PGP_CHICK
ID PGP_CHICK Reviewed; 312 AA.
AC Q5F4B1;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Glycerol-3-phosphate phosphatase {ECO:0000305};
DE Short=G3PP {ECO:0000250|UniProtKB:Q8CHP8};
DE EC=3.1.3.21 {ECO:0000250|UniProtKB:Q8CHP8};
DE AltName: Full=Aspartate-based ubiquitous Mg(2+)-dependent phosphatase {ECO:0000250|UniProtKB:Q8CHP8};
DE Short=AUM {ECO:0000250|UniProtKB:Q8CHP8};
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q8CHP8};
DE AltName: Full=Phosphoglycolate phosphatase {ECO:0000250|UniProtKB:Q8CHP8};
DE Short=PGP {ECO:0000250|UniProtKB:Q8CHP8};
GN Name=PGP {ECO:0000250|UniProtKB:A6NDG6};
GN ORFNames=RCJMB04_1e2 {ECO:0000312|EMBL:CAH65023.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: Glycerol-3-phosphate phosphatase hydrolyzing glycerol-3-
CC phosphate into glycerol. Thereby, regulates the cellular levels of
CC glycerol-3-phosphate a metabolic intermediate of glucose, lipid and
CC energy metabolism. Was also shown to have a 2-phosphoglycolate
CC phosphatase activity and a tyrosine-protein phosphatase activity.
CC However, their physiological relevance is unclear. In vitro, has also a
CC phosphatase activity toward ADP, ATP, GDP and GTP.
CC {ECO:0000250|UniProtKB:A6NDG6, ECO:0000250|UniProtKB:Q8CHP8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 1-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:46084, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57685; EC=3.1.3.21;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycerol 3-phosphate = glycerol + phosphate;
CC Xref=Rhea:RHEA:66372, ChEBI:CHEBI:15377, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57597; EC=3.1.3.21;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8CHP8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q8CHP8};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8CHP8}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
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DR EMBL; AJ851389; CAH65023.1; -; mRNA.
DR RefSeq; NP_001025809.1; NM_001030638.1.
DR AlphaFoldDB; Q5F4B1; -.
DR SMR; Q5F4B1; -.
DR STRING; 9031.ENSGALP00000009453; -.
DR PaxDb; Q5F4B1; -.
DR GeneID; 416559; -.
DR KEGG; gga:416559; -.
DR CTD; 283871; -.
DR VEuPathDB; HostDB:geneid_416559; -.
DR eggNOG; KOG2882; Eukaryota.
DR InParanoid; Q5F4B1; -.
DR OrthoDB; 982374at2759; -.
DR PhylomeDB; Q5F4B1; -.
DR PRO; PR:Q5F4B1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000121; F:glycerol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043136; F:glycerol-3-phosphatase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006114; P:glycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; ISS:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006357; HAD-SF_hydro_IIA.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006349; PGP_euk.
DR Pfam; PF13344; Hydrolase_6; 1.
DR PIRSF; PIRSF000915; PGP-type_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01460; HAD-SF-IIA; 1.
DR TIGRFAMs; TIGR01452; PGP_euk; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..312
FT /note="Glycerol-3-phosphate phosphatase"
FT /id="PRO_0000316890"
FT ACT_SITE 30
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT ACT_SITE 32
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
FT BINDING 30
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 32
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P60487"
FT SITE 195
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:Q8CHP8"
SQ SEQUENCE 312 AA; 32996 MW; B7EFD4957C78E9A2 CRC64;
MAATGGRRCR RLEGETARAV LANVDTLLFD CDGVLWRGEA ALSGAPAALG RLAAAGKRLC
YVTNNSSRTR VAYTEKLRRL GFPPAEPRHV FGSAFCAARY LRQALPPGAA AYVLGGPALS
AELEAAGIPH LGPGPAALPG PAPADWAQAP LEPAVRAVLV GFDEHFSYAK LCQALRYLLR
GPDCLLVGTN RDNRLPLEGG SAIPGTGCLV KAVETAAERE ALIVGKPSRY IFDCVASEFD
IDPARTIMVG DRLDTDILMG NTCGLTTLLT LTGVSTLEEV RGHQESDCPA RQGLVPDYYV
DSIADLLPAL ED
