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Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Inositol-1-monophosphatase; Short=I-1-Pase; Short=IMPase; Short=Inositol-1-phosphatase; EC=3.1.3.25; |
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| MyHits synonyms | SUHB_ECOLI , P0ADG4 , P22783 , P77511 , Q8X2E6 , 8FEC3508BD111301 |
 Legends: 1, Magnesium 1. {ECO:0000250}; 2, Magnesium 2. {ECO:0000250}; 3, Magnesium 1; via carbonyl oxygen. {ECO:0000250}; 4, BINDING Substrate. {ECO:0000250}; 5, CONFLICT R -> L (in Ref. 1; AAA67506). {ECO:0000305}; 6, REGION Substrate binding. {ECO:0000250}; 7, ipat:IMP_2 [T]; 8, ipat:IMP_1 [T]; 9, HELIX {ECO:0000244|PDB:2QFL}; 10, STRAND {ECO:0000244|PDB:2QFL}; 11, TURN {ECO:0000244|PDB:2QFL}.
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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 15-MAR-2017, entry version 87.
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; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2138605; DOI=10.1128/jb.172.4.2124-2130.1990;
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 277:1453-1462(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; DOI=10.1128/jb.177.1.200-205.1995;
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:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC {ECO:0000305}.
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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_000913.3.
DR RefSeq; WP_000553451.1; NZ_LN832404.1.
DR PDB; 2QFL; X-ray; 1.90 A; A=1-267.
DR PDBsum; 2QFL; -.
DR ProteinModelPortal; P0ADG4; -.
DR SMR; P0ADG4; -.
DR IntAct; P0ADG4; 10.
DR STRING; 511145.b2533; -.
DR SWISS-2DPAGE; P0ADG4; -.
DR EPD; P0ADG4; -.
DR PaxDb; P0ADG4; -.
DR PRIDE; P0ADG4; -.
DR EnsemblBacteria; AAC75586; AAC75586; b2533.
DR EnsemblBacteria; BAA16427; BAA16427; BAA16427.
DR GeneID; 947285; -.
DR KEGG; ecj:JW2517; -.
DR KEGG; eco:b2533; -.
DR PATRIC; 32120463; VBIEscCol129921_2634.
DR EchoBASE; EB0976; -.
DR EcoGene; EG10983; suhB.
DR eggNOG; ENOG4105ECY; Bacteria.
DR eggNOG; COG0483; LUCA.
DR HOGENOM; HOG000282238; -.
DR InParanoid; P0ADG4; -.
DR KO; K01092; -.
DR OMA; IGIFEDG; -.
DR PhylomeDB; P0ADG4; -.
DR BioCyc; EcoCyc:EG10983-MONOMER; -.
DR BioCyc; MetaCyc:EG10983-MONOMER; -.
DR BRENDA; 3.1.3.25; 2026.
DR EvolutionaryTrace; P0ADG4; -.
DR PRO; PR:P0ADG4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047954; F:glycerol-2-phosphatase activity; IDA:EcoCyc.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0031403; F:lithium ion binding; IDA:EcoliWiki.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:EcoliWiki.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
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. {ECO:0000250}.
FT METAL 67 67 Magnesium 1. {ECO:0000250}.
FT METAL 84 84 Magnesium 1. {ECO:0000250}.
FT METAL 84 84 Magnesium 2. {ECO:0000250}.
FT METAL 86 86 Magnesium 1; via carbonyl oxygen.
FT {ECO:0000250}.
FT METAL 87 87 Magnesium 2. {ECO:0000250}.
FT METAL 212 212 Magnesium 2. {ECO:0000250}.
FT BINDING 67 67 Substrate. {ECO:0000250}.
FT BINDING 183 183 Substrate. {ECO:0000250}.
FT BINDING 212 212 Substrate. {ECO:0000250}.
FT CONFLICT 141 141 R -> L (in Ref. 1; AAA67506).
FT {ECO:0000305}.
FT HELIX 2 23 {ECO:0000244|PDB:2QFL}.
FT STRAND 33 35 {ECO:0000244|PDB:2QFL}.
FT HELIX 38 58 {ECO:0000244|PDB:2QFL}.
FT STRAND 62 66 {ECO:0000244|PDB:2QFL}.
FT TURN 67 69 {ECO:0000244|PDB:2QFL}.
FT STRAND 70 72 {ECO:0000244|PDB:2QFL}.
FT STRAND 75 87 {ECO:0000244|PDB:2QFL}.
FT HELIX 89 94 {ECO:0000244|PDB:2QFL}.
FT STRAND 100 107 {ECO:0000244|PDB:2QFL}.
FT STRAND 110 118 {ECO:0000244|PDB:2QFL}.
FT TURN 119 122 {ECO:0000244|PDB:2QFL}.
FT STRAND 123 128 {ECO:0000244|PDB:2QFL}.
FT STRAND 133 135 {ECO:0000244|PDB:2QFL}.
FT STRAND 151 155 {ECO:0000244|PDB:2QFL}.
FT HELIX 162 164 {ECO:0000244|PDB:2QFL}.
FT HELIX 165 176 {ECO:0000244|PDB:2QFL}.
FT TURN 177 179 {ECO:0000244|PDB:2QFL}.
FT STRAND 180 184 {ECO:0000244|PDB:2QFL}.
FT HELIX 188 196 {ECO:0000244|PDB:2QFL}.
FT STRAND 199 207 {ECO:0000244|PDB:2QFL}.
FT HELIX 210 222 {ECO:0000244|PDB:2QFL}.
FT STRAND 226 228 {ECO:0000244|PDB:2QFL}.
FT STRAND 232 234 {ECO:0000244|PDB:2QFL}.
FT HELIX 236 239 {ECO:0000244|PDB:2QFL}.
FT STRAND 242 245 {ECO:0000244|PDB:2QFL}.
FT HELIX 247 255 {ECO:0000244|PDB:2QFL}.
FT TURN 256 259 {ECO:0000244|PDB:2QFL}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 2 259 ipfam:Inositol_P [T]
FT MYHIT 211 225 ipat:IMP_2 [T]
FT MYHIT 81 94 ipat:IMP_1 [T]
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
//
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