Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P37755

- RFBK9_ECOLX

UniProt

P37755 - RFBK9_ECOLX

Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in GDP-mannose biosynthesis which serves as the activated sugar nucleotide precursor for mannose residues in cell surface polysaccharides. This enzyme participates in synthesis of the LPS O9 antigen.

    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 bindingi246 – 2461MagnesiumBy similarity
    Metal bindingi248 – 2481MagnesiumBy similarity
    Metal bindingi250 – 2501MagnesiumBy 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: UniProtKB-UniPathway
    2. O antigen biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Lipopolysaccharide biosynthesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00126; UER00424.
    UPA00281.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphomannomutase (EC:5.4.2.8)
    Short name:
    PMM
    Gene namesi
    Name:manB
    Synonyms:rfbK, rfbK2
    OrganismiEscherichia coli
    Taxonomic identifieri562 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 456456PhosphomannomutasePRO_0000147824Add
    BLAST

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP37755.

    Structurei

    3D structure databases

    ProteinModelPortaliP37755.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the phosphohexose mutase family.Curated

    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.

    P37755-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTQLTCFKAY DIRGELGEEL NEDIAYRIGR AYGEFLKPGK IVVGGDVRLT    50
    SESLKLALAR GLMDAGTDVL DIGLSGTEEI YFATFHLGVD GGIEVTASHN 100
    PMNYNGMKLV RENAKPISGD TGLRDIQRLA EENQFPPVDP ARRGTLRQIS 150
    VLKEYVDHLM GYVDLANFTR PLKLVVNSGN GAAGHVIDEV EKRFAAAGVP 200
    VTFIKVHHQP DGHFPNGIPN PLLPECRQDT ADAVREHQAD MGIAFDGDFD 250
    RCFLFDDEAS FIEGYYIVGL LAEAFLQKQP GAKIIHDPRL TWNTVDIVTR 300
    NGGQPVMSKT GHAFIKERMR QEDAIYGGEM SAHHYFRDFA YCDSGMIPWL 350
    LVAELLCLKN SSLKSLVADR QAAFPASGEI NRKLGNAAEA IARIRAQYEP 400
    AAAHIDTTDG ISIEYPEWRF NLRTSNTEPV VRLNVESRAD TALMNAKTEE 450
    ILALLK 456
    Length:456
    Mass (Da):50,423
    Last modified:October 1, 1994 - v1
    Checksum:i40100B6075791BF3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti392 – 3921A → R.
    Natural varianti441 – 4411T → V.
    Natural varianti446 – 4461A → E.
    Natural varianti449 – 4535EEILA → TELLN.
    Natural varianti456 – 4561K → KEELL.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27646 Genomic DNA. Translation: AAA21138.1.
    L27632 Genomic DNA. Translation: AAA21140.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27646 Genomic DNA. Translation: AAA21138.1 .
    L27632 Genomic DNA. Translation: AAA21140.1 .

    3D structure databases

    ProteinModelPortali P37755.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P37755.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00126 ; UER00424 .
    UPA00281 .

    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. "Cloning and analysis of duplicated rfbM and rfbK genes involved in the formation of GDP-mannose in Escherichia coli O9:K30 and participation of rfb genes in the synthesis of the group I K30 capsular polysaccharide."
      Jayaratne P., Bronner D., Maclachlan R.P., Dodgson C., Kido N., Whitfield C.
      J. Bacteriol. 176:3126-3139(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: O9:K30:H12 / E69.
    2. Cited for: GENE NAME.

    Entry informationi

    Entry nameiRFBK9_ECOLX
    AccessioniPrimary (citable) accession number: P37755
    Secondary accession number(s): P82275
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are two duplicated genes for manB and manC in this E.coli strain.

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3