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Protein

Phosphomannomutase

Gene
N/A
Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei13 – 131NucleophileBy similarity
Active sitei15 – 151Proton donor/acceptorSequence Analysis
Binding sitei22 – 221SubstrateBy similarity
Binding sitei124 – 1241SubstrateBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Binding sitei142 – 1421SubstrateBy similarity
Binding sitei180 – 1801SubstrateBy similarity
Binding sitei182 – 1821SubstrateBy similarity

GO - Molecular functioni

  1. phosphomannomutase activity Source: UniProtKB-EC

GO - Biological processi

  1. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  2. mannose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Alternative name(s):
NtPMM
OrganismiNicotiana tabacum (Common tobacco)
Taxonomic identifieri4097 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeNicotianoideaeNicotianeaeNicotiana

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 252252PhosphomannomutasePRO_0000326496Add
BLAST

Proteomic databases

PRIDEiQ1W375.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ1W375.
SMRiQ1W375. Positions 10-243.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q1W375-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAARKPGLIA LFDVDGTLTA PRKEVTPEML KFMKELRKVV TVGVVGGSDL
60 70 80 90 100
VKISEQLGKT VTTDYDYCFS ENGLVAHKDG KLIGTQSLKS FLGDEKLKEF
110 120 130 140 150
INFTLHYIAD LDIPIKRGTF IEFRSGMLNV SPIGRDCSQE ERDEFEKYDK
160 170 180 190 200
VHKIRQTMVS VLREKFAHLN LTFSIGGQIS FDVFPQGWDK TYCLRYLEEF
210 220 230 240 250
NEIHFFGDKT YKGGNDHEIY ESERTVGHTV TSPEDTVKQC SEQFLGKDNG

SS
Length:252
Mass (Da):28,575
Last modified:May 2, 2006 - v1
Checksum:iE9820AF015B0099A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ442995 mRNA. Translation: ABD97874.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ442995 mRNA. Translation: ABD97874.1.

3D structure databases

ProteinModelPortaliQ1W375.
SMRiQ1W375. Positions 10-243.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ1W375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006379. HAD-SF_hydro_IIB.
IPR005002. PMM.
[Graphical view]
PANTHERiPTHR10466. PTHR10466. 1 hit.
PfamiPF03332. PMM. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01484. HAD-SF-IIB. 1 hit.
ProtoNetiSearch...

Publicationsi

  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].

Entry informationi

Entry nameiPMM_TOBAC
AccessioniPrimary (citable) accession number: Q1W375
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: May 2, 2006
Last modified: January 7, 2015
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Caution

PubMed:17217471 indicates this sequence as being of Nicotiana benthamiana origin.Curated

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.