
FT VARIANT 44
FT /note="A -> T (in SG14 mutant; lower apparent affinities
FT for substrates, fructose-1,6-bisphosphate and AMP)"
FT /evidence="ECO:0000269|PubMed:8385906"
FT VARIANT 67
FT /note="R -> C (in CL1136 mutant; less dependent on the
FT allosteric activator, fructose-1,6-bisphosphate, for
FT activity and less sensitive to inhibition by AMP)"
FT /evidence="ECO:0000269|PubMed:1339262"
FT VARIANT 295
FT /note="P -> S (in SG5 mutant)"
FT /evidence="ECO:0000269|PubMed:1320612"
FT VARIANT 336
FT /note="G -> D (in 618 mutant; causes lowered affinity for
FT AMP)"
FT /evidence="ECO:0000269|PubMed:2543670"
FT MUTAGEN 39
FT /note="K->E: The level of activation by pyridoxal phosphate
FT and fructose-1,6-phosphate is only approximately 2-fold
FT compared to activation of 15- to 28-fold respectively, for
FT the wild-type. NADPH is unable to activate the mutant
FT enzyme."
FT /evidence="ECO:0000269|PubMed:2162151"
FT MUTAGEN 74
FT /note="Q->A: Insensitive to activation by fructose-1,6-
FT bisphosphate, but still binds fructose-1,6-bisphosphate
FT with similar affinity as the wild-type. AMP causes similar
FT inhibition on the wild-type and mutant."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 74
FT /note="Q->E: Insensitive to activation by fructose-1,6-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 74
FT /note="Q->N: The enzyme is activated 35-fold by fructose-
FT 1,6-bisphosphate."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 113
FT /note="W->A: Insensitive to activation by fructose-1,6-
FT bisphosphate, but still binds fructose-1,6-bisphosphate,
FT with similar affinity as the wild-type. AMP causes similar
FT inhibition on the wild-type and mutant."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 113
FT /note="W->L: The enzyme is activated only 3-fold by
FT fructose-1,6-bisphosphate."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 113
FT /note="W->Y: The enzyme is activated 15-fold by fructose-
FT 1,6-bisphosphate."
FT /evidence="ECO:0000269|PubMed:21741429"
FT MUTAGEN 114
FT /note="Y->F: Shows a decrease of affinity for the
FT substrates and less than 2-fold activation by fructose 1,6-
FT bisphosphate in the ADP-glucose synthesis direction. In
FT contrast, in the pyrophosphorolysis direction, the mutant
FT shoqws about a 30-fold activation by fructose 1,6-
FT bisphosphate."
FT /evidence="ECO:0000269|PubMed:2844780"
FT MUTAGEN 195
FT /note="K->E,I,H,R: Decrease of the affinity for alpha-D-
FT glucose 1-phosphate, but no loss in adenylyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:1648099"
FT MUTAGEN 195
FT /note="K->Q: 600-fold decrease of the affinity for alpha-D-
FT glucose 1-phosphate compared to the wild-type. In contrast,
FT kinetic constants for ATP, magnesium and fructose-1,6-
FT bisphosphate are similar in mutant and wild-type cases. The
FT catalytic efficiency is 2-fold lower in the mutant."
FT /evidence="ECO:0000269|PubMed:1648099"
FT CONFLICT 161
FT /note="A -> V (in Ref. 3; CAA23544/AAA98736/AAA23873)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="A -> V (in Ref. 3; CAA23544/AAA98736/AAA23873)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="I -> T (in Ref. 3; CAA23544/AAA98736/AAA23873)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="E -> K (in Ref. 3; CAA23544/AAA98736)"
FT /evidence="ECO:0000305"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:5L6V"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:6R8B"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:6R8U"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 54..63
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 78..87
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 134..140
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6R8U"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 162..171
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 208..219
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5L6S"
FT TURN 240..243
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 254..258
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 302..304
FT /evidence="ECO:0007829|PDB:6R8U"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 327..334
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 339..342
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 378..384
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 395..398
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 400..406
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 407..409
FT /evidence="ECO:0007829|PDB:5L6V"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:6R8B"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:5L6V"
FT HELIX 419..424
FT /evidence="ECO:0007829|PDB:5L6V"
SQ SEQUENCE 431 AA; 48698 MW; 3C0A4C4F5B13D9D3 CRC64;
MVSLEKNDHL MLARQLPLKS VALILAGGRG TRLKDLTNKR AKPAVHFGGK FRIIDFALSN
CINSGIRRMG VITQYQSHTL VQHIQRGWSF FNEEMNEFVD LLPAQQRMKG ENWYRGTADA
VTQNLDIIRR YKAEYVVILA GDHIYKQDYS RMLIDHVEKG ARCTVACMPV PIEEASAFGV
MAVDENDKII EFVEKPANPP SMPNDPSKSL ASMGIYVFDA DYLYELLEED DRDENSSHDF
GKDLIPKITE AGLAYAHPFP LSCVQSDPDA EPYWRDVGTL EAYWKANLDL ASVVPELDMY
DRNWPIRTYN ESLPPAKFVQ DRSGSHGMTL NSLVSGGCVI SGSVVVQSVL FSRVRVNSFC
NIDSAVLLPE VWVGRSCRLR RCVIDRACVI PEGMVIGENA EEDARRFYRS EEGIVLVTRE
MLRKLGHKQE R
