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Protein

Phosphomannomutase

Gene

manB

Organism
Escherichia coli O157:H7
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 O 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)
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 sitei98Phosphoserine intermediateBy similarity1
Metal bindingi98Magnesium; via phosphate groupBy similarity1
Metal bindingi245MagnesiumBy similarity1
Metal bindingi247MagnesiumBy similarity1
Metal bindingi249MagnesiumBy 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

BioCyciECOO157:MANB-MONOMER.
UniPathwayiUPA00126; UER00424.
UPA00281.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:manB
Ordered Locus Names:Z3194, ECs2835
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001478191 – 456PhosphomannomutaseAdd BLAST456

Keywords - PTMi

Phosphoprotein

Interactioni

Protein-protein interaction databases

STRINGi155864.Z3194.

Structurei

3D structure databases

ProteinModelPortaliO85343.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiENOG4107QKV. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268679.
KOiK01840.
OMAiFDKEWVH.

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.

O85343-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSLTCFKAY DIRGKLGEEL NEDIAWRIGR AYGEFLKPKT IVLGGDVRLT
60 70 80 90 100
SEALKLALAK 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
VAELVCLKGK TLGEMVRDRM AAFPASGEIN SKLAQPVEAI NRVEQHFSRE
410 420 430 440 450
ALAVDRTDGI SMTFADWRFN LRSSNTEPVV RLNVESRGDV KLMEKKTKAL

LKLLSE
Length:456
Mass (Da):50,340
Last modified:November 1, 1998 - v1
Checksum:i6845D9D2DD7628B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061251 Genomic DNA. Translation: AAC32349.1.
AB008676 Genomic DNA. Translation: BAA77734.1.
AE005174 Genomic DNA. Translation: AAG57090.1.
BA000007 Genomic DNA. Translation: BAB36258.1.
PIRiC90983.
F85828.
RefSeqiNP_310862.1. NC_002695.1.
WP_000839208.1. NZ_LPWC02000002.1.

Genome annotation databases

EnsemblBacteriaiAAG57090; AAG57090; Z3194.
BAB36258; BAB36258; BAB36258.
GeneIDi913941.
KEGGiece:Z3194.
ecs:ECs2835.
PATRICi18355054. VBIEscCol44059_2728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF061251 Genomic DNA. Translation: AAC32349.1.
AB008676 Genomic DNA. Translation: BAA77734.1.
AE005174 Genomic DNA. Translation: AAG57090.1.
BA000007 Genomic DNA. Translation: BAB36258.1.
PIRiC90983.
F85828.
RefSeqiNP_310862.1. NC_002695.1.
WP_000839208.1. NZ_LPWC02000002.1.

3D structure databases

ProteinModelPortaliO85343.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi155864.Z3194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAG57090; AAG57090; Z3194.
BAB36258; BAB36258; BAB36258.
GeneIDi913941.
KEGGiece:Z3194.
ecs:ECs2835.
PATRICi18355054. VBIEscCol44059_2728.

Phylogenomic databases

eggNOGiENOG4107QKV. Bacteria.
COG1109. LUCA.
HOGENOMiHOG000268679.
KOiK01840.
OMAiFDKEWVH.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
UPA00281.
BioCyciECOO157:MANB-MONOMER.

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...

Entry informationi

Entry nameiMANB_ECO57
AccessioniPrimary (citable) accession number: O85343
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: November 1, 1998
Last modified: November 2, 2016
This is version 107 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

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.