RNH_ECOLI
ID RNH_ECOLI Reviewed; 155 AA.
AC P0A7Y4; P00647; Q8FKY5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Ribonuclease HI;
DE Short=RNase HI;
DE EC=3.1.26.4;
DE AltName: Full=Ribonuclease H;
DE Short=RNase H;
GN Name=rnhA; Synonyms=dasF, herA, rnh, sdrA; OrderedLocusNames=b0214, JW0204;
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=6296074; DOI=10.1016/s0021-9258(18)33189-2;
RA Kanaya S., Crouch R.J.;
RT "DNA sequence of the gene coding for Escherichia coli ribonuclease H.";
RL J. Biol. Chem. 258:1276-1281(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FB2;
RX PubMed=6316347; DOI=10.1073/pnas.80.23.7137;
RA Maki H., Horiuchi T., Sekiguchi M.;
RT "Structure and expression of the dnaQ mutator and the RNase H genes of
RT Escherichia coli: overlap of the promoter regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:7137-7141(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6302075; DOI=10.1128/jb.154.2.1021-1026.1983;
RA Kanaya S., Crouch R.J.;
RT "Low levels of RNase H activity in Escherichia coli FB2 rnh result from a
RT single-base change in the structural gene of RNase H.";
RL J. Bacteriol. 154:1021-1026(1983).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023634; DOI=10.1016/0022-2836(86)90080-x;
RA Cox E.C., Horner D.L.;
RT "DNA sequence and coding properties of mutD(dnaQ) a dominant Escherichia
RT coli mutator gene.";
RL J. Mol. Biol. 190:113-117(1986).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
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 [8]
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 [9]
RP PARTIAL PROTEIN SEQUENCE, AND MUTAGENESIS OF CYSTEINE RESIDUES.
RX PubMed=2171503; DOI=10.1042/bj2710059;
RA Kanaya S., Kimura S., Katsuda C., Ikehara M.;
RT "Role of cysteine residues in ribonuclease H from Escherichia coli. Site-
RT directed mutagenesis and chemical modification.";
RL Biochem. J. 271:59-66(1990).
RN [10]
RP MUTAGENESIS OF ASP-10; GLU-48; ASP-70; HIS-124; ASN-130 AND ASP-134.
RX PubMed=1689729; DOI=10.1016/s0021-9258(19)39607-3;
RA Kanaya S., Kohara A., Miura Y., Sekiguchi A., Iwai S., Inoue H.,
RA Ohtsuka E., Ikehara M.;
RT "Identification of the amino acid residues involved in an active site of
RT Escherichia coli ribonuclease H by site-directed mutagenesis.";
RL J. Biol. Chem. 265:4615-4621(1990).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222;
RX PubMed=7568472; DOI=10.1006/plas.1995.1026;
RA Lima T.M., Lim D.;
RT "Isolation and characterization of host mutants defective in msDNA
RT synthesis: role of ribonuclease H in msDNA synthesis.";
RL Plasmid 33:235-238(1995).
RN [12]
RP COFACTOR, AND MUTAGENESIS OF HIS-124 AND ASP-134.
RX PubMed=9852071; DOI=10.1074/jbc.273.51.34128;
RA Keck J.L., Goedken E.R., Marqusee S.;
RT "Activation/attenuation model for RNase H. A one-metal mechanism with
RT second-metal inhibition.";
RL J. Biol. Chem. 273:34128-34133(1998).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=1698262; DOI=10.1038/347306a0;
RA Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S.,
RA Ikehara M., Matsuzaki T., Morikawa K.;
RT "Three-dimensional structure of ribonuclease H from E. coli.";
RL Nature 347:306-309(1990).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND SUBUNIT.
RX PubMed=2169648; DOI=10.1126/science.2169648;
RA Yang W., Hendrickson W.A., Crouch R.J., Satow Y.;
RT "Structure of ribonuclease H phased at 2-A resolution by MAD analysis of
RT the selenomethionyl protein.";
RL Science 249:1398-1405(1990).
RN [15]
RP STRUCTURE BY NMR.
RX PubMed=1646006; DOI=10.1021/bi00238a030;
RA Yamazaki T., Yoshida M., Kanaya S., Nakamura H., Nagayama K.;
RT "Assignments of backbone 1H, 13C, and 15N resonances and secondary
RT structure of ribonuclease H from Escherichia coli by heteronuclear three-
RT dimensional NMR spectroscopy.";
RL Biochemistry 30:6036-6047(1991).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH MAGNESIUM.
RX PubMed=1311386; DOI=10.1016/0022-2836(92)90260-q;
RA Katayanagi K., Miyagawa M., Matsushima M., Ishikawa M., Kanaya S.,
RA Nakamura H., Ikehara M., Matsuzaki T., Morikawa K.;
RT "Structural details of ribonuclease H from Escherichia coli as refined to
RT an atomic resolution.";
RL J. Mol. Biol. 223:1029-1052(1992).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF MUTANTS.
RX PubMed=8381958; DOI=10.1093/protein/6.1.85;
RA Ishikawa K., Kimura S., Kanaya S., Morikawa K., Nakamura H.;
RT "Structural study of mutants of Escherichia coli ribonuclease HI with
RT enhanced thermostability.";
RL Protein Eng. 6:85-91(1993).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANTS ASN-10; GLN-48 AND ASN-70.
RX PubMed=8408067; DOI=10.1016/s0021-9258(20)80652-8;
RA Katayanagi K., Ishikawa K., Okumura M., Ariyoshi M., Kanaya S., Kawano Y.,
RA Suzuki M., Tanaka I., Morikawa K.;
RT "Crystal structures of ribonuclease HI active site mutants from Escherichia
RT coli.";
RL J. Biol. Chem. 268:22092-22099(1993).
RN [19]
RP STRUCTURE BY NMR.
RX PubMed=8527428; DOI=10.1021/bi00051a003;
RA Yamazaki T., Ogasahara K., Yutani K., Oobatake M., Kanaya S.;
RT "Folding pathway of Escherichia coli ribonuclease HI: a circular dichroism,
RT fluorescence, and NMR study.";
RL Biochemistry 34:16552-16562(1995).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF HIS-124 AND
RP ASP-134.
RX PubMed=8931125; DOI=10.1093/protein/9.10.857;
RA Kashiwagi T., Jeanteur D., Haruki M., Katayanagi K., Kanaya S.,
RA Morikawa K.;
RT "Proposal for new catalytic roles for two invariant residues in Escherichia
RT coli ribonuclease HI.";
RL Protein Eng. 9:857-867(1996).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS).
RX PubMed=11106164; DOI=10.1110/ps.9.10.1914;
RA Goedken E.R., Keck J.L., Berger J.M., Marqusee S.;
RT "Divalent metal cofactor binding in the kinetic folding trajectory of
RT Escherichia coli ribonuclease HI.";
RL Protein Sci. 9:1914-1921(2000).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS.
RX PubMed=11083878; DOI=10.1074/jbc.m009626200;
RA Goedken E.R., Marqusee S.;
RT "Co-crystal of Escherichia coli RNase HI with Mn2+ ions reveals two
RT divalent metals bound in the active site.";
RL J. Biol. Chem. 276:7266-7271(2001).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANTS ALA-48 AND ASN-134 IN
RP COMPLEX WITH MANGANESE IONS.
RX PubMed=15644213; DOI=10.1016/j.jmb.2004.11.007;
RA Tsunaka Y., Takano K., Matsumura H., Yamagata Y., Kanaya S.;
RT "Identification of single Mn(2+) binding sites required for activation of
RT the mutant proteins of E.coli RNase HI at Glu48 and/or Asp134 by X-ray
RT crystallography.";
RL J. Mol. Biol. 345:1171-1183(2005).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. RNase H participates in DNA replication; it helps to specify
CC the origin of genomic replication by suppressing initiation at origins
CC other than the oriC locus; along with the 5'-3' exonuclease of pol1, it
CC removes RNA primers from the Okazaki fragments of lagging strand
CC synthesis; and it defines the origin of replication for ColE1-type
CC plasmids by specific cleavage of an RNA preprimer. Involved in
CC production of retron derived msDNA (a branched RNA linked by a 2',5'-
CC phosphodiester bond to a single-stranded DNA). Strain K12 / MG1655 does
CC not have retrons, however they can be expressed in this strain which
CC requires this enzyme (tested with retron Ec86) (PubMed:7568472).
CC {ECO:0000269|PubMed:7568472}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:9852071};
CC Note=Binds 1 Mg(2+) ion per subunit in the absence of substrate.
CC Requires millimolar levels of Mg(2+) for maximal activity. Has low
CC activity at micromolar concentrations of Mn(2+) and is inhibited at
CC higher Mn(2+) levels. Can bind a second metal ion at a regulatory site,
CC or after substrate binding. {ECO:0000269|PubMed:9852071};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11083878,
CC ECO:0000269|PubMed:1311386, ECO:0000269|PubMed:15644213,
CC ECO:0000269|PubMed:2169648}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: In a strain that encodes a retron, the msDNA is
CC abnormally sized. {ECO:0000269|PubMed:7568472}.
CC -!- SIMILARITY: Belongs to the RNase H family. {ECO:0000305}.
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DR EMBL; K00985; AAA24565.1; -; Genomic_DNA.
DR EMBL; V00337; CAA23620.1; -; Genomic_DNA.
DR EMBL; X04027; CAA27660.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08636.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73319.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77885.1; -; Genomic_DNA.
DR PIR; A92401; NRECH.
DR RefSeq; NP_414750.1; NC_000913.3.
DR RefSeq; WP_000917883.1; NZ_STEB01000020.1.
DR PDB; 1F21; X-ray; 1.40 A; A=1-155.
DR PDB; 1G15; X-ray; 1.90 A; A=1-155.
DR PDB; 1GOA; X-ray; 1.90 A; A=1-155.
DR PDB; 1GOB; X-ray; 2.00 A; A=1-155.
DR PDB; 1GOC; X-ray; 2.00 A; A=1-155.
DR PDB; 1JL1; X-ray; 1.30 A; A=1-155.
DR PDB; 1JL2; X-ray; 1.76 A; A/B/C/D=1-49, A/B/C/D=121-155.
DR PDB; 1JXB; X-ray; 1.60 A; A=1-155.
DR PDB; 1KVA; X-ray; 1.80 A; A=1-155.
DR PDB; 1KVB; X-ray; 1.90 A; A=1-155.
DR PDB; 1KVC; X-ray; 1.90 A; A=1-155.
DR PDB; 1LAV; X-ray; 1.80 A; A=1-155.
DR PDB; 1LAW; X-ray; 1.80 A; A=1-155.
DR PDB; 1RBR; X-ray; 1.80 A; A=1-155.
DR PDB; 1RBS; X-ray; 1.80 A; A=1-155.
DR PDB; 1RBT; X-ray; 1.80 A; A=1-155.
DR PDB; 1RBU; X-ray; 1.80 A; A=1-155.
DR PDB; 1RBV; X-ray; 1.80 A; A=1-155.
DR PDB; 1RCH; NMR; -; A=1-155.
DR PDB; 1RDA; X-ray; 2.15 A; A=1-155.
DR PDB; 1RDB; X-ray; 1.90 A; A=1-155.
DR PDB; 1RDC; X-ray; 2.30 A; A=1-155.
DR PDB; 1RDD; X-ray; 2.80 A; A=1-155.
DR PDB; 1RNH; X-ray; 2.00 A; A=1-155.
DR PDB; 1WSE; X-ray; 2.30 A; A/B=1-155.
DR PDB; 1WSF; X-ray; 2.30 A; A/B/C/D=1-155.
DR PDB; 1WSG; X-ray; 2.20 A; A/B/C/D=1-155.
DR PDB; 1WSH; X-ray; 1.90 A; A/B/C/D=1-155.
DR PDB; 1WSI; X-ray; 2.00 A; A/B/C/D=1-155.
DR PDB; 1WSJ; X-ray; 2.00 A; A/B/C/D/E/F/G/H=1-155.
DR PDB; 2RN2; X-ray; 1.48 A; A=1-155.
DR PDB; 2YV0; X-ray; 1.40 A; X=1-155.
DR PDB; 2Z1G; X-ray; 2.10 A; A=1-155.
DR PDB; 2Z1H; X-ray; 2.60 A; A=1-155.
DR PDB; 2Z1I; X-ray; 2.00 A; A/B=1-155.
DR PDB; 2Z1J; X-ray; 2.38 A; A=1-155.
DR PDB; 3AA2; X-ray; 1.90 A; A=1-155.
DR PDB; 3AA3; X-ray; 2.20 A; A=1-155.
DR PDB; 3AA4; X-ray; 1.79 A; A=1-155.
DR PDB; 3AA5; X-ray; 2.10 A; X=1-155.
DR PDB; 3HYF; X-ray; 1.70 A; A=79-102.
DR PDB; 3QIN; X-ray; 1.70 A; A=79-102.
DR PDB; 3QIO; X-ray; 1.40 A; A=79-102.
DR PDB; 4Z0U; X-ray; 2.00 A; A/B=1-155.
DR PDB; 7VSA; X-ray; 1.76 A; A/B=1-155.
DR PDB; 7VSB; X-ray; 1.84 A; A/B=1-155.
DR PDB; 7VSC; X-ray; 1.83 A; A=1-155.
DR PDB; 7VSD; X-ray; 1.70 A; A/B=1-155.
DR PDB; 7VSE; X-ray; 2.08 A; A/B=1-155.
DR PDBsum; 1F21; -.
DR PDBsum; 1G15; -.
DR PDBsum; 1GOA; -.
DR PDBsum; 1GOB; -.
DR PDBsum; 1GOC; -.
DR PDBsum; 1JL1; -.
DR PDBsum; 1JL2; -.
DR PDBsum; 1JXB; -.
DR PDBsum; 1KVA; -.
DR PDBsum; 1KVB; -.
DR PDBsum; 1KVC; -.
DR PDBsum; 1LAV; -.
DR PDBsum; 1LAW; -.
DR PDBsum; 1RBR; -.
DR PDBsum; 1RBS; -.
DR PDBsum; 1RBT; -.
DR PDBsum; 1RBU; -.
DR PDBsum; 1RBV; -.
DR PDBsum; 1RCH; -.
DR PDBsum; 1RDA; -.
DR PDBsum; 1RDB; -.
DR PDBsum; 1RDC; -.
DR PDBsum; 1RDD; -.
DR PDBsum; 1RNH; -.
DR PDBsum; 1WSE; -.
DR PDBsum; 1WSF; -.
DR PDBsum; 1WSG; -.
DR PDBsum; 1WSH; -.
DR PDBsum; 1WSI; -.
DR PDBsum; 1WSJ; -.
DR PDBsum; 2RN2; -.
DR PDBsum; 2YV0; -.
DR PDBsum; 2Z1G; -.
DR PDBsum; 2Z1H; -.
DR PDBsum; 2Z1I; -.
DR PDBsum; 2Z1J; -.
DR PDBsum; 3AA2; -.
DR PDBsum; 3AA3; -.
DR PDBsum; 3AA4; -.
DR PDBsum; 3AA5; -.
DR PDBsum; 3HYF; -.
DR PDBsum; 3QIN; -.
DR PDBsum; 3QIO; -.
DR PDBsum; 4Z0U; -.
DR PDBsum; 7VSA; -.
DR PDBsum; 7VSB; -.
DR PDBsum; 7VSC; -.
DR PDBsum; 7VSD; -.
DR PDBsum; 7VSE; -.
DR AlphaFoldDB; P0A7Y4; -.
DR SMR; P0A7Y4; -.
DR BioGRID; 4263455; 263.
DR DIP; DIP-47864N; -.
DR IntAct; P0A7Y4; 22.
DR STRING; 511145.b0214; -.
DR BindingDB; P0A7Y4; -.
DR ChEMBL; CHEMBL1770039; -.
DR jPOST; P0A7Y4; -.
DR PaxDb; P0A7Y4; -.
DR PRIDE; P0A7Y4; -.
DR EnsemblBacteria; AAC73319; AAC73319; b0214.
DR EnsemblBacteria; BAA77885; BAA77885; BAA77885.
DR GeneID; 66671496; -.
DR GeneID; 946955; -.
DR KEGG; ecj:JW0204; -.
DR KEGG; eco:b0214; -.
DR PATRIC; fig|1411691.4.peg.2070; -.
DR EchoBASE; EB0853; -.
DR eggNOG; COG0328; Bacteria.
DR HOGENOM; CLU_030894_6_0_6; -.
DR InParanoid; P0A7Y4; -.
DR OMA; MQEIEIF; -.
DR PhylomeDB; P0A7Y4; -.
DR BioCyc; EcoCyc:EG10860-MON; -.
DR BioCyc; MetaCyc:EG10860-MON; -.
DR BRENDA; 3.1.13.2; 2026.
DR BRENDA; 3.1.26.4; 2026.
DR EvolutionaryTrace; P0A7Y4; -.
DR PRO; PR:P0A7Y4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003676; F:nucleic acid binding; IDA:EcoliWiki.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IDA:EcoCyc.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IMP:EcoCyc.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GO_Central.
DR CDD; cd09278; RNase_HI_prokaryote_like; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_00042; RNase_H; 1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR022892; RNaseHI.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Endonuclease;
KW Hydrolase; Magnesium; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..155
FT /note="Ribonuclease HI"
FT /id="PRO_0000195372"
FT DOMAIN 1..142
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1311386"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1311386"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1311386"
FT BINDING 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:1311386"
FT BINDING 134
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:1311386"
FT MUTAGEN 10
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1689729"
FT MUTAGEN 48
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1689729"
FT MUTAGEN 70
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1689729"
FT MUTAGEN 124
FT /note="H->A: Reduces activity."
FT /evidence="ECO:0000269|PubMed:1689729,
FT ECO:0000269|PubMed:8931125, ECO:0000269|PubMed:9852071"
FT MUTAGEN 130
FT /note="N->A: Reduces activity."
FT /evidence="ECO:0000269|PubMed:1689729"
FT MUTAGEN 134
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:1689729,
FT ECO:0000269|PubMed:8931125, ECO:0000269|PubMed:9852071"
FT MUTAGEN 134
FT /note="D->H,N: Slight decrease of activity."
FT /evidence="ECO:0000269|PubMed:1689729,
FT ECO:0000269|PubMed:8931125, ECO:0000269|PubMed:9852071"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1RDD"
FT STRAND 5..15
FT /evidence="ECO:0007829|PDB:1JL1"
FT STRAND 18..28
FT /evidence="ECO:0007829|PDB:1JL1"
FT STRAND 31..42
FT /evidence="ECO:0007829|PDB:1JL1"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:1JL1"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1JL1"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:1JL1"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:1JL1"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:1JL1"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:2YV0"
FT HELIX 101..110
FT /evidence="ECO:0007829|PDB:1JL1"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1JL1"
FT STRAND 115..120
FT /evidence="ECO:0007829|PDB:1JL1"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:1LAV"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:1JL1"
SQ SEQUENCE 155 AA; 17597 MW; B8EF81EEB2F94CBE CRC64;
MLKQVEIFTD GSCLGNPGPG GYGAILRYRG REKTFSAGYT RTTNNRMELM AAIVALEALK
EHCEVILSTD SQYVRQGITQ WIHNWKKRGW KTADKKPVKN VDLWQRLDAA LGQHQIKWEW
VKGHAGHPEN ERCDELARAA AMNPTLEDTG YQVEV
