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Protein

Probable phosphomannomutase

Gene

CG10688

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei16 – 161NucleophileBy similarity
Active sitei18 – 181Proton donor/acceptorSequence Analysis
Binding sitei25 – 251SubstrateBy similarity
Binding sitei129 – 1291SubstrateBy similarity
Binding sitei140 – 1401SubstrateBy similarity
Binding sitei147 – 1471SubstrateBy similarity
Binding sitei185 – 1851SubstrateBy similarity
Binding sitei187 – 1871SubstrateBy similarity

GO - Molecular functioni

  1. phosphomannomutase activity Source: UniProtKB-EC

GO - Biological processi

  1. cellular response to hypoxia Source: FlyBase
  2. GDP-mannose biosynthetic process Source: UniProtKB-UniPathway
  3. mannose biosynthetic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Enzyme and pathway databases

ReactomeiREACT_351330. Synthesis of GDP-mannose.
UniPathwayiUPA00126; UER00424.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable phosphomannomutase (EC:5.4.2.8)
Short name:
PMM
Gene namesi
ORF Names:CG10688
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036300. CG10688.

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 – 254254Probable phosphomannomutasePRO_0000199699Add
BLAST

Proteomic databases

PaxDbiQ9VTZ6.
PRIDEiQ9VTZ6.

Expressioni

Gene expression databases

BgeeiQ9VTZ6.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi64785. 1 interaction.
STRINGi7227.FBpp0075693.

Structurei

3D structure databases

ProteinModelPortaliQ9VTZ6.
SMRiQ9VTZ6. Positions 12-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the eukaryotic PMM family.Curated

Phylogenomic databases

eggNOGiCOG0561.
GeneTreeiENSGT00390000002918.
InParanoidiQ9VTZ6.
KOiK17497.
OMAiQEERLEF.
OrthoDBiEOG773XH0.
PhylomeDBiQ9VTZ6.

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.

Q9VTZ6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTAALKRDE ILLLFDVDGT LTMPRSVVTP EFEEFFYSRV KPRATIGIVG
60 70 80 90 100
GSDLEKMFEQ LNGRKILNEF DFIFPENGLV QIEGGKEVGK QNIIMHLGEE
110 120 130 140 150
TVKRFINFVL RYLSELDVPI KRGTFIEFRN GMMNVCPIGR QCTREERNMF
160 170 180 190 200
AEYDIEHKVR EKMIKDLKQE FADVDLTYSI GGQISFDVFP HGWDKTYCLR
210 220 230 240 250
HIEAHYKFKE IHFFGDKTEP GGNDYEIYSD PRTISHRVYT PKDTQRILTE

ILEL
Length:254
Mass (Da):29,667
Last modified:May 1, 2000 - v1
Checksum:i716E05E7BB2438BB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49899.1.
BT009926 mRNA. Translation: AAQ22395.1.
RefSeqiNP_648589.1. NM_140332.2.
UniGeneiDm.23285.

Genome annotation databases

EnsemblMetazoaiFBtr0075961; FBpp0075693; FBgn0036300.
GeneIDi39436.
KEGGidme:Dmel_CG10688.
UCSCiCG10688-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49899.1.
BT009926 mRNA. Translation: AAQ22395.1.
RefSeqiNP_648589.1. NM_140332.2.
UniGeneiDm.23285.

3D structure databases

ProteinModelPortaliQ9VTZ6.
SMRiQ9VTZ6. Positions 12-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64785. 1 interaction.
STRINGi7227.FBpp0075693.

Proteomic databases

PaxDbiQ9VTZ6.
PRIDEiQ9VTZ6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075961; FBpp0075693; FBgn0036300.
GeneIDi39436.
KEGGidme:Dmel_CG10688.
UCSCiCG10688-RA. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0036300. CG10688.

Phylogenomic databases

eggNOGiCOG0561.
GeneTreeiENSGT00390000002918.
InParanoidiQ9VTZ6.
KOiK17497.
OMAiQEERLEF.
OrthoDBiEOG773XH0.
PhylomeDBiQ9VTZ6.

Enzyme and pathway databases

UniPathwayiUPA00126; UER00424.
ReactomeiREACT_351330. Synthesis of GDP-mannose.

Miscellaneous databases

GenomeRNAii39436.
NextBioi813625.

Gene expression databases

BgeeiQ9VTZ6.

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 Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiPMM_DROME
AccessioniPrimary (citable) accession number: Q9VTZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.