PNP_ECOLI
ID PNP_ECOLI Reviewed; 711 AA.
AC P05055; P78109; Q2M946;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Polyribonucleotide nucleotidyltransferase {ECO:0000255|HAMAP-Rule:MF_01595};
DE EC=2.7.7.8 {ECO:0000255|HAMAP-Rule:MF_01595, ECO:0000269|PubMed:12162954, ECO:0000269|PubMed:18812438, ECO:0000269|PubMed:4866865};
DE AltName: Full=Polynucleotide phosphorylase {ECO:0000255|HAMAP-Rule:MF_01595};
DE Short=PNPase {ECO:0000255|HAMAP-Rule:MF_01595};
GN Name=pnp {ECO:0000255|HAMAP-Rule:MF_01595};
GN OrderedLocusNames=b3164, JW5851;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2432069; DOI=10.1016/s0021-9258(19)75888-8;
RA Regnier P., Grunberg-Manago M., Portier C.;
RT "Nucleotide sequence of the pnp gene of Escherichia coli encoding
RT polynucleotide phosphorylase. Homology of the primary structure of the
RT protein with the RNA-binding domain of ribosomal protein S1.";
RL J. Biol. Chem. 262:63-68(1987).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-196.
RX PubMed=6382163; DOI=10.1093/nar/12.15.6091;
RA Portier C., Regnier P.;
RT "Expression of the rpsO and pnp genes: structural analysis of a DNA
RT fragment carrying their control regions.";
RL Nucleic Acids Res. 12:6091-6102(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62.
RX PubMed=3005122; DOI=10.1016/0378-1119(85)90019-8;
RA Evans S., Dennis P.P.;
RT "Promoter activity and transcript mapping in the regulatory region for
RT genes encoding ribosomal protein S15 and polynucleotide phosphorylase of
RT Escherichia coli.";
RL Gene 40:15-22(1985).
RN [6]
RP PROTEIN SEQUENCE OF 1-12.
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, AND CATALYTIC ACTIVITY.
RX PubMed=4866865; DOI=10.1016/s0021-9258(18)99284-7;
RA Kimhi Y., Littauer U.Z.;
RT "Purification and properties of polynucleotide phosphorylase from
RT Escherichia coli.";
RL J. Biol. Chem. 243:231-240(1968).
RN [8]
RP SUBUNIT.
RX PubMed=1089072; DOI=10.1016/0014-5793(75)81045-3;
RA Portier C.;
RT "Quaternary structure of Escherichia coli polynucleotide phosphorylase: new
RT evidence for a trimeric structure.";
RL FEBS Lett. 50:79-81(1975).
RN [9]
RP INDUCTION.
RX PubMed=1628624; DOI=10.1002/j.1460-2075.1992.tb05329.x;
RA Robert-Le Meur M., Portier C.;
RT "E.coli polynucleotide phosphorylase expression is autoregulated through an
RT RNase III-dependent mechanism.";
RL EMBO J. 11:2633-2641(1992).
RN [10]
RP FUNCTION IN TRNA PROCESSING.
RX PubMed=7509797; DOI=10.1016/s0021-9258(17)37570-1;
RA Li Z., Deutscher M.P.;
RT "The role of individual exoribonucleases in processing at the 3' end of
RT Escherichia coli tRNA precursors.";
RL J. Biol. Chem. 269:6064-6071(1994).
RN [11]
RP INDUCTION BY COLD-SHOCK.
RC STRAIN=CSH142;
RX PubMed=8898389; DOI=10.1111/j.1365-2958.1996.tb02582.x;
RA Jones P.G., Inouye M.;
RT "RbfA, a 30S ribosomal binding factor, is a cold-shock protein whose
RT absence triggers the cold-shock response.";
RL Mol. Microbiol. 21:1207-1218(1996).
RN [12]
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 [13]
RP INTERACTION WITH RNE.
RX PubMed=9732274; DOI=10.1101/gad.12.17.2770;
RA Vanzo N.F., Li Y.S., Py B., Blum E., Higgins C.F., Raynal L.C.,
RA Krisch H.M., Carpousis A.J.;
RT "Ribonuclease E organizes the protein interactions in the Escherichia coli
RT RNA degradosome.";
RL Genes Dev. 12:2770-2781(1998).
RN [14]
RP INDUCTION.
RX PubMed=11395447; DOI=10.1128/jb.183.13.3848-3854.2001;
RA Mathy N., Jarrige A.C., Robert-Le Meur M., Portier C.;
RT "Increased expression of Escherichia coli polynucleotide phosphorylase at
RT low temperatures is linked to a decrease in the efficiency of
RT autocontrol.";
RL J. Bacteriol. 183:3848-3854(2001).
RN [15]
RP CATALYTIC ACTIVITY, FUNCTION, AND MUTAGENESIS OF ARG-100; ARG-319; VAL-428;
RP CYS-444 AND ASP-492.
RX PubMed=12162954; DOI=10.1016/s0022-2836(02)00645-9;
RA Jarrige A., Brechemier-Baey D., Mathy N., Duche O., Portier C.;
RT "Mutational analysis of polynucleotide phosphorylase from Escherichia
RT coli.";
RL J. Mol. Biol. 321:397-409(2002).
RN [16]
RP INTERACTION WITH RNE, AND ASSOCIATION WITH RNA DEGRADOSOME.
RC STRAIN=CF881;
RX PubMed=15554978; DOI=10.1111/j.1365-2958.2004.04360.x;
RA Prud'homme-Genereux A., Beran R.K., Iost I., Ramey C.S., Mackie G.A.,
RA Simons R.W.;
RT "Physical and functional interactions among RNase E, polynucleotide
RT phosphorylase and the cold-shock protein, CsdA: evidence for a 'cold shock
RT degradosome'.";
RL Mol. Microbiol. 54:1409-1421(2004).
RN [17]
RP SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [18]
RP INTERACTION WITH RNE AND RHLB.
RX PubMed=18337249; DOI=10.1074/jbc.m709118200;
RA Taghbalout A., Rothfield L.;
RT "RNaseE and RNA helicase B play central roles in the cytoskeletal
RT organization of the RNA degradosome.";
RL J. Biol. Chem. 283:13850-13855(2008).
RN [19]
RP FUNCTION IN RIBOSOME DEGRADATION DURING QUALITY CONTROL.
RC STRAIN=K12 / MG1655(Seq)*;
RX PubMed=21135037; DOI=10.1261/rna.2448911;
RA Basturea G.N., Zundel M.A., Deutscher M.P.;
RT "Degradation of ribosomal RNA during starvation: comparison to quality
RT control during steady-state growth and a role for RNase PH.";
RL RNA 17:338-345(2011).
RN [20]
RP STRUCTURE BY NMR OF 617-692.
RX PubMed=9008164; DOI=10.1016/s0092-8674(00)81844-9;
RA Bycroft M., Hubbard T.J., Proctor M., Freund S.M., Murzin A.G.;
RT "The solution structure of the S1 RNA binding domain: a member of an
RT ancient nucleic acid-binding fold.";
RL Cell 88:235-242(1997).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, RNA-BINDING, DOMAIN, AND MUTAGENESIS OF 79-ARG-ARG-80 AND ARG-83.
RX PubMed=18812438; DOI=10.1261/rna.1244308;
RA Shi Z., Yang W.Z., Lin-Chao S., Chak K.F., Yuan H.S.;
RT "Crystal structure of Escherichia coli PNPase: central channel residues are
RT involved in processive RNA degradation.";
RL RNA 14:2361-2371(2008).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-549 IN COMPLEXES WITH RNASE E;
RP RNA AND MANGANESE IONS, FUNCTION, COFACTOR, AND SUBUNIT.
RX PubMed=19327365; DOI=10.1016/j.jmb.2009.03.051;
RA Nurmohamed S., Vaidialingam B., Callaghan A.J., Luisi B.F.;
RT "Crystal structure of Escherichia coli polynucleotide phosphorylase core
RT bound to RNase E, RNA and manganese: implications for catalytic mechanism
RT and RNA degradosome assembly.";
RL J. Mol. Biol. 389:17-33(2009).
CC -!- FUNCTION: Involved in mRNA degradation. Catalyzes the phosphorolysis of
CC single-stranded polyribonucleotides processively in the 3'- to 5'-
CC direction. Also involved, along with RNase II, in tRNA processing.
CC RNases II and R contribute to rRNA degradation during starvation, while
CC RNase R and PNPase are the major contributors to quality control of
CC rRNA during steady state growth (PubMed:21135037). {ECO:0000255|HAMAP-
CC Rule:MF_01595, ECO:0000269|PubMed:12162954,
CC ECO:0000269|PubMed:18812438, ECO:0000269|PubMed:19327365,
CC ECO:0000269|PubMed:21135037, ECO:0000269|PubMed:4866865,
CC ECO:0000269|PubMed:7509797}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + RNA(n+1) = a ribonucleoside 5'-diphosphate +
CC RNA(n); Xref=Rhea:RHEA:22096, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:140395;
CC EC=2.7.7.8; Evidence={ECO:0000255|HAMAP-Rule:MF_01595,
CC ECO:0000269|PubMed:12162954, ECO:0000269|PubMed:18812438,
CC ECO:0000269|PubMed:4866865};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595,
CC ECO:0000269|PubMed:19327365};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01595,
CC ECO:0000269|PubMed:19327365};
CC Note=Magnesium. Can also use manganese. {ECO:0000255|HAMAP-
CC Rule:MF_01595, ECO:0000269|PubMed:19327365};
CC -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC complex involved in RNA processing and mRNA degradation. Interacts with
CC RNase E (rne). Homotrimer. The homotrimer forms a ring-like structure
CC with a central channel, where RNA molecules can bind. RNA molecules
CC bind between neighboring subunits. {ECO:0000255|HAMAP-Rule:MF_01595,
CC ECO:0000269|PubMed:1089072, ECO:0000269|PubMed:15554978,
CC ECO:0000269|PubMed:18337249, ECO:0000269|PubMed:18812438,
CC ECO:0000269|PubMed:19327365, ECO:0000269|PubMed:9732274}.
CC -!- INTERACTION:
CC P05055; P05055: pnp; NbExp=2; IntAct=EBI-548080, EBI-548080;
CC P05055; P0A8J8: rhlB; NbExp=8; IntAct=EBI-548080, EBI-555806;
CC P05055; P21513: rne; NbExp=13; IntAct=EBI-548080, EBI-549958;
CC P05055; P21507: srmB; NbExp=3; IntAct=EBI-548080, EBI-546628;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01595,
CC ECO:0000269|PubMed:16079137}. Note=Has also been isolated in
CC association with the inner membrane.
CC -!- INDUCTION: Expression is negatively autoregulated at the translational
CC level via an RNase III-dependent mechanism. Induced by cold shock (42
CC to 15 degrees Celsius) (at protein level) (PubMed:8898389). At low
CC temperature, the destabilizing effect of PNPase on its own mRNA is less
CC efficient, leading to a decrease in repression and an increase in the
CC expression level. {ECO:0000269|PubMed:11395447,
CC ECO:0000269|PubMed:1628624, ECO:0000269|PubMed:8898389}.
CC -!- DOMAIN: The S1 motif domain is important for trimerization and RNA-
CC binding. {ECO:0000269|PubMed:18812438}.
CC -!- SIMILARITY: Belongs to the polyribonucleotide nucleotidyltransferase
CC family. {ECO:0000255|HAMAP-Rule:MF_01595}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57967.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE77210.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J02638; AAA83905.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57967.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76198.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77210.1; ALT_INIT; Genomic_DNA.
DR EMBL; X00761; CAA25332.1; -; Genomic_DNA.
DR EMBL; M14425; AAA24596.1; -; Genomic_DNA.
DR PIR; H65106; H65106.
DR RefSeq; NP_417633.4; NC_000913.3.
DR RefSeq; WP_001295554.1; NZ_LN832404.1.
DR PDB; 1SRO; NMR; -; A=617-692.
DR PDB; 3CDI; X-ray; 2.60 A; A=2-711.
DR PDB; 3CDJ; X-ray; 2.80 A; A=2-547.
DR PDB; 3GCM; X-ray; 2.50 A; A/B/C=1-549.
DR PDB; 3GLL; X-ray; 2.70 A; A=1-549.
DR PDB; 3GME; X-ray; 2.40 A; A=1-549.
DR PDB; 3H1C; X-ray; 3.57 A; A/B/C/G/I/K/M/O/R/T/V/X=1-549.
DR PDB; 7OGK; EM; 3.40 A; A/B/C=1-711.
DR PDB; 7OGL; EM; 3.40 A; A/B/C=1-711.
DR PDB; 7OGM; EM; 3.70 A; L/N/O=1-711.
DR PDBsum; 1SRO; -.
DR PDBsum; 3CDI; -.
DR PDBsum; 3CDJ; -.
DR PDBsum; 3GCM; -.
DR PDBsum; 3GLL; -.
DR PDBsum; 3GME; -.
DR PDBsum; 3H1C; -.
DR PDBsum; 7OGK; -.
DR PDBsum; 7OGL; -.
DR PDBsum; 7OGM; -.
DR AlphaFoldDB; P05055; -.
DR SMR; P05055; -.
DR BioGRID; 4262431; 94.
DR BioGRID; 851985; 1.
DR ComplexPortal; CPX-403; RNA degradosome.
DR DIP; DIP-10522N; -.
DR IntAct; P05055; 45.
DR MINT; P05055; -.
DR STRING; 511145.b3164; -.
DR CarbonylDB; P05055; -.
DR SWISS-2DPAGE; P05055; -.
DR jPOST; P05055; -.
DR PaxDb; P05055; -.
DR PRIDE; P05055; -.
DR EnsemblBacteria; AAC76198; AAC76198; b3164.
DR EnsemblBacteria; BAE77210; BAE77210; BAE77210.
DR GeneID; 947672; -.
DR KEGG; ecj:JW5851; -.
DR KEGG; eco:b3164; -.
DR PATRIC; fig|1411691.4.peg.3566; -.
DR EchoBASE; EB0736; -.
DR eggNOG; COG1185; Bacteria.
DR HOGENOM; CLU_004217_2_2_6; -.
DR InParanoid; P05055; -.
DR OMA; LHILDVM; -.
DR PhylomeDB; P05055; -.
DR BioCyc; EcoCyc:EG10743-MON; -.
DR BioCyc; MetaCyc:EG10743-MON; -.
DR BRENDA; 2.7.7.8; 2026.
DR EvolutionaryTrace; P05055; -.
DR PRO; PR:P05055; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1990061; C:bacterial degradosome; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:EcoCyc.
DR GO; GO:0035438; F:cyclic-di-GMP binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004654; F:polyribonucleotide nucleotidyltransferase activity; IDA:EcoCyc.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IMP:EcoCyc.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IC:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.30.1370.10; -; 1.
DR Gene3D; 3.30.230.70; -; 2.
DR HAMAP; MF_01595; PNPase; 1.
DR InterPro; IPR001247; ExoRNase_PH_dom1.
DR InterPro; IPR015847; ExoRNase_PH_dom2.
DR InterPro; IPR036345; ExoRNase_PH_dom2_sf.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR012162; PNPase.
DR InterPro; IPR027408; PNPase/RNase_PH_dom_sf.
DR InterPro; IPR015848; PNPase_PH_RNA-bd_bac/org-type.
DR InterPro; IPR036456; PNPase_PH_RNA-bd_sf.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR11252; PTHR11252; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF03726; PNPase; 1.
DR Pfam; PF01138; RNase_PH; 2.
DR Pfam; PF03725; RNase_PH_C; 2.
DR Pfam; PF00575; S1; 1.
DR PIRSF; PIRSF005499; PNPase; 1.
DR SMART; SM00322; KH; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF46915; SSF46915; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF54211; SSF54211; 2.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55666; SSF55666; 2.
DR TIGRFAMs; TIGR03591; polynuc_phos; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Reference proteome; RNA-binding;
KW Stress response; Transferase.
FT CHAIN 1..711
FT /note="Polyribonucleotide nucleotidyltransferase"
FT /id="PRO_0000197913"
FT DOMAIN 553..612
FT /note="KH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT DOMAIN 622..690
FT /note="S1 motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01595"
FT REGION 77..80
FT /note="FFRR loop; important for RNA binding"
FT /evidence="ECO:0000305|PubMed:19327365"
FT REGION 327..331
FT /note="Interaction with RNase E"
FT /evidence="ECO:0000305|PubMed:19327365"
FT REGION 689..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:19327365"
FT BINDING 492
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000305|PubMed:19327365"
FT MUTAGEN 79..80
FT /note="RR->AA: Strongly reduces RNA binding. Reduces RNA
FT degradation."
FT /evidence="ECO:0000269|PubMed:18812438"
FT MUTAGEN 83
FT /note="R->A: No effect on RNA-binding. No effect on
FT degradation of long RNA molecules. Impairs degradation of
FT short RNA molecules."
FT /evidence="ECO:0000269|PubMed:18812438"
FT MUTAGEN 100
FT /note="R->D: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162954"
FT MUTAGEN 319
FT /note="R->A: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162954"
FT MUTAGEN 398..399
FT /note="RR->DD: Abolishes enzyme activity."
FT MUTAGEN 428
FT /note="V->P: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162954"
FT MUTAGEN 444
FT /note="C->W: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162954"
FT MUTAGEN 492
FT /note="D->G: Abolishes enzyme activity."
FT /evidence="ECO:0000269|PubMed:12162954"
FT CONFLICT 357
FT /note="G -> R (in Ref. 1; AAA83905)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="L -> S (in Ref. 1; AAA83905)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3CDI"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:7OGL"
FT HELIX 86..99
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 126..141
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 186..196
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 198..211
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3CDI"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 263..284
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 290..311
FT /evidence="ECO:0007829|PDB:3CDI"
FT TURN 315..318
FT /evidence="ECO:0007829|PDB:3CDJ"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 348..356
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 362..365
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 375..381
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 402..412
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 462..471
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 483..488
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 490..497
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 502..509
FT /evidence="ECO:0007829|PDB:3CDI"
FT HELIX 516..540
FT /evidence="ECO:0007829|PDB:3CDI"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:7OGK"
FT TURN 562..564
FT /evidence="ECO:0007829|PDB:7OGK"
FT HELIX 565..569
FT /evidence="ECO:0007829|PDB:7OGK"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:7OGL"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 591..598
FT /evidence="ECO:0007829|PDB:7OGK"
FT HELIX 602..615
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 624..633
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 642..645
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:7OGK"
FT HELIX 651..653
FT /evidence="ECO:0007829|PDB:7OGK"
FT STRAND 654..656
FT /evidence="ECO:0007829|PDB:7OGK"
FT TURN 660..665
FT /evidence="ECO:0007829|PDB:7OGL"
FT STRAND 671..679
FT /evidence="ECO:0007829|PDB:7OGK"
FT HELIX 681..683
FT /evidence="ECO:0007829|PDB:7OGL"
FT STRAND 685..688
FT /evidence="ECO:0007829|PDB:7OGK"
SQ SEQUENCE 711 AA; 77101 MW; 785B7D54716FC2DE CRC64;
MLNPIVRKFQ YGQHTVTLET GMMARQATAA VMVSMDDTAV FVTVVGQKKA KPGQDFFPLT
VNYQERTYAA GRIPGSFFRR EGRPSEGETL IARLIDRPIR PLFPEGFVNE VQVIATVVSV
NPQVNPDIVA MIGASAALSL SGIPFNGPIG AARVGYINDQ YVLNPTQDEL KESKLDLVVA
GTEAAVLMVE SEAQLLSEDQ MLGAVVFGHE QQQVVIQNIN ELVKEAGKPR WDWQPEPVNE
ALNARVAALA EARLSDAYRI TDKQERYAQV DVIKSETIAT LLAEDETLDE NELGEILHAI
EKNVVRSRVL AGEPRIDGRE KDMIRGLDVR TGVLPRTHGS ALFTRGETQA LVTATLGTAR
DAQVLDELMG ERTDTFLFHY NFPPYSVGET GMVGSPKRRE IGHGRLAKRG VLAVMPDMDK
FPYTVRVVSE ITESNGSSSM ASVCGASLAL MDAGVPIKAA VAGIAMGLVK EGDNYVVLSD
ILGDEDHLGD MDFKVAGSRD GISALQMDIK IEGITKEIMQ VALNQAKGAR LHILGVMEQA
INAPRGDISE FAPRIHTIKI NPDKIKDVIG KGGSVIRALT EETGTTIEIE DDGTVKIAAT
DGEKAKHAIR RIEEITAEIE VGRVYTGKVT RIVDFGAFVA IGGGKEGLVH ISQIADKRVE
KVTDYLQMGQ EVPVKVLEVD RQGRIRLSIK EATEQSQPAA APEAPAAEQG E
