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P37755

- RFBK9_ECOLX

UniProt

P37755 - RFBK9_ECOLX

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Protein

Phosphomannomutase

Gene
manB, rfbK, rfbK2
Organism
Escherichia coli
Status
Reviewed - Annotation score: 4 out of 5 - Protein inferred from homologyi

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 intermediate By similarity
Metal bindingi98 – 981Magnesium; via phosphate group By similarity
Metal bindingi246 – 2461Magnesium By similarity
Metal bindingi248 – 2481Magnesium By similarity
Metal bindingi250 – 2501Magnesium By 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
Complete GO annotation...

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.

Family & Domainsi

Sequence similaritiesi

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: April 16, 2014
This is version 72 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

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