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Protein

Monogalactosyldiacylglycerol synthase, chloroplastic

Gene

MGD A

Organism
Spinacia oleracea (Spinach)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the synthesis of the major structural component of photosynthetic membranes. The 1,2-diacylglycerol substrate preference is 18:2/18:2 > 18:0/18:1 > 18:1/18:1 > 18:1/16:0 > 16:0/18:2 > 18:3/18:3 > 16:0/18:1 > 16:0/16:0 > 18:0/18:0.1 Publication

Catalytic activityi

UDP-alpha-D-galactose + 1,2-diacyl-sn-glycerol = UDP + 3-beta-D-galactosyl-1,2-diacyl-sn-glycerol.

Cofactori

Zn2+Curated

Enzyme regulationi

Inhibited by ortho-phenanthroline and UDP (competitive inhibitor relatively to UDP-Gal only) and inactivated by citraconic anhydride, tert-butoxycarbonyl-L-methionine hydrosuccinimidyl ester (SLR) and N-ethylmaleimide (NEM).2 Publications

Kineticsi

  1. KM=0.65 mM for UDP-Gal1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei422 – 4221Substrate specificity for galactose

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.46. 5812.

    Protein family/group databases

    CAZyiGT28. Glycosyltransferase Family 28.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Monogalactosyldiacylglycerol synthase, chloroplastic (EC:2.4.1.46)
    Short name:
    SoMGD1
    Alternative name(s):
    MGDG synthase type A
    Gene namesi
    Name:MGD A
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Chloroplast, Membrane, Plastid, Plastid inner membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi171 – 1711W → A: 90% reduction of activity. 1 Publication
    Mutagenesisi173 – 1731E → N: 90% reduction of activity. 1 Publication
    Mutagenesisi177 – 1771W → A: 90% reduction of activity. 1 Publication
    Mutagenesisi240 – 2401H → A: Total loss of activity. 1 Publication
    Mutagenesisi245 – 2451H → A: 90% reduction of activity. 1 Publication
    Mutagenesisi284 – 2841C → A: No effect. 1 Publication
    Mutagenesisi286 – 2861C → A: No effect. 1 Publication
    Mutagenesisi343 – 3475Missing : Total loss of activity. 1 Publication
    Mutagenesisi346 – 3461E → A: 90% reduction of activity. 1 Publication
    Mutagenesisi378 – 3781C → A: 25% reduction of activity. 1 Publication
    Mutagenesisi380 – 3801R → E: 90% reduction of activity. 1 Publication
    Mutagenesisi402 – 4021F → A: 90% reduction of activity. 1 Publication
    Mutagenesisi415 – 4151C → A: No effect. 1 Publication
    Mutagenesisi419 – 4191K → A: Total loss of activity. 1 Publication
    Mutagenesisi427 – 4271E → A: Total loss of activity. 1 Publication
    Mutagenesisi445 – 4451E → A: Total loss of activity. 1 Publication
    Mutagenesisi448 – 4481N → A: 90% reduction of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 9898ChloroplastSequence AnalysisAdd
    BLAST
    Chaini99 – 522424Monogalactosyldiacylglycerol synthase, chloroplasticPRO_5000065674Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Structurei

    3D structure databases

    ProteinModelPortaliQ9SM44.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    The C-terminal domain (308-483) is involved in UDP-Gal binding while the N-terminal domains (131-307) is involved in dyacylglycerol binding.

    Sequence similaritiesi

    Belongs to the glycosyltransferase 28 family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    InterProiIPR009695. Diacylglyc_glucosyltr_N.
    IPR007235. Glyco_trans_28_C.
    [Graphical view]
    PfamiPF04101. Glyco_tran_28_C. 1 hit.
    PF06925. MGDG_synth. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9SM44-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSHPSTVTSE PSNLLDFVPK LGNFVLNSSL HGNNSNGYSS FSSNSVHFGG
    60 70 80 90 100
    LATQNRYKFV NSLSFSKEGS NLKRILSDFN RVIRLHCDRI PLGFSSIGLN
    110 120 130 140 150
    SGESNGVSDN GHGVLEDVRV PVNAVEPESP KRVLILMSDT GGGHRASAEA
    160 170 180 190 200
    IKAAFNEEFG DDYQVFVTDL WSEHTPWPFN QLPRSYNFLV KHGPLWKMMY
    210 220 230 240 250
    YGTSPRVIHQ SNFAATSVFI AREVARGLMK YQPDIIISVH PLMQHVPLRI
    260 270 280 290 300
    LRGRGLLEKI VFTTVVTDLS TCHPTWFHKL VTRCYCPSNE VAKRATKAGL
    310 320 330 340 350
    QPSQIKVYGL PVRPSFVRSV RPKNELRKEL GMDEHLPAVL LMGGGEGMGP
    360 370 380 390 400
    IEATARALGN ALYDANLGEP TGQLLVICGR NKKLAGKLSS IDWKIPVQVK
    410 420 430 440 450
    GFVTKIEECM GACDCIITKA GPGTIAEAMI RGLPIILNDY IAGQEAGNVP
    460 470 480 490 500
    YVIENGIGKY LKSPKEIAKT VSQWFGPKAN ELQIMSQNAL KHARPDAVFK
    510 520
    IVHDLDELVR QKIFVRQYSC AA
    Length:522
    Mass (Da):57,511
    Last modified:May 1, 2000 - v1
    Checksum:i02E2B929732551A7
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ249607 mRNA. Translation: CAB56218.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AJ249607 mRNA. Translation: CAB56218.1.

    3D structure databases

    ProteinModelPortaliQ9SM44.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein family/group databases

    CAZyiGT28. Glycosyltransferase Family 28.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi2.4.1.46. 5812.

    Family and domain databases

    InterProiIPR009695. Diacylglyc_glucosyltr_N.
    IPR007235. Glyco_trans_28_C.
    [Graphical view]
    PfamiPF04101. Glyco_tran_28_C. 1 hit.
    PF06925. MGDG_synth. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    1. "Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG."
      Miege C., Marechal E., Shimojima M., Awai K., Block M.A., Ohta H., Takamiya K., Douce R., Joyard J.
      Eur. J. Biochem. 265:990-1001(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, SUBUNIT.
    2. "Kinetic properties of monogalactosyldiacylglycerol synthase from spinach chloroplast envelope membranes."
      Marechal E., Block M.A., Joyard J., Douce R.
      J. Biol. Chem. 269:5788-5798(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    3. "The catalytic site of monogalactosyldiacylglycerol synthase from spinach chloroplast envelope membranes. Biochemical analysis of the structure and of the metal content."
      Marechal E., Miege C., Block M.A., Douce R., Joyard J.
      J. Biol. Chem. 270:5714-5722(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, ENZYME REGULATION.
    4. "Molecular modeling and site-directed mutagenesis of plant chloroplast monogalactosyldiacylglycerol synthase reveal critical residues for activity."
      Botte C., Jeanneau C., Snajdrova L., Bastien O., Imberty A., Breton C., Marechal E.
      J. Biol. Chem. 280:34691-34701(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING, MUTAGENESIS OF TRP-171; GLU-173; TRP-177; HIS-240; HIS-245; CYS-284; CYS-286; 343-GLY--GLY-347; GLU-346; CYS-378; ARG-380; PHE-402; CYS-415; LYS-419; GLU-427; GLU-445 AND ASN-448.

    Entry informationi

    Entry nameiMGDG_SPIOL
    AccessioniPrimary (citable) accession number: Q9SM44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: May 1, 2000
    Last modified: January 7, 2015
    This is version 41 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.