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Protein

HMP-PP phosphatase

Gene

cof

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P). Can also hydrolyze other substrates such as MeO-HMP-PP and 4-amino-2-trifluoromethyl 5-hydroxymethylpyrimidine pyrophosphate (CF3-HMP-PP) to give MeO-HMP-P and 4-amino-2-trifluoromethyl-5-hydroxymethylpyrimidine phosphate. This hydrolysis generates resistance to the antibiotics (bacimethrin, CF3-HMP) by reducing the formation of their toxic forms, 2'-methoxythiamin pyrophosphate (MeO-TPP) and CF3-HMP-PP. Also hydrolyzes pyridoxal-phosphate (PLP) and flavin mononucleotide (FMN), and purines (GMP and IMP) as secondary substrates.UniRule annotation2 Publications

Cofactori

Mg2+UniRule annotation1 Publication, Mn2+UniRule annotation1 Publication, Co2+UniRule annotation1 Publication, Zn2+UniRule annotation1 PublicationNote: Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.UniRule annotation1 Publication

Kineticsi

  1. KM=0.68 mM for PLP (with magnesium ions as cofactor and at pH 9)1 Publication
  2. KM=2.5 mM for 2-deoxyglucose-6-P (with magnesium ions as cofactor and at pH 9)1 Publication

    pH dependencei

    Optimum pH is between 6 and 7.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei8 – 81NucleophileUniRule annotation
    Metal bindingi8 – 81MagnesiumUniRule annotation
    Metal bindingi10 – 101Magnesium; via carbonyl oxygenUniRule annotation
    Metal bindingi212 – 2121MagnesiumUniRule annotation

    GO - Molecular functioni

    • magnesium ion binding Source: UniProtKB
    • nucleoside-diphosphatase activity Source: EcoliWiki
    • phosphatase activity Source: UniProtKB

    GO - Biological processi

    • antibiotic catabolic process Source: UniProtKB
    • thiamine biosynthetic process Source: EcoliWiki
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G6246-MONOMER.
    ECOL316407:JW0436-MONOMER.
    MetaCyc:G6246-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    HMP-PP phosphataseUniRule annotation (EC:3.6.1.-UniRule annotation)
    Gene namesi
    Name:cofUniRule annotation
    Ordered Locus Names:b0446, JW0436
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13216. cof.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 272272HMP-PP phosphatasePRO_0000054418Add
    BLAST

    Proteomic databases

    PaxDbiP46891.

    Interactioni

    Protein-protein interaction databases

    BioGridi4260651. 7 interactions.
    IntActiP46891. 1 interaction.
    STRINGi511145.b0446.

    Structurei

    3D structure databases

    ProteinModelPortaliP46891.
    SMRiP46891. Positions 1-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAD-like hydrolase superfamily. Cof family.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4108AZI. Bacteria.
    COG0561. LUCA.
    HOGENOMiHOG000184784.
    InParanoidiP46891.
    KOiK11938.
    OMAiKRIPAHQ.
    OrthoDBiEOG6K13W0.
    PhylomeDBiP46891.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    HAMAPiMF_01847. HMP_PP_phosphat.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR023938. HMP-PP_phosphatase.
    IPR000150. Hypothet_cof.
    [Graphical view]
    PfamiPF08282. Hydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR00099. Cof-subfamily. 1 hit.
    TIGR01484. HAD-SF-IIB. 1 hit.
    PROSITEiPS01228. COF_1. 1 hit.
    PS01229. COF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46891-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MARLAAFDMD GTLLMPDHHL GEKTLSTLAR LRERDITLTF ATGRHALEMQ
    60 70 80 90 100
    HILGALSLDA YLITGNGTRV HSLEGELLHR DDLPADVAEL VLYQQWDTRA
    110 120 130 140 150
    SMHIFNDDGW FTGKEIPALL QAFVYSGFRY QIIDVKKMPL GSVTKICFCG
    160 170 180 190 200
    DHDDLTRLQI QLYEALGERA HLCFSATDCL EVLPVGCNKG AALTVLTQHL
    210 220 230 240 250
    GLSLRDCMAF GDAMNDREML VSVGSGFIMG NAMPQLRAEL PHLPVIGHCR
    260 270
    NQAVSHYLTH WLDYPHLPYS PE
    Length:272
    Mass (Da):30,371
    Last modified:October 1, 1996 - v2
    Checksum:iD8FC034BF81E41AC
    GO

    Sequence cautioni

    The sequence AAB40202.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence CAA91181.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti173 – 1731C → S in BAA11650 (Ref. 2) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z54355 Genomic DNA. Translation: CAA91181.1. Different initiation.
    D82943 Genomic DNA. Translation: BAA11650.1.
    U82664 Genomic DNA. Translation: AAB40202.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73549.2.
    AP009048 Genomic DNA. Translation: BAE76226.1.
    PIRiF64774.
    RefSeqiNP_414980.2. NC_000913.3.
    WP_001336137.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73549; AAC73549; b0446.
    BAE76226; BAE76226; BAE76226.
    GeneIDi945089.
    KEGGiecj:JW0436.
    eco:b0446.
    PATRICi32116045. VBIEscCol129921_0464.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z54355 Genomic DNA. Translation: CAA91181.1. Different initiation.
    D82943 Genomic DNA. Translation: BAA11650.1.
    U82664 Genomic DNA. Translation: AAB40202.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC73549.2.
    AP009048 Genomic DNA. Translation: BAE76226.1.
    PIRiF64774.
    RefSeqiNP_414980.2. NC_000913.3.
    WP_001336137.1. NZ_LN832404.1.

    3D structure databases

    ProteinModelPortaliP46891.
    SMRiP46891. Positions 1-258.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4260651. 7 interactions.
    IntActiP46891. 1 interaction.
    STRINGi511145.b0446.

    Proteomic databases

    PaxDbiP46891.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73549; AAC73549; b0446.
    BAE76226; BAE76226; BAE76226.
    GeneIDi945089.
    KEGGiecj:JW0436.
    eco:b0446.
    PATRICi32116045. VBIEscCol129921_0464.

    Organism-specific databases

    EchoBASEiEB3007.
    EcoGeneiEG13216. cof.

    Phylogenomic databases

    eggNOGiENOG4108AZI. Bacteria.
    COG0561. LUCA.
    HOGENOMiHOG000184784.
    InParanoidiP46891.
    KOiK11938.
    OMAiKRIPAHQ.
    OrthoDBiEOG6K13W0.
    PhylomeDBiP46891.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6246-MONOMER.
    ECOL316407:JW0436-MONOMER.
    MetaCyc:G6246-MONOMER.

    Miscellaneous databases

    PROiP46891.

    Family and domain databases

    Gene3Di3.40.50.1000. 2 hits.
    HAMAPiMF_01847. HMP_PP_phosphat.
    InterProiIPR023214. HAD-like_dom.
    IPR006379. HAD-SF_hydro_IIB.
    IPR023938. HMP-PP_phosphatase.
    IPR000150. Hypothet_cof.
    [Graphical view]
    PfamiPF08282. Hydrolase_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR00099. Cof-subfamily. 1 hit.
    TIGR01484. HAD-SF-IIB. 1 hit.
    PROSITEiPS01228. COF_1. 1 hit.
    PS01229. COF_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Patzer S.I., Hantke K.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    2. "Nucleotide sequence analysis of the E. coli chromosome around the 10.0 min region."
      Hatada E., Ohmori H., Qiao Y., Tsuji M., Fukuda R.
      Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "A genetic screen for the identification of thiamin metabolic genes."
      Lawhorn B.G., Gerdes S.Y., Begley T.P.
      J. Biol. Chem. 279:43555-43559(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PYROPHOSPHATASE AND IN THE ANTIBIOTIC RESISTANCE.
      Strain: K12 / MG1655 / ATCC 47076.
    7. "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family."
      Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V., Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V., Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.
      J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.

    Entry informationi

    Entry nameiCOF_ECOLI
    AccessioniPrimary (citable) accession number: P46891
    Secondary accession number(s): P71208, P77198, Q2MBY0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 1, 1996
    Last modified: July 6, 2016
    This is version 116 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.