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Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Involved in the biosynthesis of the capsular polysaccharide colanic acid.

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ 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: UniProtKB-UniPathway
  2. lipopolysaccharide biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10162. manB.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: GO_Central
Complete GO annotation...

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.
InParanoidiP24175.
KOiK01840.
OMAiSIEYPNW.
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

        10         20         30         40         50
MKKLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT
60 70 80 90 100
SETLKLALAK GLQDAGVDVL DIGMSGTEEI YFATFHLGVD GGIEVTASHN
110 120 130 140 150
PMDYNGMKLV REGARPISGD TGLRDVQRLA EANDFPPVDE TKRGRYQQIN
160 170 180 190 200
LRDAYVDHLF GYINVKNLTP LKLVINSGNG AAGPVVDAIE ARFKALGAPV
210 220 230 240 250
ELIKVHNTPD GNFPNGIPNP LLPECRDDTR NAVIKHGADM GIAFDGDFDR
260 270 280 290 300
CFLFDEKGQF IEGYYIVGLL AEAFLEKNPG AKIIHDPRLS WNTVDVVTAA
310 320 330 340 350
GGTPVMSKTG HAFIKERMRK EDAIYGGEMS AHHYFRDFAY CDSGMIPWLL
360 370 380 390 400
VAELVCLKDK TLGELVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE
410 420 430 440 450
ALAVDRTDGI SMTFADWRFN LRTSNTEPVV RLNVESRGDV PLMEARTRTL

LTLLNE
Length:456
Mass (Da):50,463
Last modified:February 29, 1992 - v1
Checksum:i8A96663D7A60BFD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP24175. 9 interactions.
STRINGi511145.b2048.

Proteomic databases

PRIDEiP24175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0160.
EcoGeneiEG10162. manB.

Phylogenomic databases

HOGENOMiHOG000268679.
InParanoidiP24175.
KOiK01840.
OMAiSIEYPNW.
OrthoDBiEOG6W9X55.
PhylomeDBiP24175.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP24175.

Gene expression databases

GenevestigatoriP24175.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of the phosphoglucomutase gene in E. coli."
    Tal R., Eichinger G., Emerick A., Wong H.C.
    Submitted (AUG-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(1993) [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(1995) [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(2005) [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: February 29, 1992
Last sequence update: February 29, 1992
Last modified: March 31, 2015
This is version 128 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

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 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.