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DGDG1_ARATH
ID   DGDG1_ARATH             Reviewed;         808 AA.
AC   Q9S7D1; Q3EB81; W8PUU5;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Digalactosyldiacylglycerol synthase 1, chloroplastic;
DE            EC=2.4.1.241;
DE   Flags: Precursor;
GN   Name=DGD1; OrderedLocusNames=At3g11670; ORFNames=T19F11.7;
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 [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
RP   AND MUTAGENESIS OF 640-TYR--TRP-808.
RX   PubMed=10381884; DOI=10.1126/science.284.5423.2181;
RA   Doermann P., Balbo I., Benning C.;
RT   "Arabidopsis galactolipid biosynthesis and lipid trafficking mediated by
RT   DGD1.";
RL   Science 284:2181-2184(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=24905498; DOI=10.1111/tpj.12577;
RA   Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA   Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA   Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA   Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA   Loque D., Scheller H.V., Heazlewood J.L.;
RT   "The plant glycosyltransferase clone collection for functional genomics.";
RL   Plant J. 79:517-529(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11429410; DOI=10.1074/jbc.m104652200;
RA   Froehlich J.E., Benning C., Doermann P.;
RT   "The digalactosyldiacylglycerol (DGDG) synthase DGD1 is inserted into the
RT   outer envelope membrane of chloroplasts in a manner independent of the
RT   general import pathway and does not depend on direct interaction with
RT   monogalactosyldiacylglycerol synthase for DGDG biosynthesis.";
RL   J. Biol. Chem. 276:31806-31812(2001).
RN   [7]
RP   INDUCTION, AND FUNCTION.
RX   PubMed=14600212; DOI=10.1105/tpc016675;
RA   Kelly A.A., Froehlich J.E., Doermann P.;
RT   "Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and
RT   DGD2 in Arabidopsis reveals the existence of an additional enzyme of
RT   galactolipid synthesis.";
RL   Plant Cell 15:2694-2706(2003).
RN   [8]
RP   FUNCTION.
RX   PubMed=15961080; DOI=10.1016/j.febslet.2005.05.049;
RA   Guo J., Zhang Z., Bi Y., Yang W., Xu Y., Zhang L.;
RT   "Decreased stability of photosystem I in dgd1 mutant of Arabidopsis
RT   thaliana.";
RL   FEBS Lett. 579:3619-3624(2005).
RN   [9]
RP   FUNCTION.
RX   PubMed=16854937; DOI=10.1093/pcp/pcj089;
RA   Ivanov A.G., Hendrickson L., Krol M., Selstam E., Oquist G., Hurry V.,
RA   Huner N.P.;
RT   "Digalactosyl-diacylglycerol deficiency impairs the capacity for
RT   photosynthetic intersystem electron transport and state transitions in
RT   Arabidopsis thaliana due to photosystem I acceptor-side limitations.";
RL   Plant Cell Physiol. 47:1146-1157(2006).
CC   -!- FUNCTION: Involved in the synthesis of diacylglycerol galactolipids
CC       that are specifically found in thylakoid membranes. Specific for alpha-
CC       glycosidic linkages (PubMed:10381884, PubMed:14600212). Responsible for
CC       the final assembly of galactolipids in photosynthetic membranes.
CC       Digalactosyldiacylglycerol (DGDG) provides stability to the photosystem
CC       I (PSI) complex, especially to the PsaA, PsaB, PsaC, PsaL and PsaH
CC       subunits (PubMed:15961080, PubMed:16854937).
CC       {ECO:0000269|PubMed:10381884, ECO:0000269|PubMed:14600212,
CC       ECO:0000269|PubMed:15961080, ECO:0000269|PubMed:16854937}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol + UDP-alpha-
CC         D-galactose = 1,2-diacyl-3-O-[alpha-D-galactosyl-(1->6)-beta-D-
CC         galactosyl]-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:10520,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17615, ChEBI:CHEBI:28396,
CC         ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.241;
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast outer membrane
CC       {ECO:0000269|PubMed:11429410}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9S7D1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9S7D1-2; Sequence=VSP_022342;
CC   -!- INDUCTION: 6-fold up-regulation by phosphate deficiency.
CC       {ECO:0000269|PubMed:14600212}.
CC   -!- DISRUPTION PHENOTYPE: Altered thylakoid membrane lipid composition and
CC       stunted phenotype. {ECO:0000269|PubMed:10381884}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC       Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR   EMBL; AF149842; AAD42379.1; -; Genomic_DNA.
DR   EMBL; AF149841; AAD42378.1; -; mRNA.
DR   EMBL; KJ138827; AHL38767.1; -; mRNA.
DR   EMBL; AC009918; AAF02140.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75081.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75082.1; -; Genomic_DNA.
DR   EMBL; AY101521; AAM26642.1; -; mRNA.
DR   EMBL; AY075649; AAL77656.1; -; mRNA.
DR   RefSeq; NP_187773.1; NM_111999.4. [Q9S7D1-1]
DR   RefSeq; NP_850561.1; NM_180230.1. [Q9S7D1-2]
DR   AlphaFoldDB; Q9S7D1; -.
DR   SMR; Q9S7D1; -.
DR   STRING; 3702.AT3G11670.1; -.
DR   SwissLipids; SLP:000001451; -.
DR   CAZy; GT4; Glycosyltransferase Family 4.
DR   iPTMnet; Q9S7D1; -.
DR   PaxDb; Q9S7D1; -.
DR   PRIDE; Q9S7D1; -.
DR   ProteomicsDB; 224036; -. [Q9S7D1-1]
DR   EnsemblPlants; AT3G11670.1; AT3G11670.1; AT3G11670. [Q9S7D1-1]
DR   EnsemblPlants; AT3G11670.2; AT3G11670.2; AT3G11670. [Q9S7D1-2]
DR   GeneID; 820339; -.
DR   Gramene; AT3G11670.1; AT3G11670.1; AT3G11670. [Q9S7D1-1]
DR   Gramene; AT3G11670.2; AT3G11670.2; AT3G11670. [Q9S7D1-2]
DR   KEGG; ath:AT3G11670; -.
DR   Araport; AT3G11670; -.
DR   TAIR; locus:2098333; AT3G11670.
DR   eggNOG; ENOG502QQ73; Eukaryota.
DR   HOGENOM; CLU_011647_0_1_1; -.
DR   InParanoid; Q9S7D1; -.
DR   OMA; DHAKHDP; -.
DR   PhylomeDB; Q9S7D1; -.
DR   BioCyc; MetaCyc:AT3G11670-MON; -.
DR   BRENDA; 2.4.1.241; 399.
DR   PRO; PR:Q9S7D1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9S7D1; baseline and differential.
DR   Genevisible; Q9S7D1; AT.
DR   GO; GO:0009707; C:chloroplast outer membrane; IDA:TAIR.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0046481; F:digalactosyldiacylglycerol synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016757; F:glycosyltransferase activity; IMP:TAIR.
DR   GO; GO:0035250; F:UDP-galactosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0019375; P:galactolipid biosynthetic process; IDA:TAIR.
DR   GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:TAIR.
DR   GO; GO:0009809; P:lignin biosynthetic process; IMP:TAIR.
DR   GO; GO:0031408; P:oxylipin biosynthetic process; IMP:TAIR.
DR   GO; GO:0042550; P:photosystem I stabilization; TAS:TAIR.
DR   GO; GO:0009266; P:response to temperature stimulus; IMP:TAIR.
DR   InterPro; IPR044525; DGDG1/2.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   PANTHER; PTHR46132; PTHR46132; 1.
DR   Pfam; PF00534; Glycos_transf_1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chloroplast; Glycosyltransferase; Membrane; Plastid;
KW   Plastid outer membrane; Reference proteome; Transferase; Transit peptide.
FT   TRANSIT         1..58
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           59..808
FT                   /note="Digalactosyldiacylglycerol synthase 1,
FT                   chloroplastic"
FT                   /id="PRO_0000252337"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         640..808
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_022342"
FT   MUTAGEN         640..808
FT                   /note="Missing: In dgd1-1; altered thylakoid membrane lipid
FT                   composition and stunted phenotype."
FT                   /evidence="ECO:0000269|PubMed:10381884"
SQ   SEQUENCE   808 AA;  91829 MW;  A6FC227AF98BB24D CRC64;
     MVKETLIPPS STSMTTGTSS SSSLSMTLSS TNALSFLSKG WREVWDSADA DLQLMRDRAN
     SVKNLASTFD REIENFLNNS ARSAFPVGSP SASSFSNEIG IMKKLQPKIS EFRRVYSAPE
     ISRKVMERWG PARAKLGMDL SAIKKAIVSE MELDERQGVL EMSRLRRRRN SDRVRFTEFF
     AEAERDGEAY FGDWEPIRSL KSRFKEFEKR SSLEILSGFK NSEFVEKLKT SFKSIYKETD
     EAKDVPPLDV PELLACLVRQ SEPFLDQIGV RKDTCDRIVE SLCKCKSQQL WRLPSAQASD
     LIENDNHGVD LDMRIASVLQ STGHHYDGGF WTDFVKPETP ENKRHVAIVT TASLPWMTGT
     AVNPLFRAAY LAKAAKQSVT LVVPWLCESD QELVYPNNLT FSSPEEQESY IRKWLEERIG
     FKADFKISFY PGKFSKERRS IFPAGDTSQF ISSKDADIAI LEEPEHLNWY YHGKRWTDKF
     NHVVGIVHTN YLEYIKREKN GALQAFFVNH VNNWVTRAYC DKVLRLSAAT QDLPKSVVCN
     VHGVNPKFLM IGEKIAEERS RGEQAFSKGA YFLGKMVWAK GYRELIDLMA KHKSELGSFN
     LDVYGNGEDA VEVQRAAKKH DLNLNFLKGR DHADDALHKY KVFINPSISD VLCTATAEAL
     AMGKFVVCAD HPSNEFFRSF PNCLTYKTSE DFVSKVQEAM TKEPLPLTPE QMYNLSWEAA
     TQRFMEYSDL DKILNNGEGG RKMRKSRSVP SFNEVVDGGL AFSHYVLTGN DFLRLCTGAT
     PRTKDYDNQH CKDLNLVPPH VHKPIFGW
 
 
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