ID MTNN_ECOLI Reviewed; 232 AA. AC P0AF12; P24247; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 1. DT 02-SEP-2026, entry version 151. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000303|PubMed:16101288}; DE Short=MTA/SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTAN {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000303|PubMed:16101288}; DE EC=3.2.2.9 {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000269|PubMed:15911379, ECO:0000269|PubMed:16101288, ECO:0000269|PubMed:3911944}; DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:15911379}; DE Short=DOA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:15911379}; DE Short=dAdo nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305|PubMed:15911379}; DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=AdoHcy nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SRH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; GN Name=mtnN {ECO:0000255|HAMAP-Rule:MF_01684}; Synonyms=mtn, pfs, yadA; GN OrderedLocusNames=b0159, JW0155; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=2157212; DOI=10.1073/pnas.87.7.2740; RA Wurgler S.M., Richardson C.C.; RT "Structure and regulation of the gene for dGTP triphosphohydrolase from RT Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2740-2744(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=9524204; DOI=10.1016/s0167-4781(97)00169-3; RA Cornell K.A., Riscoe M.K.; RT "Cloning and expression of Escherichia coli 5'-methylthioadenosine/S- RT adenosylhomocysteine nucleosidase: identification of the pfs gene RT product."; RL Biochim. Biophys. Acta 1396:8-14(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8202364; DOI=10.1093/nar/22.9.1637; RA Fujita N., Mori H., Yura T., Ishihama A.; RT "Systematic sequencing of the Escherichia coli genome: analysis of the 2.4- RT 4.1 min (110,917-193,643 bp) region."; RL Nucleic Acids Res. 22:1637-1639(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.; RT "Sequence of minutes 4-25 of Escherichia coli."; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. 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 FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=3911944; DOI=10.1042/bj2320335; RA Della Ragione F., Porcelli M., Carteni-Farina M., Zappia V., Pegg A.E.; RT "Escherichia coli S-adenosylhomocysteine/5'-methylthioadenosine RT nucleosidase. Purification, substrate specificity and mechanism of RT action."; RL Biochem. J. 232:335-341(1985). RN [8] RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION. RX PubMed=8941345; DOI=10.1006/bbrc.1996.1723; RA Cornell K.A., Swarts W.E., Barry R.D., Riscoe M.K.; RT "Characterization of recombinant Eschericha coli 5'-methylthioadenosine/S- RT adenosylhomocysteine nucleosidase: analysis of enzymatic activity and RT substrate specificity."; RL Biochem. Biophys. Res. Commun. 228:724-732(1996). 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, KINETIC PARAMETERS, AND MUTAGENESIS OF MET-9; RP GLU-12; ILE-50; SER-76; PHE-151; MET-173; GLU-174; ARG-193; SER-196; RP ASP-197 AND PHE-207. RX PubMed=16101288; DOI=10.1021/bi050493q; RA Lee J.E., Luong W., Huang D.J., Cornell K.A., Riscoe M.K., Howell P.L.; RT "Mutational analysis of a nucleosidase involved in quorum-sensing RT autoinducer-2 biosynthesis."; RL Biochemistry 44:11049-11057(2005). RN [11] RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE. RX PubMed=15911379; DOI=10.1016/j.chembiol.2005.04.012; RA Choi-Rhee E., Cronan J.E.; RT "A nucleosidase required for in vivo function of the S-adenosyl-L- RT methionine radical enzyme, biotin synthase."; RL Chem. Biol. 12:589-593(2005). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH SUBSTRATE, AND RP SUBUNIT. RX PubMed=11591349; DOI=10.1016/s0969-2126(01)00656-6; RA Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.; RT "Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine RT nucleosidase reveals similarity to the purine nucleoside phosphorylases."; RL Structure 9:941-953(2001). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, RP AND ACTIVITY REGULATION. RX PubMed=12496243; DOI=10.1074/jbc.m210836200; RA Lee J.E., Cornell K.A., Riscoe M.K., Howell P.L.; RT "Structure of Escherichia coli 5'-methylthioadenosine/ S- RT adenosylhomocysteine nucleosidase inhibitor complexes provide insight into RT the conformational changes required for substrate binding and catalysis."; RL J. Biol. Chem. 278:8761-8770(2003). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, RP AND ACTIVITY REGULATION. RX PubMed=15749708; DOI=10.1074/jbc.m414472200; RA Singh V., Evans G.B., Lenz D.H., Mason J.M., Clinch K., Mee S., RA Painter G.F., Tyler P.C., Furneaux R.H., Lee J.E., Howell P.L., RA Schramm V.L.; RT "Femtomolar transition state analogue inhibitors of 5'- RT methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia RT coli."; RL J. Biol. Chem. 280:18265-18273(2005). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF WILD-TYPE AND MUTANTS ASN-197 AND RP GLN-12 IN COMPLEX WITH MTA SUBSTRATE OR PRODUCTS, REACTION MECHANISM, AND RP ACTIVE SITES. RX PubMed=16109423; DOI=10.1016/j.jmb.2005.07.027; RA Lee J.E., Smith G.D., Horvatin C., Huang D.J., Cornell K.A., Riscoe M.K., RA Howell P.L.; RT "Structural snapshots of MTA/AdoHcy nucleosidase along the reaction RT coordinate provide insights into enzyme and nucleoside flexibility during RT catalysis."; RL J. Mol. Biol. 352:559-574(2005). CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in CC both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine CC (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- CC methylthioribose and S-ribosylhomocysteine, respectively CC (PubMed:16101288, PubMed:3911944). Also cleaves 5'-deoxyadenosine, a CC toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5- CC deoxyribose and adenine. Thus, is required for in vivo function of the CC radical SAM enzymes biotin synthase and lipoic acid synthase, that are CC inhibited by 5'-deoxyadenosine accumulation (PubMed:15911379). Can also CC use 5'-isobutylthioadenosine, 5'-n-butylthioadenosine, S-adenosyl-D- CC homocysteine, decarboxylated adenosylhomocysteine, deaminated CC adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates in CC vitro (PubMed:3911944). {ECO:0000269|PubMed:15911379, CC ECO:0000269|PubMed:16101288, ECO:0000269|PubMed:3911944}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L- CC homocysteine + adenine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01684, CC ECO:0000269|PubMed:16101288, ECO:0000269|PubMed:3911944}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-methyl-5'-thioadenosine + H2O = 5-(methylsulfanyl)-D-ribose CC + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01684, CC ECO:0000269|PubMed:16101288, ECO:0000269|PubMed:3911944}; CC -!- CATALYTIC ACTIVITY: CC Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine; CC Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01684, CC ECO:0000269|PubMed:15911379}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01684, CC ECO:0000269|PubMed:15911379}; CC -!- ACTIVITY REGULATION: Strongly inhibited by aryl-substituted MTA CC analogs, alkyl-substituted MTA analogs, 5'-methylthioformycin, 5'- CC chloroformycin, S-formycinylhomocysteine, 5'-methylthiotubercidin, S- CC tubercidinylhomocysteine and S-8-aza-adenosylhomocysteine. Poorly CC inhibited by 5'-isobutylthioinosine, 5'-n-butylthioinosine, 5'- CC methylthio-3-deaza-adenosine, 5'-isobutylthio-3-deaza-adenosine, S-n-6- CC methyl-3-deaza-adenosylhomocysteine, S-adenosylhomocysteine sulphoxide CC and Sinefungin. {ECO:0000269|PubMed:12496243, CC ECO:0000269|PubMed:15749708, ECO:0000269|PubMed:3911944, CC ECO:0000269|PubMed:8941345}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.4 uM for 5'-methylthioadenosine (at pH 7 and 37 degrees Celsius) CC {ECO:0000269|PubMed:3911944}; CC KM=0.8 uM for 5'-methylthioadenosine (at pH 7 and 22 degrees Celsius) CC {ECO:0000269|PubMed:16101288}; CC KM=4.3 uM for S-adenosylhomocysteine (at pH 7 and 37 degrees Celsius) CC {ECO:0000269|PubMed:3911944}; CC KM=1.3 uM for S-adenosylhomocysteine (at pH 7 and 22 degrees Celsius) CC {ECO:0000269|PubMed:16101288}; CC Note=kcat is 3.0 sec(-1) and 2.6 sec(-1) with 5'-methylthioadenosine CC and S-adenosylhomocysteine as substrate, respectively. CC {ECO:0000269|PubMed:16101288}; CC pH dependence: CC Exhibits activity across a broad pH range. Enzyme activity is CC moderately improved under acidic conditions. CC {ECO:0000269|PubMed:8941345}; CC Temperature dependence: CC Optimum temperature is 37-45 degrees Celsius. Rapidly inactivated CC after exposure for 10 minutes at 55 degrees Celsius. CC {ECO:0000269|PubMed:8941345}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'- CC thioadenosine (hydrolase route): step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01684}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01684, CC ECO:0000269|PubMed:11591349, ECO:0000269|PubMed:12496243, CC ECO:0000269|PubMed:15749708, ECO:0000269|PubMed:16109423}. CC -!- INTERACTION: CC P0AF12; P0AF12: mtnN; NbExp=2; IntAct=EBI-1114261, EBI-1114261; CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are deficient in biotin CC synthase (BioB) activity in vivo due to accumulation of 5'- CC deoxyadenosine. {ECO:0000269|PubMed:15911379}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01684, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA23678.1; Type=Erroneous initiation; 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; M31772; AAA23678.1; ALT_INIT; Genomic_DNA. DR EMBL; U24438; AAC38291.1; -; Genomic_DNA. DR EMBL; M83735; AAA24322.1; -; Genomic_DNA. DR EMBL; U70214; AAB08589.1; -; Genomic_DNA. DR EMBL; U00096; AAC73270.1; -; Genomic_DNA. DR EMBL; AP009048; BAB96736.1; -; Genomic_DNA. DR PIR; S45227; S45227. DR RefSeq; NP_414701.1; NC_000913.3. DR RefSeq; WP_000689844.1; NZ_CP009789.1. DR PDB; 1JYS; X-ray; 1.90 A; A/B=1-232. DR PDB; 1NC1; X-ray; 2.00 A; A/B=1-232. DR PDB; 1NC3; X-ray; 2.20 A; A/B=1-232. DR PDB; 1Y6Q; X-ray; 2.20 A; A/B=1-232. DR PDB; 1Y6R; X-ray; 2.20 A; A/B=1-232. DR PDB; 1Z5N; X-ray; 2.10 A; A/B=1-232. DR PDB; 1Z5O; X-ray; 2.00 A; A/B=1-232. DR PDB; 1Z5P; X-ray; 2.00 A; A=1-232. DR PDB; 3O4V; X-ray; 1.75 A; A/B=1-232. DR PDB; 4WKC; X-ray; 1.64 A; A=1-232. DR PDB; 4YML; X-ray; 1.75 A; A=1-232. DR AlphaFoldDB; P0AF12; -. DR MDposit; P0AF12; -. DR MDRepo; P0AF12; -. DR SMR; P0AF12; -. DR BioGRID; 4260991; 46. DR BioGRID; 852836; 1. DR DIP; DIP-10270N; -. DR FunCoup; P0AF12; 323. DR IntAct; P0AF12; 7. DR STRING; 511145.b0159; -. DR BindingDB; P0AF12; -. DR DrugBank; DB02158; (2S,3S,4R,5S)-2-(4-Amino-4,5-dihydro-1H-pyrrolo[3,2-d]pyrimidin-7-yl)-5-[(methylsulfanyl)methyl]-3,4-pyrrolidinediol. DR DrugBank; DB08606; (3R,4S)-1-[(4-AMINO-5H-PYRROLO[3,2-D]PYRIMIDIN-7-YL)METHYL]-4-[(METHYLSULFANYL)METHYL]PYRROLIDIN-3-OL. DR DrugBank; DB02933; 5'-Deoxy-5'-(Methylthio)-Tubercidin. DR DrugBank; DB00173; Adenine. DR DrugBank; DB02281; Formycin. DR jPOST; P0AF12; -. DR PaxDb; 511145-b0159; -. DR EnsemblBacteria; AAC73270; AAC73270; b0159. DR GeneID; 93777267; -. DR GeneID; 948542; -. DR KEGG; ecj:JW0155; -. DR KEGG; eco:b0159; -. DR KEGG; ecoc:C3026_00725; -. DR PATRIC; fig|1411691.4.peg.2121; -. DR EchoBASE; EB1082; -. DR eggNOG; COG0775; Bacteria. DR HOGENOM; CLU_031248_2_2_6; -. DR InParanoid; P0AF12; -. DR OMA; DQFVHSK; -. DR OrthoDB; 9792278at2; -. DR PhylomeDB; P0AF12; -. DR BioCyc; EcoCyc:EG11090-MONOMER; -. DR BioCyc; MetaCyc:EG11090-MONOMER; -. DR BRENDA; 3.2.2.16; 2026. DR BRENDA; 3.2.2.30; 2026. DR BRENDA; 3.2.2.9; 2026. DR SABIO-RK; P0AF12; -. DR UniPathway; UPA00904; UER00871. DR EvolutionaryTrace; P0AF12; -. DR PRO; PR:P0AF12; -. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IDA:EcoCyc. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0046124; P:purine deoxyribonucleoside catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0110052; P:toxic metabolite repair; IMP:UniProtKB. DR CDD; cd09008; MTAN; 1. DR FunFam; 3.40.50.1580:FF:000001; MTA/SAH nucleosidase family protein; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR HAMAP; MF_01684; Salvage_MtnN; 1. DR InterPro; IPR010049; MTA_SAH_Nsdase. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR NCBIfam; TIGR01704; MTA_SAH-Nsdase; 1. DR NCBIfam; NF004079; PRK05584.1; 1. DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1. DR PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PDBsum; 1JYS; -. DR PDBsum; 1NC1; -. DR PDBsum; 1NC3; -. DR PDBsum; 1Y6Q; -. DR PDBsum; 1Y6R; -. DR PDBsum; 1Z5N; -. DR PDBsum; 1Z5O; -. DR PDBsum; 1Z5P; -. DR PDBsum; 3O4V; -. DR PDBsum; 4WKC; -. DR PDBsum; 4YML; -. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis; KW Reference proteome. FT CHAIN 1..232 FT /note="5'-methylthioadenosine/S-adenosylhomocysteine FT nucleosidase" FT /id="PRO_0000164439" FT ACT_SITE 12 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684, FT ECO:0000305|PubMed:16109423" FT ACT_SITE 197 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684, FT ECO:0000305|PubMed:16109423" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684, FT ECO:0000269|PubMed:11591349" FT BINDING 152 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684, FT ECO:0000269|PubMed:11591349" FT BINDING 173..174 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" FT MUTAGEN 9 FT /note="M->A: 13-19% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 12 FT /note="E->A,Q: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 50 FT /note="I->A: 12-23% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 76 FT /note="S->A: 13-23% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 151 FT /note="F->A: 0.5% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 173 FT /note="M->A: 0.5% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 174 FT /note="E->A,Q: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 193 FT /note="R->A: 13-28% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 196 FT /note="S->A: 2-4% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 197 FT /note="D->A,N: Loss of catalytic activity." FT /evidence="ECO:0000269|PubMed:16101288" FT MUTAGEN 207 FT /note="F->A: 2% of wild-type catalytic efficiency." FT /evidence="ECO:0000269|PubMed:16101288" FT CONFLICT 212..232 FT /note="AVAAKQSSLMVESLVQKLAHG -> LLPLNSPA (in Ref. 1; FT AAA23678/AAA24322)" FT /evidence="ECO:0000305" FT STRAND 2..9 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 10..17 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 21..28 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 31..38 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 41..47 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 52..66 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 69..79 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 89..99 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 117..120 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 123..135 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 140..147 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 155..164 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 168..174 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 175..185 FT /evidence="ECO:0007829|PDB:3O4V" FT STRAND 189..197 FT /evidence="ECO:0007829|PDB:3O4V" FT HELIX 203..231 FT /evidence="ECO:0007829|PDB:3O4V" SQ SEQUENCE 232 AA; 24354 MW; 9B1FF9BEC39D4F2C CRC64; MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK ADDKLIAAAE ACIAELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG //