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Processive diacylglycerol alpha-glucosyltransferase (EC 2.4.1.208) (EC 2.4.1.337) (Alpha-diglucosyldiacylglycerol synthase) (Alpha-DGS) (DGlcDAG synthase) (Alpha-monoglucosyldiacylglycerol synthase) (Alpha-MGS) (MGlcDAG synthase) (Glucosyl-alpha-1,2-glucosyldiacylglycerol synthase) (UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase)

 PADGT_ACHLA             Reviewed;         332 AA.
Q8KQL6;
19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
22-NOV-2017, entry version 43.
RecName: Full=Processive diacylglycerol alpha-glucosyltransferase;
EC=2.4.1.208 {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160};
EC=2.4.1.337 {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160};
AltName: Full=Alpha-diglucosyldiacylglycerol synthase;
Short=Alpha-DGS;
Short=DGlcDAG synthase;
AltName: Full=Alpha-monoglucosyldiacylglycerol synthase;
Short=Alpha-MGS;
Short=MGlcDAG synthase;
AltName: Full=Glucosyl-alpha-1,2-glucosyldiacylglycerol synthase;
AltName: Full=UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase;
Name=dgs;
Acholeplasma laidlawii.
Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
Acholeplasmataceae; Acholeplasma.
NCBI_TaxID=2148;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION,
CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
STRAIN=A-EF22;
PubMed=12464611; DOI=10.1074/jbc.M211492200;
Edman M., Berg S., Storm P., Wikstrom M., Vikstrom S., Ohman A.,
Wieslander A.;
"Structural features of glycosyltransferases synthesizing major
bilayer and nonbilayer-prone membrane lipids in Acholeplasma laidlawii
and Streptococcus pneumoniae.";
J. Biol. Chem. 278:8420-8428(2003).
[2]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
STRAIN=A-EF22;
PubMed=1533160; DOI=10.1016/0005-2736(92)90171-H;
Dahlqvist A., Andersson S., Wieslander A.;
"The enzymatic synthesis of membrane glucolipids in Acholeplasma
laidlawii.";
Biochim. Biophys. Acta 1105:131-140(1992).
[3]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL
PROPERTIES, AND COFACTOR.
STRAIN=A-EF22;
PubMed=10220338; DOI=10.1021/bi982532m;
Vikstrom S., Li L., Karlsson O.P., Wieslander A.;
"Key role of the diglucosyldiacylglycerol synthase for the nonbilayer-
bilayer lipid balance of Acholeplasma laidlawii membranes.";
Biochemistry 38:5511-5520(1999).
-!- FUNCTION: Processive glucosyltransferase involved in the
biosynthesis of both the non-bilayer-prone alpha-
monoglucosyldiacylglycerol and the bilayer-forming membrane lipid
alpha-diglucosyldiacylglycerol. These are major components for
maintaining the anionic lipid surface charge density, for
balancing the bilayer to non-bilayer phase equilibria and for
keeping a constant lipid bilayer spontaneous curvature (curvature
packing stress). Catalyzes the transfer of a glucosyl residue from
UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding
alpha-glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-
glycerol), which then acts as acceptor to give alpha-diglucosyl-
DAG product (3-O-(alpha-D-glucopyranosyl-alpha-(1->2)-D-
glucopyranosyl)-1,2-diacyl-sn-glycerol). It can only use UDP-Glc
as sugar donor. {ECO:0000269|PubMed:10220338,
ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + a 1,2-diacyl-sn-glycerol
= UDP + a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol.
{ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611,
ECO:0000269|PubMed:1533160}.
-!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose + 1,2-diacyl-3-O-(alpha-D-
glucopyranosyl)-sn-glycerol = 1,2-diacyl-3-O-(alpha-D-
glucopyranosyl-(1->2)-O-alpha-D-glucopyranosyl)-sn-glycerol + UDP.
{ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611,
ECO:0000269|PubMed:1533160}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:10220338};
-!- ENZYME REGULATION: Activated by the negatively charged lipids
phosphatidylglycerol (PG), cardiolipin (CL), nonbilayer-prone 1,3-
DAG, 1,2-dioleoylphosphatidylglycerol (DOPG) and 1,2-
dioleoylphosphatidylserine (DOPS). Inhibited by 1,2-diacyl-3-O-
(alpha-D-galactopyranosyl)-sn-glycerol, 1,2-diacyl-3-O-[6-O-
acyl(alpha-D-glucopyranosyl)]-sn-glycerol and 1,2-diacyl-3-O-
[alpha-D-glucopyranosyl-(1->2)-O-(6-O-acyl-alpha-D-
glucopyranosyl)]-sn-glycerol. {ECO:0000269|PubMed:10220338,
ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.14 mM for UDP-Glc (alpha-diglucosyldiacylglycerol synthase
activity at 28 degrees Celsius) {ECO:0000269|PubMed:10220338};
Vmax=19 nmol/h/mg enzyme (alpha-diglucosyldiacylglycerol
synthase activity at 28 degrees Celsius)
{ECO:0000269|PubMed:10220338};
-!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol
biosynthesis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12464611,
ECO:0000269|PubMed:1533160}.
-!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
Glycosyltransferase 4 subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AY078412; AAL83700.1; -; Genomic_DNA.
RefSeq; WP_012242482.1; NZ_NELN01000002.1.
ProteinModelPortal; Q8KQL6; -.
CAZy; GT4; Glycosyltransferase Family 4.
eggNOG; ENOG4105W2C; Bacteria.
eggNOG; COG0438; LUCA.
BioCyc; MetaCyc:GI40-529-MONOMER; -.
UniPathway; UPA00894; -.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0047257; F:diglucosyl diacylglycerol synthase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
InterPro; IPR001296; Glyco_trans_1.
InterPro; IPR028098; Glyco_trans_4-like_N.
Pfam; PF13439; Glyco_transf_4; 1.
Pfam; PF00534; Glycos_transf_1; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell membrane; Direct protein sequencing;
Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis;
Lipid metabolism; Magnesium; Membrane; Transferase.
CHAIN 1 332 Processive diacylglycerol alpha-
glucosyltransferase.
/FTId=PRO_0000425274.
SEQUENCE 332 AA; 38447 MW; 89D874EEF79E6793 CRC64;
MKVLLYSQKQ SMLKKSGIGR AFYHQKRALE AVGIEYTTDP KDTYDLVHVN IAHSNKIKKF
RKKYPVIVHG HSTVQDFRRS FAFWRVIAPF FYKHLQNIYG IADLIITPTR YSKFLIESMH
VVKSPVVALS NGIDLDAYEY KQENVDAFRK HFDLEPNQKV VIGVGLLFER KGIHDFIEVA
RTMPNVTFIW FGNLSKLATT HFIRKRIKNK PKNMIMPGYV DGAVIKGAFS GADCVFFPSY
EETEGIVVLE GLASKTPVVL RDIPVYYDWL FHKEHVLKGH NNFEFSKLIE KVLHEDQTEM
IENGYKIVQD RSIEKIGEGL KQAYQEVIKI KR


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