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Q9SM44

- MGDG_SPIOL

UniProt

Q9SM44 - MGDG_SPIOL

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Protein

Monogalactosyldiacylglycerol synthase, chloroplastic

Gene

MGD A

Organism
Spinacia oleracea (Spinach)
Status
Reviewed - 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

  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
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

Plastidchloroplast inner membrane 1 Publication

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. plastid inner membrane Source: UniProtKB-KW
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

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: November 26, 2014
This is version 40 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