ID SUHB_ECOLI Reviewed; 267 AA.
AC P0ADG4; P22783; P77511; Q8X2E6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 64.
DE RecName: Full=Inositol-1-monophosphatase;
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25;
GN Name=suhB; Synonyms=ssyA; OrderedLocusNames=b2533, JW2517;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2138605;
RA Yano R., Nagai H., Shiba K., Yura T.;
RT "A mutation that enhances synthesis of sigma 32 and suppresses
RT temperature-sensitive growth of the rpoH15 mutant of Escherichia
RT coli.";
RL J. Bacteriol. 172:2124-2130(1990).
RN [2]
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.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(1997).
RN [4]
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
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=8002619;
RA Matsuhisa A., Suzuki N., Noda T., Shiba K.;
RT "Inositol monophosphatase activity from the Escherichia coli suhB gene
RT product.";
RL J. Bacteriol. 177:200-205(1995).
RN [6]
RP CHARACTERIZATION.
RX PubMed=10747806; DOI=10.1021/bi992424f;
RA Chen L., Roberts M.F.;
RT "Overexpression, purification, and analysis of complementation
RT behavior of E. coli SuhB protein: comparison with bacterial and
RT archaeal inositol monophosphatases.";
RL Biochemistry 39:4145-4153(2000).
CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR EMBL; M34828; AAA67506.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75586.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16427.1; -; Genomic_DNA.
DR PIR; D65030; D65030.
DR RefSeq; NP_417028.1; NC_000913.2.
DR RefSeq; YP_490761.1; NC_007779.1.
DR PDB; 2QFL; X-ray; 1.90 A; A=1-267.
DR PDBsum; 2QFL; -.
DR ProteinModelPortal; P0ADG4; -.
DR SMR; P0ADG4; 1-262.
DR IntAct; P0ADG4; 5.
DR STRING; 511145.b2533; -.
DR SWISS-2DPAGE; P0ADG4; -.
DR PaxDb; P0ADG4; -.
DR PRIDE; P0ADG4; -.
DR EnsemblBacteria; AAC75586; AAC75586; b2533.
DR EnsemblBacteria; BAA16427; BAA16427; BAA16427.
DR GeneID; 12931606; -.
DR GeneID; 947285; -.
DR KEGG; ecj:Y75_p2486; -.
DR KEGG; eco:b2533; -.
DR PATRIC; 32120463; VBIEscCol129921_2634.
DR EchoBASE; EB0976; -.
DR EcoGene; EG10983; suhB.
DR eggNOG; COG0483; -.
DR HOGENOM; HOG000282238; -.
DR KO; K01092; -.
DR OMA; KGINDYV; -.
DR ProtClustDB; PRK10757; -.
DR BioCyc; EcoCyc:EG10983-MONOMER; -.
DR BioCyc; ECOL316407:JW2517-MONOMER; -.
DR BioCyc; MetaCyc:EG10983-MONOMER; -.
DR EvolutionaryTrace; P0ADG4; -.
DR Genevestigator; P0ADG4; -.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0047954; F:glycerol-2-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:EC.
DR GO; GO:0031403; F:lithium ion binding; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:EcoliWiki.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR InterPro; IPR022337; Inositol_monophosphatase_SuhB.
DR PANTHER; PTHR20854; PTHR20854; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR01959; SBIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1 267 Inositol-1-monophosphatase.
FT /FTId=PRO_0000142559.
FT REGION 86 89 Substrate binding (By similarity).
FT METAL 67 67 Magnesium 1 (By similarity).
FT METAL 84 84 Magnesium 1 (By similarity).
FT METAL 84 84 Magnesium 2 (By similarity).
FT METAL 86 86 Magnesium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 87 87 Magnesium 2 (By similarity).
FT METAL 212 212 Magnesium 2 (By similarity).
FT BINDING 67 67 Substrate (By similarity).
FT BINDING 183 183 Substrate (By similarity).
FT BINDING 212 212 Substrate (By similarity).
FT CONFLICT 141 141 R -> L (in Ref. 1; AAA67506).
FT HELIX 2 23
FT STRAND 33 35
FT HELIX 38 58
FT STRAND 62 66
FT TURN 67 69
FT STRAND 70 72
FT STRAND 75 87
FT HELIX 89 94
FT STRAND 100 107
FT STRAND 110 118
FT TURN 119 122
FT STRAND 123 128
FT STRAND 133 135
FT STRAND 151 155
FT HELIX 162 164
FT HELIX 165 176
FT TURN 177 179
FT STRAND 180 184
FT HELIX 188 196
FT STRAND 199 207
FT HELIX 210 222
FT STRAND 226 228
FT STRAND 232 234
FT HELIX 236 239
FT STRAND 242 245
FT HELIX 247 255
FT TURN 256 259
SQ SEQUENCE 267 AA; 29172 MW; 8FEC3508BD111301 CRC64;
MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP
QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM
RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IVGKLFNECA
DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG
NIVAGNPRVV KAMLANMRDE LSDALKR
//
