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Q1W375 (PMM_TOBAC) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphomannomutase
EC=5.4.2.8
Alternative name(s):
NtPMM
OrganismNicotiana tabacum (Common tobacco)
Taxonomic identifier4097 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in ascorbic acid biosynthesis and in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions By similarity.

Catalytic activity

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

Pathway

Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the eukaryotic PMM family.

Caution

Ref.1 indicates this sequence as being of Nicotiana benthamiana origin.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processGDP-mannose biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

mannose biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionphosphomannomutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 252252Phosphomannomutase
PRO_0000326496

Sites

Active site131Nucleophile By similarity
Active site151 By similarity
Active site481 By similarity
Active site1901 By similarity
Binding site221Substrate By similarity
Binding site1241Substrate By similarity
Binding site1351Substrate By similarity
Binding site1421Substrate By similarity
Binding site1801Substrate By similarity
Binding site1821Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1W375 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: E9820AF015B0099A

FASTA25228,575
        10         20         30         40         50         60 
MAARKPGLIA LFDVDGTLTA PRKEVTPEML KFMKELRKVV TVGVVGGSDL VKISEQLGKT 

        70         80         90        100        110        120 
VTTDYDYCFS ENGLVAHKDG KLIGTQSLKS FLGDEKLKEF INFTLHYIAD LDIPIKRGTF 

       130        140        150        160        170        180 
IEFRSGMLNV SPIGRDCSQE ERDEFEKYDK VHKIRQTMVS VLREKFAHLN LTFSIGGQIS 

       190        200        210        220        230        240 
FDVFPQGWDK TYCLRYLEEF NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEDTVKQC 

       250 
SEQFLGKDNG SS

« Hide

References

[1]"Molecular and functional analysis of phosphomannomutase (PMM) from higher plants and genetic evidence for the involvement of PMM in ascorbic acid biosynthesis in Arabidopsis and Nicotiana benthamiana."
Qian W., Yu C., Qin H., Liu X., Zhang A., Johansen I.E., Wang D.
Plant J. 49:399-413(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		DQ442995 mRNA. Translation: ABD97874.1.

3D structure databases

ProteinModelPortalQ1W375.
SMRQ1W375. Positions 10-243.
ModBaseSearch...

Proteomic databases

PRIDEQ1W375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00126; UER00424.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
InterProIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERPTHR10466. PTHR10466. 1 hit.
PfamPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMSSF56784. HAD-like_dom. 1 hit.
TIGRFAMsTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePMM_TOBAC
AccessionPrimary (citable) accession number: Q1W375
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: March 6, 2013
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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