ID RIR1_ECOLI Reviewed; 761 AA. AC P00452; P78088; P78177; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Ribonucleoside-diphosphate reductase 1 subunit alpha; DE EC=1.17.4.1; DE AltName: Full=Protein B1; DE AltName: Full=Ribonucleoside-diphosphate reductase 1 R1 subunit; DE AltName: Full=Ribonucleotide reductase 1; GN Name=nrdA; Synonyms=dnaF; OrderedLocusNames=b2234, JW2228; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6087316; DOI=10.1073/pnas.81.14.4294; RA Carlson J., Fuchs J.A., Messing J.; RT "Primary structure of the Escherichia coli ribonucleoside diphosphate RT reductase operon."; RL Proc. Natl. Acad. Sci. U.S.A. 81:4294-4297(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=3287341; DOI=10.1093/nar/16.9.4174; RA Nilsson O., Aaberg A., Lundqvist T., Sjoeberg B.-M.; RT "Nucleotide sequence of the gene coding for the large subunit of RT ribonucleotide reductase of Escherichia coli. Correction."; RL Nucleic Acids Res. 16:4174-4174(1988). RN [3] RP SEQUENCE REVISION TO 526-527. RA Sjoeberg B.-M.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=9205837; DOI=10.1093/dnares/4.2.91; RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S., RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.; RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of RT its sequence features."; RL DNA Res. 4:91-113(1997). 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 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 [7] RP PARTIAL PROTEIN SEQUENCE. RX PubMed=3894026; DOI=10.1111/j.1432-1033.1985.tb09037.x; RA Sjoeberg B.-M., Eriksson S., Joernvall H., Carlquist M., Eklund H.; RT "Protein B1 of ribonucleotide reductase. Direct analytical data and RT comparisons with data indirectly deduced from the nucleotide sequence of RT the Escherichia coli nrdA gene."; RL Eur. J. Biochem. 150:423-427(1985). RN [8] RP ACTIVE SITES. RX PubMed=2663852; DOI=10.1016/s0021-9258(18)63849-9; RA Aaberg A., Hahne S., Karlsson M., Larsson A., Ormoe M., Aahgren A., RA Sjoeberg B.-M.; RT "Evidence for two different classes of redox-active cysteines in RT ribonucleotide reductase of Escherichia coli."; RL J. Biol. Chem. 264:12249-12252(1989). RN [9] RP ACTIVE SITES, AND MUTAGENESIS OF TYR-730 AND TYR-731. RX PubMed=8702814; DOI=10.1074/jbc.271.34.20655; RA Ekberg M., Sahlin M., Eriksson M., Sjoberg B.M.; RT "Two conserved tyrosine residues in protein R1 participate in an RT intermolecular electron transfer in ribonucleotide reductase."; RL J. Biol. Chem. 271:20655-20659(1996). RN [10] RP ACTIVITY REGULATION, AND INDUCTION BY HYDROXYUREA. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024; RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., RA Walker G.C.; RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia RT coli."; RL Mol. Cell 36:845-860(2009). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX PubMed=8052308; DOI=10.1038/370533a0; RA Uhlin U., Eklund H.; RT "Structure of ribonucleotide reductase protein R1."; RL Nature 370:533-539(1994). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF MUTANTS ALA-441; ASP-441 AND RP GLN-441, DISULFIDE BOND, SUBUNIT, ACTIVE SITE, ACTIVITY REGULATION, ENZYME RP MECHANISM, AND MUTAGENESIS OF GLU-441. RX PubMed=9395490; DOI=10.1074/jbc.272.50.31533; RA Persson A.L., Eriksson M., Katterle B., Potsch S., Sahlin M., Sjoberg B.M.; RT "A new mechanism-based radical intermediate in a mutant R1 protein RT affecting the catalytically essential Glu441 in Escherichia coli RT ribonucleotide reductase."; RL J. Biol. Chem. 272:31533-31541(1997). RN [14] {ECO:0007744|PDB:1R1R, ECO:0007744|PDB:2R1R, ECO:0007744|PDB:3R1R, ECO:0007744|PDB:4R1R} RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEXES WITH ATP; GDP AND DTTP, RP DISULFIDE BOND, SUBUNIT, AND ACTIVITY REGULATION. RX PubMed=9309223; DOI=10.1016/s0969-2126(97)00259-1; RA Eriksson M., Uhlin U., Ramaswamy S., Ekberg M., Regnstroem K., RA Sjoeberg B.-M., Eklund H.; RT "Binding of allosteric effectors to ribonucleotide reductase protein R1: RT reduction of active-site cysteines promotes substrate binding."; RL Structure 5:1077-1092(1997). RN [15] RP STRUCTURE BY NMR OF 737-761, AND BINDING SITES. RX PubMed=10493864; DOI=10.1006/jmbi.1999.3067; RA Berardi M.J., Bushweller J.H.; RT "Binding specificity and mechanistic insight into glutaredoxin-catalyzed RT protein disulfide reduction."; RL J. Mol. Biol. 292:151-161(1999). CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis. CC Catalyzes the biosynthesis of deoxyribonucleotides from the CC corresponding ribonucleotides. R1 contains the binding sites for both CC substrates and allosteric effectors and carries out the actual CC reduction of the ribonucleotide. It also provides redox-active CC cysteines. CC -!- CATALYTIC ACTIVITY: CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'- CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'- CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA- CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1; CC -!- ACTIVITY REGULATION: Under complex allosteric control mediated by CC deoxynucleoside triphosphates and ATP binding to separate specificity CC and activation sites on the alpha subunit. The type of nucleotide bound CC at the specificity site determines substrate preference. It seems CC probable that ATP makes the enzyme reduce CDP and UDP, dGTP favors ADP CC reduction and dTTP favors GDP reduction. Stimulated by ATP and CC inhibited by dATP binding to the activity site. In vitro, its activity CC is increased by dithiothreitol (DTT) or thioredoxins (non-specific). CC Inhibited by hydroxyurea, leads to dNTP depletion, replication fork CC arrest and genomic instability (PubMed:20005847). CC {ECO:0000269|PubMed:9309223, ECO:0000269|PubMed:9395490, CC ECO:0000305|PubMed:20005847}. CC -!- SUBUNIT: Tetramer of two alpha (R1) and two beta (R2) subunits. The B1 CC protein is a dimer of alpha subunits. A radical transfer pathway occurs CC between 'Tyr-122' of R2 and R1. {ECO:0000269|PubMed:9309223, CC ECO:0000269|PubMed:9395490}. CC -!- INTERACTION: CC P00452; P00452: nrdA; NbExp=3; IntAct=EBI-370018, EBI-370018; CC P00452; P69924: nrdB; NbExp=11; IntAct=EBI-370018, EBI-555196; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=Alpha; CC IsoId=P00452-1; Sequence=Displayed; CC Name=Alpha'; CC IsoId=P00452-2; Sequence=VSP_018871, VSP_018872; CC -!- INDUCTION: Induced 5-fold by hydroxyurea (at protein level). CC {ECO:0000269|PubMed:20005847}. CC -!- PTM: Binding of the substrate occurs primarily when the active-site CC cysteines are reduced. CC -!- MISCELLANEOUS: E.coli produces two separate class I enzymes. This one CC is the functional enzyme during growth. CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: one CC controls substrate specificity and the other regulates the overall CC catalytic activity. A substrate-binding catalytic site, located on R1, CC is formed only in the presence of the second subunit R2. CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large CC chain family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA24223.1; Type=Miscellaneous discrepancy; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; K02672; AAA24223.1; ALT_SEQ; Genomic_DNA. DR EMBL; X06999; CAA30056.2; -; Genomic_DNA. DR EMBL; U00096; AAC75294.1; -; Genomic_DNA. DR EMBL; AP009048; BAA16053.1; -; Genomic_DNA. DR PIR; H64993; RDEC1R. DR RefSeq; NP_416737.1; NC_000913.3. DR RefSeq; WP_001075164.1; NZ_STEB01000002.1. DR PDB; 1QFN; NMR; -; B=737-761. DR PDB; 1R1R; X-ray; 2.90 A; A/B/C=1-761. DR PDB; 1RLR; X-ray; 2.50 A; A=1-761. DR PDB; 2R1R; X-ray; 3.00 A; A/B/C=1-761. DR PDB; 2X0X; X-ray; 2.30 A; A/B/C=1-761. DR PDB; 2XAK; X-ray; 2.80 A; A/B/C=1-761. DR PDB; 2XAP; X-ray; 2.10 A; A/B/C=1-761. DR PDB; 2XAV; X-ray; 2.80 A; A/B/C=1-761. DR PDB; 2XAW; X-ray; 3.10 A; A/B/C=1-761. DR PDB; 2XAX; X-ray; 2.75 A; A/B/C=1-761. DR PDB; 2XAY; X-ray; 2.65 A; A/B/C=1-761. DR PDB; 2XAZ; X-ray; 2.60 A; A/B/C=1-761. DR PDB; 2XO4; X-ray; 2.50 A; A/B/C=1-761. DR PDB; 2XO5; X-ray; 2.70 A; A/B/C=1-761. DR PDB; 3R1R; X-ray; 3.00 A; A/B/C=1-761. DR PDB; 3UUS; X-ray; 5.65 A; A/B/C/D=1-761. DR PDB; 4ERM; X-ray; 3.95 A; A/B/C/D=1-761. DR PDB; 4ERP; X-ray; 4.45 A; A/B/C/D=1-761. DR PDB; 4R1R; X-ray; 3.20 A; A/B/C=1-761. DR PDB; 5CNS; X-ray; 2.98 A; A/B/C/D=1-761. DR PDB; 5CNT; X-ray; 3.25 A; A/B/C/D=1-761. DR PDB; 5CNU; X-ray; 3.40 A; A/B/C/D=1-761. DR PDB; 5CNV; X-ray; 3.20 A; A/B/C/D=1-761. DR PDB; 5R1R; X-ray; 3.10 A; A/B/C=1-761. DR PDB; 6R1R; X-ray; 3.10 A; A/B/C=1-761. DR PDB; 6W4X; EM; 3.60 A; A/B=1-761. DR PDB; 7R1R; X-ray; 3.10 A; A/B/C=1-761. DR PDBsum; 1QFN; -. DR PDBsum; 1R1R; -. DR PDBsum; 1RLR; -. DR PDBsum; 2R1R; -. DR PDBsum; 2X0X; -. DR PDBsum; 2XAK; -. DR PDBsum; 2XAP; -. DR PDBsum; 2XAV; -. DR PDBsum; 2XAW; -. DR PDBsum; 2XAX; -. DR PDBsum; 2XAY; -. DR PDBsum; 2XAZ; -. DR PDBsum; 2XO4; -. DR PDBsum; 2XO5; -. DR PDBsum; 3R1R; -. DR PDBsum; 3UUS; -. DR PDBsum; 4ERM; -. DR PDBsum; 4ERP; -. DR PDBsum; 4R1R; -. DR PDBsum; 5CNS; -. DR PDBsum; 5CNT; -. DR PDBsum; 5CNU; -. DR PDBsum; 5CNV; -. DR PDBsum; 5R1R; -. DR PDBsum; 6R1R; -. DR PDBsum; 6W4X; -. DR PDBsum; 7R1R; -. DR AlphaFoldDB; P00452; -. DR EMDB; EMD-21540; -. DR SMR; P00452; -. DR BioGRID; 4262130; 184. DR ComplexPortal; CPX-1075; Ribonucleoside-diphosphate reductase 1 complex. DR DIP; DIP-584N; -. DR IntAct; P00452; 10. DR STRING; 511145.b2234; -. DR iPTMnet; P00452; -. DR jPOST; P00452; -. DR PaxDb; 511145-b2234; -. DR EnsemblBacteria; AAC75294; AAC75294; b2234. DR GeneID; 946612; -. DR KEGG; ecj:JW2228; -. DR KEGG; eco:b2234; -. DR PATRIC; fig|1411691.4.peg.1; -. DR EchoBASE; EB0654; -. DR eggNOG; COG0209; Bacteria. DR HOGENOM; CLU_000404_3_0_6; -. DR InParanoid; P00452; -. DR OMA; QMSSCYL; -. DR OrthoDB; 9762933at2; -. DR PhylomeDB; P00452; -. DR BioCyc; EcoCyc:NRDA-MONOMER; -. DR BioCyc; MetaCyc:NRDA-MONOMER; -. DR BRENDA; 1.17.4.1; 2026. DR SABIO-RK; P00452; -. DR EvolutionaryTrace; P00452; -. DR PRO; PR:P00452; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0005971; C:ribonucleoside-diphosphate reductase complex; IDA:EcoliWiki. DR GO; GO:0005524; F:ATP binding; IDA:EcoliWiki. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0044183; F:protein folding chaperone; EXP:DisProt. DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IDA:EcoCyc. DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IDA:ComplexPortal. DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IDA:EcoliWiki. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IDA:EcoliWiki. DR GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IDA:ComplexPortal. DR CDD; cd01679; RNR_I; 1. DR DisProt; DP02715; -. DR Gene3D; 1.10.1650.20; -; 1. DR Gene3D; 3.20.70.20; -; 1. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR013346; NrdE_NrdA_C. DR InterPro; IPR000788; RNR_lg_C. DR InterPro; IPR013509; RNR_lsu_N. DR InterPro; IPR008926; RNR_R1-su_N. DR InterPro; IPR039718; Rrm1. DR NCBIfam; TIGR02506; NrdE_NrdA; 1. DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1. DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1. DR Pfam; PF03477; ATP-cone; 1. DR Pfam; PF02867; Ribonuc_red_lgC; 1. DR Pfam; PF00317; Ribonuc_red_lgN; 1. DR PRINTS; PR01183; RIBORDTASEM1. DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1. DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS00089; RIBORED_LARGE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Alternative initiation; KW ATP-binding; Deoxyribonucleotide synthesis; Direct protein sequencing; KW Disulfide bond; Nucleotide-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..761 FT /note="Ribonucleoside-diphosphate reductase 1 subunit FT alpha" FT /id="PRO_0000030596" FT DOMAIN 5..95 FT /note="ATP-cone" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00492" FT ACT_SITE 437 FT /note="Proton acceptor" FT ACT_SITE 439 FT /note="Cysteine radical intermediate" FT ACT_SITE 441 FT /note="Proton acceptor" FT BINDING 9 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:3R1R" FT BINDING 15..21 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:3R1R" FT BINDING 55 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:3R1R" FT BINDING 91 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="allosteric activator" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:3R1R" FT BINDING 209 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 232..234 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 262 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 269 FT /ligand="dTTP" FT /ligand_id="ChEBI:CHEBI:37568" FT /ligand_note="allosteric effector that controls substrate FT specificity" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 437 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 441 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT BINDING 623..625 FT /ligand="GDP" FT /ligand_id="ChEBI:CHEBI:58189" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0007744|PDB:4R1R" FT SITE 225 FT /note="Important for hydrogen atom transfer" FT SITE 462 FT /note="Important for hydrogen atom transfer" FT SITE 730 FT /note="Important for electron transfer" FT SITE 731 FT /note="Important for electron transfer" FT SITE 754 FT /note="Interacts with thioredoxin/glutaredoxin" FT SITE 759 FT /note="Interacts with thioredoxin/glutaredoxin" FT MOD_RES 283 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT DISULFID 225..462 FT /note="Redox-active" FT /evidence="ECO:0000269|PubMed:9309223, FT ECO:0000269|PubMed:9395490" FT VAR_SEQ 1..25 FT /note="Missing (in isoform Alpha')" FT /evidence="ECO:0000305" FT /id="VSP_018871" FT VAR_SEQ 26 FT /note="L -> M (in isoform Alpha')" FT /evidence="ECO:0000305" FT /id="VSP_018872" FT VARIANT 1..2 FT /note="Missing (in 15% of the chains)" FT VARIANT 1 FT /note="Missing (in 30% of the chains)" FT MUTAGEN 441 FT /note="E->A,Q: Loss of activity." FT /evidence="ECO:0000269|PubMed:9395490" FT MUTAGEN 441 FT /note="E->D: Decrease in activity." FT /evidence="ECO:0000269|PubMed:9395490" FT MUTAGEN 730 FT /note="Y->F: Loss of activity." FT /evidence="ECO:0000269|PubMed:8702814" FT MUTAGEN 731 FT /note="Y->F: Loss of activity." FT /evidence="ECO:0000269|PubMed:8702814" FT STRAND 6..8 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 14..16 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 19..30 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 38..46 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 55..68 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 77..94 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 95..98 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 102..111 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 118..122 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 125..134 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 145..154 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 160..162 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 169..180 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 186..188 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 189..201 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 204..206 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 209..214 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:5CNS" FT STRAND 225..229 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 234..248 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 253..257 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:1RLR" FT HELIX 274..276 FT /evidence="ECO:0007829|PDB:5R1R" FT HELIX 278..289 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 290..292 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 296..299 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 301..307 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 313..317 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 326..328 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 333..339 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 341..349 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 352..356 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 358..360 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 364..370 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 372..384 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 386..388 FT /evidence="ECO:0007829|PDB:2XAX" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 395..409 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 412..416 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 419..422 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 423..426 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 428..430 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 438..440 FT /evidence="ECO:0007829|PDB:5CNS" FT STRAND 463..468 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 469..471 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 475..477 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 478..495 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 501..510 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 513..518 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 520..526 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 531..534 FT /evidence="ECO:0007829|PDB:2X0X" FT HELIX 537..562 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 568..570 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 573..575 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 579..582 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 585..589 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 599..609 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 612..614 FT /evidence="ECO:0007829|PDB:2XO5" FT HELIX 624..628 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 639..645 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:5CNS" FT STRAND 652..655 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 659..662 FT /evidence="ECO:0007829|PDB:2XAP" FT TURN 663..665 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 669..671 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 672..675 FT /evidence="ECO:0007829|PDB:2XAK" FT HELIX 676..686 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 697..699 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 701..703 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 705..707 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 711..723 FT /evidence="ECO:0007829|PDB:2XAP" FT STRAND 732..734 FT /evidence="ECO:0007829|PDB:2XAP" FT HELIX 738..741 FT /evidence="ECO:0007829|PDB:1RLR" SQ SEQUENCE 761 AA; 85775 MW; 7E034F154567C3FC CRC64; MNQNLLVTKR DGSTERINLD KIHRVLDWAA EGLHNVSISQ VELRSHIQFY DGIKTSDIHE TIIKAAADLI SRDAPDYQYL AARLAIFHLR KKAYGQFEPP ALYDHVVKMV EMGKYDNHLL EDYTEEEFKQ MDTFIDHDRD MTFSYAAVKQ LEGKYLVQNR VTGEIYESAQ FLYILVAACL FSNYPRETRL QYVKRFYDAV STFKISLPTP IMSGVRTPTR QFSSCVLIEC GDSLDSINAT SSAIVKYVSQ RAGIGINAGR IRALGSPIRG GEAFHTGCIP FYKHFQTAVK SCSQGGVRGG AATLFYPMWH LEVESLLVLK NNRGVEGNRV RHMDYGVQIN KLMYTRLLKG EDITLFSPSD VPGLYDAFFA DQEEFERLYT KYEKDDSIRK QRVKAVELFS LMMQERASTG RIYIQNVDHC NTHSPFDPAI APVRQSNLCL EIALPTKPLN DVNDENGEIA LCTLSAFNLG AINNLDELEE LAILAVRALD ALLDYQDYPI PAAKRGAMGR RTLGIGVINF AYYLAKHGKR YSDGSANNLT HKTFEAIQYY LLKASNELAK EQGACPWFNE TTYAKGILPI DTYKKDLDTI ANEPLHYDWE ALRESIKTHG LRNSTLSALM PSETSSQISN ATNGIEPPRG YVSIKASKDG ILRQVVPDYE HLHDAYELLW EMPGNDGYLQ LVGIMQKFID QSISANTNYD PSRFPSGKVP MQQLLKDLLT AYKFGVKTLY YQNTRDGAED AQDDLVPSIQ DDGCESGACK I //