PADGT_ACHLA
ID PADGT_ACHLA Reviewed; 332 AA.
AC Q8KQL6;
DT 19-FEB-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Processive diacylglycerol alpha-glucosyltransferase;
DE EC=2.4.1.208 {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160};
DE EC=2.4.1.337 {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160};
DE AltName: Full=Alpha-diglucosyldiacylglycerol synthase;
DE Short=Alpha-DGS;
DE Short=DGlcDAG synthase;
DE AltName: Full=Alpha-monoglucosyldiacylglycerol synthase;
DE Short=Alpha-MGS;
DE Short=MGlcDAG synthase;
DE AltName: Full=Glucosyl-alpha-1,2-glucosyldiacylglycerol synthase;
DE AltName: Full=UDP-glucose:1,2-diacylglycerol 3-alpha-D-glucosyltransferase;
GN Name=dgs;
OS Acholeplasma laidlawii.
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Acholeplasma.
OX NCBI_TaxID=2148;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-30, FUNCTION,
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY REGULATION.
RC STRAIN=A-EF22;
RX PubMed=12464611; DOI=10.1074/jbc.m211492200;
RA Edman M., Berg S., Storm P., Wikstrom M., Vikstrom S., Ohman A.,
RA Wieslander A.;
RT "Structural features of glycosyltransferases synthesizing major bilayer and
RT nonbilayer-prone membrane lipids in Acholeplasma laidlawii and
RT Streptococcus pneumoniae.";
RL J. Biol. Chem. 278:8420-8428(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ACTIVITY
RP REGULATION.
RC STRAIN=A-EF22;
RX PubMed=1533160; DOI=10.1016/0005-2736(92)90171-h;
RA Dahlqvist A., Andersson S., Wieslander A.;
RT "The enzymatic synthesis of membrane glucolipids in Acholeplasma
RT laidlawii.";
RL Biochim. Biophys. Acta 1105:131-140(1992).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND COFACTOR.
RC STRAIN=A-EF22;
RX PubMed=10220338; DOI=10.1021/bi982532m;
RA Vikstrom S., Li L., Karlsson O.P., Wieslander A.;
RT "Key role of the diglucosyldiacylglycerol synthase for the nonbilayer-
RT bilayer lipid balance of Acholeplasma laidlawii membranes.";
RL Biochemistry 38:5511-5520(1999).
CC -!- FUNCTION: Processive glucosyltransferase involved in the biosynthesis
CC of both the non-bilayer-prone alpha-monoglucosyldiacylglycerol and the
CC bilayer-forming membrane lipid alpha-diglucosyldiacylglycerol. These
CC are major components for maintaining the anionic lipid surface charge
CC density, for balancing the bilayer to non-bilayer phase equilibria and
CC for keeping a constant lipid bilayer spontaneous curvature (curvature
CC packing stress). Catalyzes the transfer of a glucosyl residue from UDP-
CC Glc to diacylglycerol (DAG) acceptor to form the corresponding alpha-
CC glucosyl-DAG (1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol),
CC which then acts as acceptor to give alpha-diglucosyl-DAG product (3-O-
CC (alpha-D-glucopyranosyl-alpha-(1->2)-D-glucopyranosyl)-1,2-diacyl-sn-
CC glycerol). It can only use UDP-Glc as sugar donor.
CC {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611,
CC ECO:0000269|PubMed:1533160}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycerol + UDP-alpha-D-glucose = a 1,2-diacyl-
CC 3-O-(alpha-D-glucopyranosyl)-sn-glycerol + H(+) + UDP;
CC Xref=Rhea:RHEA:47612, ChEBI:CHEBI:15378, ChEBI:CHEBI:17670,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC EC=2.4.1.337; Evidence={ECO:0000269|PubMed:10220338,
CC ECO:0000269|PubMed:12464611, ECO:0000269|PubMed:1533160};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol + UDP-
CC alpha-D-glucose = 1,2-diacyl-3-O-[alpha-D-glucosyl-(1-> 2)-alpha-D-
CC glucosyl]-sn-glycerol + H(+) + UDP; Xref=Rhea:RHEA:19165,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17670, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:76166; EC=2.4.1.208;
CC Evidence={ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611,
CC ECO:0000269|PubMed:1533160};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:10220338};
CC -!- ACTIVITY REGULATION: Activated by the negatively charged lipids
CC phosphatidylglycerol (PG), cardiolipin (CL), nonbilayer-prone 1,3-DAG,
CC 1,2-dioleoylphosphatidylglycerol (DOPG) and 1,2-
CC dioleoylphosphatidylserine (DOPS). Inhibited by 1,2-diacyl-3-O-(alpha-
CC D-galactopyranosyl)-sn-glycerol, 1,2-diacyl-3-O-[6-O-acyl(alpha-D-
CC glucopyranosyl)]-sn-glycerol and 1,2-diacyl-3-O-[alpha-D-
CC glucopyranosyl-(1->2)-O-(6-O-acyl-alpha-D-glucopyranosyl)]-sn-glycerol.
CC {ECO:0000269|PubMed:10220338, ECO:0000269|PubMed:12464611,
CC ECO:0000269|PubMed:1533160}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for UDP-Glc (alpha-diglucosyldiacylglycerol synthase
CC activity at 28 degrees Celsius) {ECO:0000269|PubMed:10220338};
CC Vmax=19 nmol/h/mg enzyme (alpha-diglucosyldiacylglycerol synthase
CC activity at 28 degrees Celsius) {ECO:0000269|PubMed:10220338};
CC -!- PATHWAY: Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12464611,
CC ECO:0000269|PubMed:1533160}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; AY078412; AAL83700.1; -; Genomic_DNA.
DR RefSeq; WP_012242482.1; NZ_VKID01000001.1.
DR AlphaFoldDB; Q8KQL6; -.
DR SMR; Q8KQL6; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR GeneID; 66293530; -.
DR OMA; GQVQERK; -.
DR BioCyc; MetaCyc:GI40-529-MON; -.
DR UniPathway; UPA00894; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047257; F:diglucosyl diacylglycerol synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0009246; P:enterobacterial common antigen biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0046467; P:membrane lipid biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cell membrane; Direct protein sequencing;
KW Glycerol metabolism; Glycosyltransferase; Lipid biosynthesis;
KW Lipid metabolism; Magnesium; Membrane; Transferase.
FT CHAIN 1..332
FT /note="Processive diacylglycerol alpha-glucosyltransferase"
FT /id="PRO_0000425274"
SQ 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
