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PGPS1_ARATH
ID   PGPS1_ARATH             Reviewed;         296 AA.
AC   O80952; Q67ZP8;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase 1, chloroplastic;
DE            EC=2.7.8.5;
DE   AltName: Full=Phosphatidylglycerophosphate synthase 1;
DE            Short=PGP synthase 1;
DE   Flags: Precursor;
GN   Name=PGPS1; Synonyms=PGP1, PGS1; OrderedLocusNames=At2g39290;
GN   ORFNames=T16B24.7;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF PRO-170, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=12068104; DOI=10.1104/pp.002725;
RA   Xu C., Hartel H., Wada H., Hagio M., Yu B., Eakin C., Benning C.;
RT   "The pgp1 mutant locus of Arabidopsis encodes a
RT   phosphatidylglycerolphosphate synthase with impaired activity.";
RL   Plant Physiol. 129:594-604(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Kim C.J., Chen H., Shinn P., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11741606; DOI=10.1016/s0014-5793(01)03163-5;
RA   Muller F., Frentzen M.;
RT   "Phosphatidylglycerophosphate synthases from Arabidopsis thaliana.";
RL   FEBS Lett. 509:298-302(2001).
CC   -!- FUNCTION: Catalyzes the committed step to the synthesis of the acidic
CC       phospholipids. Transfers specifically a phosphatidyl group from CDP-
CC       diacylglycerol to glycerol-3-phosphate to form
CC       phosphatidylglycerophosphate. Cannot catalyze the phosphatidyl group
CC       transfer to inositol, serine, choline or phosphatidylglycerol.
CC       Possesses high activity with CDP-dipalmitoylglycerol and low activity
CC       with CDP-dioleoylglycerol. {ECO:0000269|PubMed:11741606,
CC       ECO:0000269|PubMed:12068104}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC         diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC         H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC         ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC         Evidence={ECO:0000269|PubMed:11741606};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:11741606};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=52 uM for glycerol-3-phosphate {ECO:0000269|PubMed:11741606};
CC         KM=12 uM for CDP-dipalmitoylglycerol {ECO:0000269|PubMed:11741606};
CC       pH dependence:
CC         Optimum pH is 8.5. {ECO:0000269|PubMed:11741606};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC       phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC       {ECO:0000305|PubMed:11741606}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Pale green plants with impaired photosynthesis.
CC       {ECO:0000269|PubMed:12068104}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
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DR   EMBL; AB048535; BAB39133.1; -; mRNA.
DR   EMBL; AB058617; BAB68508.1; -; mRNA.
DR   EMBL; AC004697; AAC28995.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC09655.1; -; Genomic_DNA.
DR   EMBL; AK176069; BAD43832.1; -; mRNA.
DR   EMBL; BT024857; ABD65588.1; -; mRNA.
DR   PIR; T02573; T02573.
DR   RefSeq; NP_181461.1; NM_129486.5.
DR   AlphaFoldDB; O80952; -.
DR   SMR; O80952; -.
DR   BioGRID; 3852; 11.
DR   IntAct; O80952; 11.
DR   STRING; 3702.AT2G39290.1; -.
DR   PaxDb; O80952; -.
DR   PRIDE; O80952; -.
DR   ProteomicsDB; 234901; -.
DR   EnsemblPlants; AT2G39290.1; AT2G39290.1; AT2G39290.
DR   GeneID; 818514; -.
DR   Gramene; AT2G39290.1; AT2G39290.1; AT2G39290.
DR   KEGG; ath:AT2G39290; -.
DR   Araport; AT2G39290; -.
DR   TAIR; locus:2056068; AT2G39290.
DR   eggNOG; KOG1617; Eukaryota.
DR   HOGENOM; CLU_051314_2_1_1; -.
DR   InParanoid; O80952; -.
DR   OMA; CVFAPRH; -.
DR   OrthoDB; 1169813at2759; -.
DR   PhylomeDB; O80952; -.
DR   BioCyc; MetaCyc:AT2G39290-MON; -.
DR   SABIO-RK; O80952; -.
DR   UniPathway; UPA00084; UER00503.
DR   PRO; PR:O80952; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; O80952; baseline and differential.
DR   Genevisible; O80952; AT.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IDA:TAIR.
DR   GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006655; P:phosphatidylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IDA:TAIR.
DR   GO; GO:0010027; P:thylakoid membrane organization; IMP:TAIR.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   TIGRFAMs; TIGR00560; pgsA; 1.
DR   PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Plastid;
KW   Reference proteome; Transferase; Transit peptide; Transmembrane;
KW   Transmembrane helix.
FT   TRANSIT         1..39
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           40..296
FT                   /note="CDP-diacylglycerol--glycerol-3-phosphate 3-
FT                   phosphatidyltransferase 1, chloroplastic"
FT                   /id="PRO_0000429135"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          62..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         170
FT                   /note="P->S: In pgp1; reduces activity 5-fold."
FT                   /evidence="ECO:0000269|PubMed:12068104"
FT   CONFLICT        276
FT                   /note="A -> V (in Ref. 4; BAD43832)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   296 AA;  32158 MW;  384987E0780B1446 CRC64;
     MLRSGLASLI VDVNLRRTLR PSPTFSFPAH LSRCIITSRY SSRTSLRFPI QISRHQHRLS
     YFSSSSSSEQ SRPTSSSRNS FSGHGQLDSD DNSSPPPSQS SSKVLTLPTV LTLGRVAAVP
     LLVATFYVDS WWGTTATTSI FIAAAITDWL DGYLARKMRL GSAFGAFLDP VADKLMVAAT
     LILLCTKPIQ VAELGPLPWL LTVPSIAIIG REITMSAVRE WAASQNGKLL EAVAVNNLGK
     WKTATQMTAL TILLASRDSN VGWLVASGAG LLYVSAGLSV WSLAVYMRKI WKVLMK
 
 
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