PGPP1_CHLRE
ID PGPP1_CHLRE Reviewed; 269 AA.
AC A0A2K3DU55;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 1.
DT 25-MAY-2022, entry version 17.
DE RecName: Full=Phosphatidylglycerophosphate phosphatase 1, chloroplastic {ECO:0000303|PubMed:25910650};
DE Short=CrPGPP1 {ECO:0000303|PubMed:25910650};
DE Short=PGP phosphatase 1 {ECO:0000303|PubMed:25910650};
DE EC=3.1.3.27 {ECO:0000269|PubMed:25910650};
DE Flags: Precursor;
GN Name=PGPP1 {ECO:0000303|PubMed:25910650};
GN Synonyms=Cre04.g219900 {ECO:0000303|PubMed:25910650};
GN ORFNames=CHLRE_04g219900v5 {ECO:0000312|EMBL:PNW84070.1};
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=17932292; DOI=10.1126/science.1143609;
RA Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT "The Chlamydomonas genome reveals the evolution of key animal and plant
RT functions.";
RL Science 318:245-250(2007).
RN [2]
RP FUNCTION, MUTAGENESIS OF ASP-103 AND ASP-105, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=25910650; DOI=10.1016/j.plaphy.2015.04.002;
RA Hung C.-H., Kobayashi K., Wada H., Nakamura Y.;
RT "Isolation and characterization of a phosphatidylglycerophosphate
RT phosphatase1, PGPP1, in Chlamydomonas reinhardtii.";
RL Plant Physiol. Biochem. 92:56-61(2015).
CC -!- FUNCTION: Phosphatidylglycerophosphate phosphatase involved in the
CC biosynthesis of phosphatidylglycerol (PG), a phosphoglycerolipid
CC predominantly present in chloroplastic thylakoid membranes and which
CC has important photosynthetic function (PubMed:25910650). Required for
CC thylakoid membranes development and chloroplast function (By
CC similarity). {ECO:0000250|UniProtKB:Q9LXR9,
CC ECO:0000269|PubMed:25910650}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) +
CC H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate;
CC Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27;
CC Evidence={ECO:0000269|PubMed:25910650};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33752;
CC Evidence={ECO:0000269|PubMed:25910650};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 2/2.
CC {ECO:0000269|PubMed:25910650}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; CM008965; PNW84070.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3DU55; -.
DR STRING; 3055.EDP04115; -.
DR EnsemblPlants; PNW84070; PNW84070; CHLRE_04g219900v5.
DR Gramene; PNW84070; PNW84070; CHLRE_04g219900v5.
DR OMA; IFVGDRY; -.
DR UniPathway; UPA00084; UER00504.
DR Proteomes; UP000006906; Chromosome 4.
DR ExpressionAtlas; A0A2K3DU55; baseline.
DR GO; GO:0009507; C:chloroplast; ISS:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IDA:UniProtKB.
DR GO; GO:0009658; P:chloroplast organization; ISS:UniProtKB.
DR GO; GO:0046486; P:glycerolipid metabolic process; IDA:UniProtKB.
DR GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046839; P:phospholipid dephosphorylation; IDA:UniProtKB.
DR GO; GO:0015979; P:photosynthesis; ISS:UniProtKB.
DR GO; GO:0010027; P:thylakoid membrane organization; ISS:UniProtKB.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR027706; PGP_Pase.
DR InterPro; IPR010021; PGPP1/Gep4.
DR PANTHER; PTHR19288:SF25; PTHR19288:SF25; 1.
DR Pfam; PF09419; PGP_phosphatase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01668; YqeG_hyp_ppase; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 34..269
FT /note="Phosphatidylglycerophosphate phosphatase 1,
FT chloroplastic"
FT /id="PRO_0000449814"
FT REGION 25..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 103..107
FT /note="Phosphoryl acceptor"
FT /evidence="ECO:0000250|UniProtKB:P38812"
FT SITE 103
FT /note="Required for phosphatidylglycerophosphate
FT phosphatase activity"
FT /evidence="ECO:0000269|PubMed:25910650"
FT MUTAGEN 103
FT /note="D->N: Disturbed phosphatidylglycerophosphate
FT phosphatase activity. Impaired phosphatidylglycerophosphate
FT phosphatase activity; when associated with N-105."
FT /evidence="ECO:0000269|PubMed:25910650"
FT MUTAGEN 105
FT /note="D->N: Normal phosphatidylglycerophosphate
FT phosphatase activity. Impaired phosphatidylglycerophosphate
FT phosphatase activity; when associated with N-103."
FT /evidence="ECO:0000269|PubMed:25910650"
SQ SEQUENCE 269 AA; 28620 MW; 888CADDAEB9CCE5F CRC64;
MRSVPGPSPP CTRSLAHSCR AAARGPCGSA RPRARSVSAR AHSSEASDMA RVQQNFNSAG
VGLFFSLFGG NQSLALPHLA APDIRHVDWR ALKAAGFKGL VFDKDNTLSL PFALEVEPRL
QPALAGCLEA FGGRAVLYSN SAGLQQYDPE GKEAAALEAA LGIPVLRHAD KKPGGGCAEL
EAHFGCPAPQ LIMVGDRYLT DIAFGNRHGM LTVHVQPLTT SGEPFGVVMA RRIEEFWVAR
WTSFGVHPPA HSLAPHDTLA AYVKDQPIA
