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Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 3 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 O7 antigen.

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: GDP-alpha-D-mannose biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphomannomutase (manB), Phosphomannomutase (manB)
This subpathway is part of the pathway GDP-alpha-D-mannose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes alpha-D-mannose 1-phosphate from D-fructose 6-phosphate, the pathway GDP-alpha-D-mannose biosynthesis and in Nucleotide-sugar biosynthesis.

Pathwayi: LPS O-antigen biosynthesis

This protein is involved in the pathway LPS O-antigen biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS O-antigen biosynthesis and in Bacterial outer membrane biogenesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei96Phosphoserine intermediateBy similarity1
Metal bindingi96Magnesium; via phosphate groupBy similarity1
Metal bindingi243MagnesiumBy similarity1
Metal bindingi245MagnesiumBy similarity1
Metal bindingi247MagnesiumBy similarity1

GO - Molecular functioni

GO - Biological processi

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
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001478231 – 453PhosphomannomutaseAdd BLAST453

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP37742.

Structurei

3D structure databases

ProteinModelPortaliP37742.
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.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P37742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLTCFKAYDI RGKLGEELNE DIAWRIGRAY GEFLKPKTIV LGGDVRLTSE
60 70 80 90 100
TLKLALAKGL QDAGVDVLDI GMSGTEEIYF ATFHLGVDGG IEVTASHNPM
110 120 130 140 150
DYNGMKLVRE GARPISGDTG LRDVQRLAEA NDFPPVDETK RGRYQQINLR
160 170 180 190 200
DAYVDHLFGY INVKNLTPLK LVINSGNGAA GPVVDAIEAR FKALGAPVEL
210 220 230 240 250
IKVHNTPDGN FPNGIPNPLL PECRDDTRNA VIKHGADMGI AFDGDFDRCF
260 270 280 290 300
LFDEKGQFIE GYYIVGLLAE AFLEKNPGAK IIHDPRLSWN TVDVVTAAGT
310 320 330 340 350
PVMSKTGHAF IKERMRKEDA IYGGEMSAHH YFRDFAYCDT GMIPWLLVAE
360 370 380 390 400
LVCLKGKTLG ELVRDRMAAF PASGEINSKL AHPVEAINRV EQHFSRDAGG
410 420 430 440 450
GSHRWHQHDL CRLAALTCAS SNTEPVVRLN VESRGDVPLM EEKTKLILEL

LNK
Length:453
Mass (Da):49,932
Last modified:October 1, 1994 - v1
Checksum:iF1D1F69F97804391
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIRiD40630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF125322 Genomic DNA. Translation: AAC27539.1. Sequence problems.
PIRiD40630.

3D structure databases

ProteinModelPortaliP37742.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP37742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.

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.
[Graphical view]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRFBK7_ECOLX
AccessioniPrimary (citable) accession number: P37742
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: November 30, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.