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Protein

Phosphomannomutase

Gene

pmm1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved 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.

Pathway:iGDP-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. Mannose-6-phosphate isomerase (pmi40)
  2. Phosphomannomutase (pmm1)
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei19 – 191NucleophileBy similarity
Active sitei21 – 211Proton donor/acceptorSequence Analysis
Binding sitei28 – 281SubstrateBy similarity
Binding sitei133 – 1331SubstrateBy similarity
Binding sitei144 – 1441SubstrateBy similarity
Binding sitei151 – 1511SubstrateBy similarity
Binding sitei189 – 1891SubstrateBy similarity
Binding sitei191 – 1911SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • ER to Golgi vesicle-mediated transport Source: PomBase
  • GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  • intracellular protein transport Source: PomBase
  • mannose biosynthetic process Source: InterPro
  • nuclear envelope organization Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiREACT_292344. Synthesis of GDP-mannose.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
Name:pmm1
ORF Names:SPAC1556.07
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.07.
PomBaseiSPAC1556.07. pmm1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 257257PhosphomannomutasePRO_0000199702Add
BLAST

Proteomic databases

MaxQBiQ9UTJ2.
PaxDbiQ9UTJ2.
PRIDEiQ9UTJ2.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi278170. 4 interactions.
MINTiMINT-4710595.

Structurei

3D structure databases

ProteinModelPortaliQ9UTJ2.
SMRiQ9UTJ2. Positions 13-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiCOG0561.
HOGENOMiHOG000181843.
InParanoidiQ9UTJ2.
KOiK17497.
OMAiNDYEIYD.
OrthoDBiEOG7X3R31.
PhylomeDBiQ9UTJ2.

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.

Q9UTJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVIPIEERK FPKTLVLFDV DGTLTPARLS VSPEMLETLQ NLRKVVAIGF
60 70 80 90 100
VGGSDLSKQQ EQLSVNGENV IDSFDYAFAE NGLTAYRYGQ QLASQSFIAW
110 120 130 140 150
LGEEKYQKLV NFCLHYIADL DIPVKRGTFI EFRNGMINIS PVGRNANTEE
160 170 180 190 200
RNEFERFDKG RKIRATMVDV LREKFKDYGL TFSIGGQISF DVFPAGWDKT
210 220 230 240 250
YCLQHVEKEG FDTIHFFGDK TYKGGNDYEI FVDPRTIGHS VTNPDDTIAE

LKKIFNI
Length:257
Mass (Da):29,223
Last modified:May 1, 2000 - v1
Checksum:i789AA77A7C169E52
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB61218.1.
AB000703 mRNA. Translation: BAA19164.1.
PIRiT50086.
RefSeqiNP_594325.1. NM_001019747.2.

Genome annotation databases

EnsemblFungiiSPAC1556.07.1; SPAC1556.07.1:pep; SPAC1556.07.
GeneIDi2541674.
KEGGispo:SPAC1556.07.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB61218.1.
AB000703 mRNA. Translation: BAA19164.1.
PIRiT50086.
RefSeqiNP_594325.1. NM_001019747.2.

3D structure databases

ProteinModelPortaliQ9UTJ2.
SMRiQ9UTJ2. Positions 13-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278170. 4 interactions.
MINTiMINT-4710595.

Proteomic databases

MaxQBiQ9UTJ2.
PaxDbiQ9UTJ2.
PRIDEiQ9UTJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC1556.07.1; SPAC1556.07.1:pep; SPAC1556.07.
GeneIDi2541674.
KEGGispo:SPAC1556.07.

Organism-specific databases

EuPathDBiFungiDB:SPAC1556.07.
PomBaseiSPAC1556.07. pmm1.

Phylogenomic databases

eggNOGiCOG0561.
HOGENOMiHOG000181843.
InParanoidiQ9UTJ2.
KOiK17497.
OMAiNDYEIYD.
OrthoDBiEOG7X3R31.
PhylomeDBiQ9UTJ2.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
ReactomeiREACT_292344. Synthesis of GDP-mannose.

Miscellaneous databases

NextBioi20802767.
PROiQ9UTJ2.

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

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "S.pombe phosphomannomutase homolog."
    Kawamukai M.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-257.

Entry informationi

Entry nameiPMM_SCHPO
AccessioniPrimary (citable) accession number: Q9UTJ2
Secondary accession number(s): P79012
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  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.