位置:首页 > 蛋白库 > PGAM5_CAEBR
PGAM5_CAEBR
ID   PGAM5_CAEBR             Reviewed;         283 AA.
AC   Q61CA3; A8XGV6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Serine/threonine-protein phosphatase Pgam5, mitochondrial;
DE            EC=3.1.3.16 {ECO:0000250|UniProtKB:Q96HS1};
DE   AltName: Full=Phosphoglycerate mutase family member 5 homolog;
GN   Name=pgam-5; ORFNames=CBG13006;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Displays phosphatase activity for serine/threonine residues.
CC       Has apparently no phosphoglycerate mutase activity.
CC       {ECO:0000250|UniProtKB:Q96HS1}.
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:0000250|UniProtKB:Q96HS1};
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:0000250|UniProtKB:Q96HS1};
CC   -!- SUBUNIT: Interacts with skn-1. {ECO:0000250|UniProtKB:Q09422}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC       {ECO:0000250|UniProtKB:Q96HS1}; Single-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC       dependent PGAM subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; HE600938; CAP31880.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q61CA3; -.
DR   SMR; Q61CA3; -.
DR   STRING; 6238.CBG13006; -.
DR   PRIDE; Q61CA3; -.
DR   EnsemblMetazoa; CBG13006a.1; CBG13006a.1; WBGene00033850.
DR   WormBase; CBG13006a; CBP36220; WBGene00033850; Cbr-pgam-5.
DR   eggNOG; KOG4609; Eukaryota.
DR   HOGENOM; CLU_063130_1_1_1; -.
DR   InParanoid; Q61CA3; -.
DR   OMA; WHSPLPR; -.
DR   OrthoDB; 1112626at2759; -.
DR   Proteomes; UP000008549; Chromosome II.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:UniProtKB.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IBA:GO_Central.
DR   GO; GO:0090141; P:positive regulation of mitochondrial fission; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
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; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..283
FT                   /note="Serine/threonine-protein phosphatase Pgam5,
FT                   mitochondrial"
FT                   /id="PRO_0000288788"
FT   TRANSMEM        7..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   283 AA;  32352 MW;  13294946775B4DB6 CRC64;
     MVSKILMYGL PSAAVAVGTA LLNEDNRNTI FRKAFAFTQN HTPKSFDEHF PRGEWDKNWD
     FRDPTSLVDK SKWEKADEVG KKKLLEECKA TASRNIFLIR HGQYHLDREQ KHLTELGREQ
     AELLGKRLAN SDIKFTNMTM STMTRATETA NIILKHLPGD LPKSSSSLIE EGPPYPPVPD
     HKTWRPLDPE FYTEAARIES AFRKLIHRAP PSQKEDSYEL IVCHANVIRY FICRALQFPP
     EGWLRMSLGN CSITWLVIRP KGHVSIRSVG DIGHLTPNKI SFT
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024