Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Serine/threonine-protein phosphatase Pgam5, mitochondrial

Gene

Pgam5

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Displays phosphatase activity for serine/threonine residues, and dephosphorylates and activates Pk92B kinase. Has apparently no phosphoglycerate mutase activity.1 Publication

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • phosphoprotein phosphatase activity Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: FlyBase

GO - Biological processi

  • peptidyl-threonine dephosphorylation Source: FlyBase
  • positive regulation of mitochondrial fission Source: FlyBase
  • positive regulation of protein serine/threonine kinase activity Source: GOC
  • protein dephosphorylation Source: UniProtKB
  • regulation of mitochondrion organization Source: FlyBase
  • response to anesthetic Source: FlyBase
  • response to heat Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase Pgam5, mitochondrial (EC:3.1.3.16)
Short name:
DPGAM5
Alternative name(s):
Phosphoglycerate mutase family member 5 homolog
Gene namesi
Name:Pgam5
ORF Names:CG14816
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0023517. Pgam5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2317HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: FlyBase
  • mitochondrial outer membrane Source: UniProtKB-SubCell
  • mitochondrion Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion outer membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Serine/threonine-protein phosphatase Pgam5, mitochondrialPRO_0000288789Add
BLAST

Proteomic databases

PaxDbiO46084.
PRIDEiO46084.

Expressioni

Gene expression databases

BgeeiO46084.
GenevisibleiO46084. DM.

Interactioni

Subunit structurei

Interacts with Pk92B/ASK1.1 Publication

Protein-protein interaction databases

BioGridi57689. 20 interactions.
DIPiDIP-18549N.
IntActiO46084. 17 interactions.
MINTiMINT-928929.
STRINGi7227.FBpp0070350.

Structurei

3D structure databases

ProteinModelPortaliO46084.
SMRiO46084. Positions 78-278.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71348.
GeneTreeiENSGT00390000004796.
InParanoidiO46084.
KOiK15637.
OMAiEIIVCHA.
OrthoDBiEOG7966H1.
PhylomeDBiO46084.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.

Sequencei

Sequence statusi: Complete.

O46084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKLTSFVCG TGAGLAAYYL QRLRDPQTVV QNSWTHSDKP VDPWALWDTN
60 70 80 90 100
WDCREPRALV RPLRNSQPEE ENRYNAELEK AKAKKARHII LVRHGEYLDV
110 120 130 140 150
GDSDDTHHLT ERGRKQAEFT GKRLCELGIK WDKVVASTMV RAQETSDIIL
160 170 180 190 200
KQIDFEKEKV VNCAFLREGA PIPPQPPVGH WKPEASQFLR DGSRIEAGFR
210 220 230 240 250
RYFHRAYPDQ EKESYTLIVG HGNVIRYFVC RALQFPAEGW LRININHASI
260 270 280
TWLTISPSGN VSIKYLGDSG FMPAELLTNR IPRDVKNVV
Length:289
Mass (Da):33,166
Last modified:June 1, 1998 - v1
Checksum:i6DE63EE448170361
GO

Sequence cautioni

The sequence AAL28156.2 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF45678.1.
AL021106 Genomic DNA. Translation: CAA15939.1.
AY060608 mRNA. Translation: AAL28156.2. Different initiation.
PIRiT12682.
RefSeqiNP_569951.1. NM_130595.3.

Genome annotation databases

EnsemblMetazoaiFBtr0070366; FBpp0070350; FBgn0023517.
GeneIDi31143.
KEGGidme:Dmel_CG14816.
UCSCiCG14816-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014298 Genomic DNA. Translation: AAF45678.1.
AL021106 Genomic DNA. Translation: CAA15939.1.
AY060608 mRNA. Translation: AAL28156.2. Different initiation.
PIRiT12682.
RefSeqiNP_569951.1. NM_130595.3.

3D structure databases

ProteinModelPortaliO46084.
SMRiO46084. Positions 78-278.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57689. 20 interactions.
DIPiDIP-18549N.
IntActiO46084. 17 interactions.
MINTiMINT-928929.
STRINGi7227.FBpp0070350.

Proteomic databases

PaxDbiO46084.
PRIDEiO46084.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070366; FBpp0070350; FBgn0023517.
GeneIDi31143.
KEGGidme:Dmel_CG14816.
UCSCiCG14816-RA. d. melanogaster.

Organism-specific databases

CTDi192111.
FlyBaseiFBgn0023517. Pgam5.

Phylogenomic databases

eggNOGiNOG71348.
GeneTreeiENSGT00390000004796.
InParanoidiO46084.
KOiK15637.
OMAiEIIVCHA.
OrthoDBiEOG7966H1.
PhylomeDBiO46084.

Miscellaneous databases

GenomeRNAii31143.
NextBioi772127.
PROiO46084.

Gene expression databases

BgeeiO46084.
GenevisibleiO46084. DM.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
[Graphical view]
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 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(2000) [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 GENOMIC DNA].
    Strain: Oregon-R.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.
  5. "Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity as a protein serine/threonine phosphatase to activate ASK1."
    Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S., Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.
    Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PK92B.

Entry informationi

Entry nameiPGAM5_DROME
AccessioniPrimary (citable) accession number: O46084
Secondary accession number(s): Q7K2X2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 1998
Last modified: June 24, 2015
This is version 103 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. 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.