PGAM5_DROME
ID PGAM5_DROME Reviewed; 289 AA.
AC O46084; Q7K2X2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial;
DE Short=DPGAM5;
DE EC=3.1.3.16;
DE AltName: Full=Phosphoglycerate mutase family member 5 homolog;
GN Name=Pgam5; ORFNames=CG14816;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH PK92B.
RX PubMed=19590015; DOI=10.1073/pnas.0901823106;
RA Takeda K., Komuro Y., Hayakawa T., Oguchi H., Ishida Y., Murakami S.,
RA Noguchi T., Kinoshita H., Sekine Y., Iemura S., Natsume T., Ichijo H.;
RT "Mitochondrial phosphoglycerate mutase 5 uses alternate catalytic activity
RT as a protein serine/threonine phosphatase to activate ASK1.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:12301-12305(2009).
CC -!- FUNCTION: Displays phosphatase activity for serine/threonine residues,
CC and dephosphorylates and activates Pk92B kinase. Has apparently no
CC phosphoglycerate mutase activity. {ECO:0000269|PubMed:19590015}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19590015};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:19590015};
CC -!- SUBUNIT: Interacts with Pk92B/ASK1. {ECO:0000269|PubMed:19590015}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28156.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF45678.1; -; Genomic_DNA.
DR EMBL; AL021106; CAA15939.1; -; Genomic_DNA.
DR EMBL; AY060608; AAL28156.2; ALT_INIT; mRNA.
DR PIR; T12682; T12682.
DR RefSeq; NP_569951.1; NM_130595.3.
DR AlphaFoldDB; O46084; -.
DR SMR; O46084; -.
DR BioGRID; 57689; 26.
DR DIP; DIP-18549N; -.
DR IntAct; O46084; 21.
DR STRING; 7227.FBpp0070350; -.
DR PaxDb; O46084; -.
DR DNASU; 31143; -.
DR EnsemblMetazoa; FBtr0070366; FBpp0070350; FBgn0023517.
DR GeneID; 31143; -.
DR KEGG; dme:Dmel_CG14816; -.
DR UCSC; CG14816-RA; d. melanogaster.
DR CTD; 192111; -.
DR FlyBase; FBgn0023517; Pgam5.
DR VEuPathDB; VectorBase:FBgn0023517; -.
DR eggNOG; KOG4609; Eukaryota.
DR GeneTree; ENSGT00390000004796; -.
DR HOGENOM; CLU_063130_0_1_1; -.
DR InParanoid; O46084; -.
DR OMA; AWLRINI; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; O46084; -.
DR Reactome; R-DME-8934903; Receptor Mediated Mitophagy.
DR SignaLink; O46084; -.
DR BioGRID-ORCS; 31143; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31143; -.
DR PRO; PR:O46084; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0023517; Expressed in secondary oocyte and 21 other tissues.
DR ExpressionAtlas; O46084; baseline and differential.
DR Genevisible; O46084; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:FlyBase.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:FlyBase.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:FlyBase.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:FlyBase.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; IDA:FlyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0010821; P:regulation of mitochondrion organization; IMP:FlyBase.
DR GO; GO:0072347; P:response to anesthetic; IMP:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:FlyBase.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..289
FT /note="Serine/threonine-protein phosphatase Pgam5,
FT mitochondrial"
FT /id="PRO_0000288789"
FT TRANSMEM 7..23
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 289 AA; 33166 MW; 6DE63EE448170361 CRC64;
MRKLTSFVCG TGAGLAAYYL QRLRDPQTVV QNSWTHSDKP VDPWALWDTN WDCREPRALV
RPLRNSQPEE ENRYNAELEK AKAKKARHII LVRHGEYLDV GDSDDTHHLT ERGRKQAEFT
GKRLCELGIK WDKVVASTMV RAQETSDIIL KQIDFEKEKV VNCAFLREGA PIPPQPPVGH
WKPEASQFLR DGSRIEAGFR RYFHRAYPDQ EKESYTLIVG HGNVIRYFVC RALQFPAEGW
LRININHASI TWLTISPSGN VSIKYLGDSG FMPAELLTNR IPRDVKNVV
