PYRG_ECOLI
ID PYRG_ECOLI Reviewed; 545 AA.
AC P0A7E5; P08398; Q2MA52;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=CTP synthase {ECO:0000303|PubMed:11336655};
DE EC=6.3.4.2 {ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:4550559, ECO:0000269|PubMed:8385490};
DE AltName: Full=Cytidine 5'-triphosphate synthase {ECO:0000303|PubMed:11336655};
DE AltName: Full=Cytidine triphosphate synthetase {ECO:0000303|PubMed:15157079};
DE Short=CTP synthetase {ECO:0000303|PubMed:3514618};
DE Short=CTPS {ECO:0000303|PubMed:15157079};
DE AltName: Full=UTP--ammonia ligase;
GN Name=pyrG {ECO:0000303|PubMed:3514618}; OrderedLocusNames=b2780, JW2751;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DOMAIN.
RX PubMed=3514618; DOI=10.1016/s0021-9258(19)57252-0;
RA Weng M., Makaroff C.A., Zalkin H.;
RT "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase.";
RL J. Biol. Chem. 261:5568-5574(1986).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-13.
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 [5]
RP CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=4550559; DOI=10.1021/bi00752a015;
RA Levitzki A., Koshland D.E. Jr.;
RT "Role of an allosteric effector. Guanosine triphosphate activation in
RT cytosine triphosphate synthetase.";
RL Biochemistry 11:241-246(1972).
RN [6]
RP SUBUNIT.
RX PubMed=4550560; DOI=10.1021/bi00752a016;
RA Levitzki A., Koshland D.E. Jr.;
RT "Ligand-induced dimer-to-tetramer transformation in cytosine triphosphate
RT synthetase.";
RL Biochemistry 11:247-253(1972).
RN [7]
RP DOMAIN, AND MUTAGENESIS OF VAL-349 AND GLY-352.
RX PubMed=3298209; DOI=10.1128/jb.169.7.3023-3028.1987;
RA Weng M., Zalkin H.;
RT "Structural role for a conserved region in the CTP synthetase glutamine
RT amide transfer domain.";
RL J. Bacteriol. 169:3023-3028(1987).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=8385490; DOI=10.1021/bi00065a032;
RA Robertson J.G., Villafranca J.J.;
RT "Characterization of metal ion activation and inhibition of CTP
RT synthetase.";
RL Biochemistry 32:3769-3777(1993).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, MUTAGENESIS OF CYS-379, AND ACTIVE SITE.
RX PubMed=11336655; DOI=10.1042/0264-6021:3560223;
RA Bearne S.L., Hekmat O., MacDonnell J.E.;
RT "Inhibition of Escherichia coli CTP synthase by glutamate gamma-
RT semialdehyde and the role of the allosteric effector GTP in glutamine
RT hydrolysis.";
RL Biochem. J. 356:223-232(2001).
RN [11]
RP SUBCELLULAR LOCATION.
RC STRAIN=B / BL21-DE3 / Transetta;
RX PubMed=32507415; DOI=10.1016/j.jgg.2020.03.004;
RA Zhou S., Xiang H., Liu J.L.;
RT "CTP synthase forms cytoophidia in archaea.";
RL J. Genet. Genomics 47:213-223(2020).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), FUNCTION, DOMAIN, AND ACTIVE SITE.
RX PubMed=15157079; DOI=10.1021/bi0496945;
RA Endrizzi J.A., Kim H., Anderson P.M., Baldwin E.P.;
RT "Crystal structure of Escherichia coli cytidine triphosphate synthetase, a
RT nucleotide-regulated glutamine amidotransferase/ATP-dependent amidoligase
RT fusion protein and homologue of anticancer and antiparasitic drug
RT targets.";
RL Biochemistry 43:6447-6463(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEX WITH ADP; CTP AND
RP MAGNESIUM, AND ACTIVITY REGULATION.
RX PubMed=16216072; DOI=10.1021/bi051282o;
RA Endrizzi J.A., Kim H., Anderson P.M., Baldwin E.P.;
RT "Mechanisms of product feedback regulation and drug resistance in cytidine
RT triphosphate synthetases from the structure of a CTP-inhibited complex.";
RL Biochemistry 44:13491-13499(2005).
CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with
CC either L-glutamine or ammonia as the source of nitrogen. Regulates
CC intracellular CTP levels through interactions with the four
CC ribonucleotide triphosphates. {ECO:0000269|PubMed:11336655,
CC ECO:0000269|PubMed:8385490, ECO:0000305|PubMed:15157079}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-
CC glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2;
CC Evidence={ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:4550559,
CC ECO:0000269|PubMed:8385490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359;
CC Evidence={ECO:0000269|PubMed:11336655, ECO:0000305|PubMed:8385490};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NH4(+) + UTP = ADP + CTP + 2 H(+) + phosphate;
CC Xref=Rhea:RHEA:16597, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:8385490};
CC -!- ACTIVITY REGULATION: Allosterically activated by GTP, when glutamine is
CC the substrate; GTP has no effect on the reaction when ammonia is the
CC substrate (PubMed:4550559). The allosteric effector GTP functions by
CC stabilizing the protein conformation that binds the tetrahedral
CC intermediate(s) formed during glutamine hydrolysis (PubMed:11336655).
CC Also activated by magnesium; the enzyme requires more Mg(2+) for full
CC catalytic activity than required simply to complex the nucleotide
CC substrates (PubMed:8385490). Inhibited by the product CTP, via
CC allosteric rather than competitive inhibition (PubMed:8385490,
CC PubMed:16216072). Also inhibited by divalent metal ions such as copper
CC and zinc (PubMed:8385490). Is potently inhibited by the intermediate
CC analog inhibitor glutamate gamma-semialdehyde (PubMed:11336655).
CC {ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:4550559,
CC ECO:0000269|PubMed:8385490, ECO:0000305|PubMed:16216072}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.0 mM for ammonia {ECO:0000269|PubMed:11336655};
CC KM=0.30 mM for L-glutamine (in the presence of 0.25 mM GTP)
CC {ECO:0000269|PubMed:11336655};
CC Note=kcat is 13 sec(-1) with ammonia as substrate. kcat is 6.6 sec(-
CC 1) with L-glutamine as substrate (in the presence of 0.25 mM GTP).
CC {ECO:0000269|PubMed:11336655};
CC pH dependence:
CC Optimum pH is 8.7. {ECO:0000269|PubMed:8385490};
CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway;
CC CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}.
CC -!- SUBUNIT: Homodimer that associates to form homotetramer in the presence
CC of ATP and UTP. The substrate nucleotides ATP and UTP act
CC synergistically to promote oligomerization of CTPS from inactive dimers
CC to active tetramers. {ECO:0000269|PubMed:4550560}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:32507415}.
CC Note=Localizes to the cytoophidium, a subcellular filamentary structure
CC where CTP synthase is compartmentalized. Many cells form cytoophidia
CC which are observed in stationary phase. {ECO:0000269|PubMed:32507415}.
CC -!- DOMAIN: Sequence consists of two domains: the C-terminal glutamine
CC amide transfer (GAT) domain catalyzes the hydrolysis of glutamine; the
CC N-terminal synthase domain catalyzes the amination of UTP
CC (PubMed:3514618, PubMed:3298209). Structure shows each subunit consists
CC of three distinct segments: the N-terminal amidoligase (ALase) domain,
CC which mediates oligomerization and contains the ALase active site where
CC ATP and UTP substrates bind, and an interrupted helical interdomain
CC linker segment that connects the ALase domain to the Type I glutamine
CC amidotransferase (GATase) C-terminal domain, which generates ammonia
CC via glutamine hydrolysis (PubMed:15157079). A gated channel that spans
CC 25 Angstroms between the glutamine hydrolysis and amidoligase active
CC sites provides a path for ammonia diffusion; the channel is accessible
CC to solvent at the base of a cleft adjoining the glutamine hydrolysis
CC active site, providing an entry point for exogenous ammonia
CC (PubMed:15157079). {ECO:0000305|PubMed:15157079,
CC ECO:0000305|PubMed:3298209, ECO:0000305|PubMed:3514618}.
CC -!- MISCELLANEOUS: CTPSs have evolved a hybrid strategy for distinguishing
CC between UTP and CTP. The overlapping regions of the product feedback
CC inhibitory and substrate sites recognize a common feature in both
CC compounds, the triphosphate moiety. To differentiate isosteric
CC substrate and product pyrimidine rings, an additional pocket far from
CC the expected kinase/ligase catalytic site, specifically recognizes the
CC cytosine and ribose portions of the product inhibitor.
CC {ECO:0000305|PubMed:16216072}.
CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_01227}.
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DR EMBL; M12843; AAA24485.1; -; mRNA.
DR EMBL; U29580; AAA69290.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75822.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76854.1; -; Genomic_DNA.
DR PIR; H65059; SYECTP.
DR RefSeq; NP_417260.1; NC_000913.3.
DR RefSeq; WP_000210878.1; NZ_STEB01000030.1.
DR PDB; 1S1M; X-ray; 2.30 A; A/B=1-545.
DR PDB; 2AD5; X-ray; 2.80 A; A/B=1-545.
DR PDB; 5TKV; X-ray; 2.70 A; A/B=1-545.
DR PDB; 5U05; EM; 7.90 A; A/B/C/D=1-545.
DR PDB; 5U3C; EM; 4.60 A; A/B/C/D=1-545.
DR PDB; 5U6R; EM; 5.70 A; A/B/C/D=1-545.
DR PDBsum; 1S1M; -.
DR PDBsum; 2AD5; -.
DR PDBsum; 5TKV; -.
DR PDBsum; 5U05; -.
DR PDBsum; 5U3C; -.
DR PDBsum; 5U6R; -.
DR AlphaFoldDB; P0A7E5; -.
DR SMR; P0A7E5; -.
DR BioGRID; 4262298; 5.
DR DIP; DIP-10628N; -.
DR IntAct; P0A7E5; 8.
DR STRING; 511145.b2780; -.
DR MEROPS; C26.964; -.
DR SWISS-2DPAGE; P0A7E5; -.
DR jPOST; P0A7E5; -.
DR PaxDb; P0A7E5; -.
DR PRIDE; P0A7E5; -.
DR EnsemblBacteria; AAC75822; AAC75822; b2780.
DR EnsemblBacteria; BAE76854; BAE76854; BAE76854.
DR GeneID; 66673353; -.
DR GeneID; 946116; -.
DR KEGG; ecj:JW2751; -.
DR KEGG; eco:b2780; -.
DR PATRIC; fig|1411691.4.peg.3955; -.
DR EchoBASE; EB0803; -.
DR eggNOG; COG0504; Bacteria.
DR HOGENOM; CLU_011675_5_0_6; -.
DR InParanoid; P0A7E5; -.
DR OMA; EFNNAYR; -.
DR PhylomeDB; P0A7E5; -.
DR BioCyc; EcoCyc:CTPSYN-MON; -.
DR BioCyc; MetaCyc:CTPSYN-MON; -.
DR BRENDA; 6.3.4.2; 2026.
DR SABIO-RK; P0A7E5; -.
DR UniPathway; UPA00159; UER00277.
DR EvolutionaryTrace; P0A7E5; -.
DR PRO; PR:P0A7E5; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0097268; C:cytoophidium; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003883; F:CTP synthase activity; IDA:EcoCyc.
DR GO; GO:0004359; F:glutaminase activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006241; P:CTP biosynthetic process; IDA:EcoCyc.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR CDD; cd03113; CTPS_N; 1.
DR CDD; cd01746; GATase1_CTP_Synthase; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01227; PyrG; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR004468; CTP_synthase.
DR InterPro; IPR017456; CTP_synthase_N.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR033828; GATase1_CTP_Synthase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11550; PTHR11550; 1.
DR Pfam; PF06418; CTP_synth_N; 1.
DR Pfam; PF00117; GATase; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00337; PyrG; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW Glutamine amidotransferase; Ligase; Magnesium; Metal-binding;
KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 2..545
FT /note="CTP synthase"
FT /id="PRO_0000138183"
FT DOMAIN 291..542
FT /note="Glutamine amidotransferase type-1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT REGION 2..266
FT /note="Amidoligase domain"
FT /evidence="ECO:0000305|PubMed:15157079"
FT ACT_SITE 379
FT /note="Nucleophile; for glutamine hydrolysis"
FT /evidence="ECO:0000305|PubMed:11336655,
FT ECO:0000305|PubMed:15157079"
FT ACT_SITE 515
FT /evidence="ECO:0000305|PubMed:15157079"
FT ACT_SITE 517
FT /evidence="ECO:0000305|PubMed:15157079"
FT BINDING 14
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:16216072"
FT BINDING 14
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000305|PubMed:16216072"
FT BINDING 15..20
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 72
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 140
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 147..149
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 187..192
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 187..192
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000305|PubMed:16216072"
FT BINDING 223
FT /ligand="CTP"
FT /ligand_id="ChEBI:CHEBI:37563"
FT /ligand_note="allosteric inhibitor"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 223
FT /ligand="UTP"
FT /ligand_id="ChEBI:CHEBI:46398"
FT /evidence="ECO:0000305|PubMed:16216072"
FT BINDING 239..241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:16216072,
FT ECO:0007744|PDB:2AD5"
FT BINDING 352
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT BINDING 380..383
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT BINDING 403
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT BINDING 470
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01227"
FT MUTAGEN 349
FT /note="V->S: 30% increase in both glutamine-dependent and
FT ammonia-dependent activities."
FT /evidence="ECO:0000269|PubMed:3298209"
FT MUTAGEN 352
FT /note="G->P: Loss of glutamine-dependent activity, but no
FT change in ammonia-dependent activity."
FT /evidence="ECO:0000269|PubMed:3298209"
FT MUTAGEN 379
FT /note="C->A,S: Loss of glutamine-dependent activity, but no
FT change in ammonia-dependent activity."
FT /evidence="ECO:0000269|PubMed:11336655"
FT CONFLICT 338
FT /note="V -> L (in Ref. 1; AAA24485)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="M -> S (in Ref. 1; AAA24485)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 18..30
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:5TKV"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2AD5"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2AD5"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 92..104
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 105..110
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 115..131
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2AD5"
FT HELIX 151..164
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 168..176
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 206..214
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:5TKV"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 256..263
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 274..284
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 321..329
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 330..336
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 338..343
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 411..414
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 416..418
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 422..424
FT /evidence="ECO:0007829|PDB:5TKV"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 453..457
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 460..469
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 475..483
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:1S1M"
FT STRAND 506..514
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:1S1M"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1S1M"
FT HELIX 527..542
FT /evidence="ECO:0007829|PDB:1S1M"
SQ SEQUENCE 545 AA; 60374 MW; FBB9E2E18FA355FC CRC64;
MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPIQHGEV
FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL RKERRGDYLG ATVQVIPHIT
NAIKERVLEG GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AVEIGREHTL FMHLTLVPYM
AASGEVKTKP TQHSVKELLS IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD
VDSIYKIPGL LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE
LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP GGFGYRGVEG
MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN STEFVPDCKY PVVALITEWR
DENGNVEVRS EKSDLGGTMR LGAQQCQLVD DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ
IEDAGLRVAG RSGDDQLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ
KRQAK
