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Q9SM44

- MGDG_SPIOL

UniProt

Q9SM44 - MGDG_SPIOL

Protein

Monogalactosyldiacylglycerol synthase, chloroplastic

Gene

MGD A

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 38 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    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

    Zinc.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

    1. 1,2-diacylglycerol 3-beta-galactosyltransferase activity Source: UniProtKB-EC
    2. carbohydrate binding Source: InterPro

    GO - Biological processi

    1. glycolipid biosynthetic process Source: InterPro
    2. lipid glycosylation Source: InterPro

    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

    Plastidchloroplast inner membrane 1 Publication

    GO - Cellular componenti

    1. chloroplast inner membrane Source: UniProtKB-SubCell

    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.
    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

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    MSHPSTVTSE PSNLLDFVPK LGNFVLNSSL HGNNSNGYSS FSSNSVHFGG    50
    LATQNRYKFV NSLSFSKEGS NLKRILSDFN RVIRLHCDRI PLGFSSIGLN 100
    SGESNGVSDN GHGVLEDVRV PVNAVEPESP KRVLILMSDT GGGHRASAEA 150
    IKAAFNEEFG DDYQVFVTDL WSEHTPWPFN QLPRSYNFLV KHGPLWKMMY 200
    YGTSPRVIHQ SNFAATSVFI AREVARGLMK YQPDIIISVH PLMQHVPLRI 250
    LRGRGLLEKI VFTTVVTDLS TCHPTWFHKL VTRCYCPSNE VAKRATKAGL 300
    QPSQIKVYGL PVRPSFVRSV RPKNELRKEL GMDEHLPAVL LMGGGEGMGP 350
    IEATARALGN ALYDANLGEP TGQLLVICGR NKKLAGKLSS IDWKIPVQVK 400
    GFVTKIEECM GACDCIITKA GPGTIAEAMI RGLPIILNDY IAGQEAGNVP 450
    YVIENGIGKY LKSPKEIAKT VSQWFGPKAN ELQIMSQNAL KHARPDAVFK 500
    IVHDLDELVR QKIFVRQYSC AA 522
    Length:522
    Mass (Da):57,511
    Last modified:May 1, 2000 - v1
    Checksum:i02E2B929732551A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249607 mRNA. Translation: CAB56218.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249607 mRNA. Translation: CAB56218.1 .

    3D structure databases

    ProteinModelPortali Q9SM44.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GT28. Glycosyltransferase Family 28.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 2.4.1.46. 5812.

    Family and domain databases

    InterProi IPR009695. Diacylglyc_glucosyltr_N.
    IPR007235. Glyco_trans_28_C.
    [Graphical view ]
    Pfami PF04101. Glyco_tran_28_C. 1 hit.
    PF06925. MGDG_synth. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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: October 1, 2014
    This is version 38 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