MTNN_ECOLI
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 03-AUG-2022, entry version 135.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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:3911944, PubMed:16101288). 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=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-
CC ribos-5-yl)-L-homocysteine; 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=H2O + S-methyl-5'-thioadenosine = 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};
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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_SSZK01000004.1.
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 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; -.
DR AlphaFoldDB; P0AF12; -.
DR SMR; P0AF12; -.
DR BioGRID; 4260991; 38.
DR BioGRID; 852836; 1.
DR DIP; DIP-10270N; -.
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 SWISS-2DPAGE; P0AF12; -.
DR jPOST; P0AF12; -.
DR PaxDb; P0AF12; -.
DR PRIDE; P0AF12; -.
DR EnsemblBacteria; AAC73270; AAC73270; b0159.
DR EnsemblBacteria; BAB96736; BAB96736; BAB96736.
DR GeneID; 66671551; -.
DR GeneID; 948542; -.
DR KEGG; ecj:JW0155; -.
DR KEGG; eco:b0159; -.
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 PhylomeDB; P0AF12; -.
DR BioCyc; EcoCyc:EG11090-MON; -.
DR BioCyc; MetaCyc:EG11090-MON; -.
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; UP000000318; Chromosome.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; 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 Gene3D; 3.40.50.1580; -; 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 Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1.
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
