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P24175

- MANB_ECOLI

UniProt

P24175 - MANB_ECOLI

Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of the capsular polysaccharide colanic acid.

    Catalytic activityi

    Alpha-D-mannose 1-phosphate = D-mannose 6-phosphate.

    Cofactori

    Binds 1 magnesium ion per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei98 – 981Phosphoserine intermediateBy similarity
    Metal bindingi98 – 981Magnesium; via phosphate groupBy similarity
    Metal bindingi245 – 2451MagnesiumBy similarity
    Metal bindingi247 – 2471MagnesiumBy similarity
    Metal bindingi249 – 2491MagnesiumBy similarity

    GO - Molecular functioni

    1. magnesium ion binding Source: InterPro
    2. phosphomannomutase activity Source: UniProtKB-EC

    GO - Biological processi

    1. GDP-mannose biosynthetic process Source: EcoCyc
    2. lipopolysaccharide biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Capsule biogenesis/degradation, Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:PHOSMANMUT-MONOMER.
    ECOL316407:JW2033-MONOMER.
    MetaCyc:PHOSMANMUT-MONOMER.
    UniPathwayiUPA00126; UER00424.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase (EC:5.4.2.8)
    Short name:
    PMM
    Gene namesi
    Name:manB
    Synonyms:cpsG, rfbL
    Ordered Locus Names:b2048, JW2033
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10162. manB.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RefGenome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456PhosphomannomutasePRO_0000147818Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP24175.

    Expressioni

    Gene expression databases

    GenevestigatoriP24175.

    Interactioni

    Protein-protein interaction databases

    IntActiP24175. 9 interactions.
    STRINGi511145.b2048.

    Structurei

    3D structure databases

    ProteinModelPortaliP24175.
    SMRiP24175. Positions 1-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    Phylogenomic databases

    HOGENOMiHOG000268679.
    KOiK01840.
    OMAiVVGCDIR.
    OrthoDBiEOG6W9X55.
    PhylomeDBiP24175.

    Family and domain databases

    Gene3Di3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view]
    PfamiPF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view]
    PRINTSiPR00509. PGMPMM.
    SUPFAMiSSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEiPS00710. PGM_PMM. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P24175-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT    50
    SETLKLALAK GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN 100
    PMDYNGMKLV REGARPISGD TGLRDVQRLA EANDFPPVDE TKRGRYQQIN 150
    LRDAYVDHLF GYINVKNLTP LKLVINSGNG AAGPVVDAIE ARFKALGAPV 200
    ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM GIAFDGDFDR 250
    CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA 300
    GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL 350
    VAELVCLKDK TLGELVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE 400
    ALAVDRTDGI SMTFADWRFN LRTSNTEPVV RLNVESRGDV PLMEARTRTL 450
    LTLLNE 456
    Length:456
    Mass (Da):50,463
    Last modified:March 1, 1992 - v1
    Checksum:i8A96663D7A60BFD1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77127 Genomic DNA. Translation: AAA02894.1.
    U38473 Genomic DNA. Translation: AAC77847.1.
    U00096 Genomic DNA. Translation: AAC75109.1.
    AP009048 Genomic DNA. Translation: BAA15901.1.
    PIRiB55239.
    RefSeqiNP_416552.1. NC_000913.3.
    YP_490290.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75109; AAC75109; b2048.
    BAA15901; BAA15901; BAA15901.
    GeneIDi12934315.
    946574.
    KEGGiecj:Y75_p2011.
    eco:b2048.
    PATRICi32119429. VBIEscCol129921_2125.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77127 Genomic DNA. Translation: AAA02894.1 .
    U38473 Genomic DNA. Translation: AAC77847.1 .
    U00096 Genomic DNA. Translation: AAC75109.1 .
    AP009048 Genomic DNA. Translation: BAA15901.1 .
    PIRi B55239.
    RefSeqi NP_416552.1. NC_000913.3.
    YP_490290.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P24175.
    SMRi P24175. Positions 1-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P24175. 9 interactions.
    STRINGi 511145.b2048.

    Proteomic databases

    PRIDEi P24175.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75109 ; AAC75109 ; b2048 .
    BAA15901 ; BAA15901 ; BAA15901 .
    GeneIDi 12934315.
    946574.
    KEGGi ecj:Y75_p2011.
    eco:b2048.
    PATRICi 32119429. VBIEscCol129921_2125.

    Organism-specific databases

    EchoBASEi EB0160.
    EcoGenei EG10162. manB.

    Phylogenomic databases

    HOGENOMi HOG000268679.
    KOi K01840.
    OMAi VVGCDIR.
    OrthoDBi EOG6W9X55.
    PhylomeDBi P24175.

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00424 .
    BioCyci EcoCyc:PHOSMANMUT-MONOMER.
    ECOL316407:JW2033-MONOMER.
    MetaCyc:PHOSMANMUT-MONOMER.

    Miscellaneous databases

    PROi P24175.

    Gene expression databases

    Genevestigatori P24175.

    Family and domain databases

    Gene3Di 3.30.310.50. 1 hit.
    3.40.120.10. 3 hits.
    InterProi IPR005844. A-D-PHexomutase_a/b/a-I.
    IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
    IPR005845. A-D-PHexomutase_a/b/a-II.
    IPR005846. A-D-PHexomutase_a/b/a-III.
    IPR005843. A-D-PHexomutase_C.
    IPR016066. A-D-PHexomutase_CS.
    IPR005841. Alpha-D-phosphohexomutase_SF.
    [Graphical view ]
    Pfami PF02878. PGM_PMM_I. 1 hit.
    PF02879. PGM_PMM_II. 1 hit.
    PF02880. PGM_PMM_III. 1 hit.
    PF00408. PGM_PMM_IV. 1 hit.
    [Graphical view ]
    PRINTSi PR00509. PGMPMM.
    SUPFAMi SSF53738. SSF53738. 3 hits.
    SSF55957. SSF55957. 1 hit.
    PROSITEi PS00710. PGM_PMM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of the phosphoglucomutase gene in E. coli."
      Tal R., Eichinger G., Emerick A., Wong H.C.
      Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Evidence for effect of random genetic drift on G+C content after lateral transfer of fucose pathway genes to Escherichia coli K-12."
      Aoyama K., Haase A.M., Reeves P.R.
      Mol. Biol. Evol. 11:829-838(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Organization of the Escherichia coli K-12 gene cluster responsible for production of the extracellular polysaccharide colanic acid."
      Stevenson G., Andrianopoulos K., Hobbs M., Reeves P.R.
      J. Bacteriol. 178:4885-4893(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    6. "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.

    Entry informationi

    Entry nameiMANB_ECOLI
    AccessioniPrimary (citable) accession number: P24175
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3