OCTT_MYCS2
ID OCTT_MYCS2 Reviewed; 252 AA.
AC A0R109;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Diglucosylglycerate octanoyltransferase {ECO:0000303|PubMed:26324178};
DE Short=DGG octanoyltransferase {ECO:0000303|PubMed:26324178};
DE EC=2.3.1.273 {ECO:0000269|PubMed:26324178};
GN Name=octT {ECO:0000303|PubMed:26324178};
GN OrderedLocusNames=MSMEG_4578 {ECO:0000312|EMBL:ABK73636.1},
GN MSMEI_4466 {ECO:0000312|EMBL:AFP40920.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=26324178; DOI=10.1038/srep13610;
RA Maranha A., Moynihan P.J., Miranda V., Correia Lourenco E., Nunes-Costa D.,
RA Fraga J.S., Jose Barbosa Pereira P., Macedo-Ribeiro S., Ventura M.R.,
RA Clarke A.J., Empadinhas N.;
RT "Octanoylation of early intermediates of mycobacterial methylglucose
RT lipopolysaccharides.";
RL Sci. Rep. 5:13610-13610(2015).
CC -!- FUNCTION: Sugar octanoyltransferase likely involved in the biosynthesis
CC of mycobacterial methylglucose lipopolysaccharide (MGLP). Catalyzes the
CC transfer of an octanoyl group from octanoyl-CoA to the C6 OH of the
CC second glucose in diglucosylglycerate (DGG). DGG is the preferred
CC acceptor, but to a lesser extent, GG (glucosylglycerate) can also be
CC used as substrate. DGG and GG are the two earliest intermediates in
CC MGLP biosynthesis. {ECO:0000269|PubMed:26324178}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-O-[alpha-D-glucopyranosyl-(1->6)-alpha-D-
CC glucopyranosyl]-glycerate + octanoyl-CoA = (2R)-2-O-[6-O-octanoyl-
CC alpha-D-glucopyranosyl-(1->6)-alpha-D-glucopyranosyl]-glycerate +
CC CoA; Xref=Rhea:RHEA:56868, ChEBI:CHEBI:57287, ChEBI:CHEBI:57386,
CC ChEBI:CHEBI:141056, ChEBI:CHEBI:141058; EC=2.3.1.273;
CC Evidence={ECO:0000269|PubMed:26324178};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.0 mM for diglucosylglycerate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26324178};
CC KM=19.0 mM for glucosylglycerate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26324178};
CC KM=0.03 mM for octanoyl-CoA (when DGG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC KM=0.02 uM for octanoyl-CoA (when GG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC Vmax=1939 nmol/min/mg enzyme with diglucosylglycerate and octanoyl-
CC CoA as substrates (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26324178};
CC Vmax=20 nmol/min/mg enzyme with glucosylglycerate and octanoyl-CoA as
CC substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26324178}.
CC -!- SIMILARITY: Belongs to the OctT acyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000480; ABK73636.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40920.1; -; Genomic_DNA.
DR RefSeq; WP_011729938.1; NZ_SIJM01000004.1.
DR RefSeq; YP_888847.1; NC_008596.1.
DR AlphaFoldDB; A0R109; -.
DR STRING; 246196.MSMEI_4466; -.
DR PRIDE; A0R109; -.
DR EnsemblBacteria; ABK73636; ABK73636; MSMEG_4578.
DR EnsemblBacteria; AFP40920; AFP40920; MSMEI_4466.
DR GeneID; 66735905; -.
DR KEGG; msg:MSMEI_4466; -.
DR KEGG; msm:MSMEG_4578; -.
DR PATRIC; fig|246196.19.peg.4481; -.
DR eggNOG; COG2755; Bacteria.
DR OMA; IMSGRGN; -.
DR OrthoDB; 1248190at2; -.
DR BRENDA; 2.3.1.273; 3512.
DR SABIO-RK; A0R109; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; Chromosome.
DR GO; GO:0016414; F:O-octanoyltransferase activity; IDA:UniProtKB.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR036514; SGNH_hydro_sf.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..252
FT /note="Diglucosylglycerate octanoyltransferase"
FT /id="PRO_0000436912"
SQ SEQUENCE 252 AA; 27762 MW; 87247413D1175822 CRC64;
MSSETSSEST GHRPVLLVFA DSLSYFGPTG GLPADDPRIW PNIVGEQLGW DVELIGRIGW
TCRDVWWAAT QDPRSWAALP RAGAVVFATS GMDSLPSPLP TALREMIRYV RPPWLRRWVR
DGYGWVQPRL SPIARSALPP HVTVEYLEMT RNAIDFNRPG IPVVASLPSV HIAETYGRAH
HGREPTVRAI TAWAEEHHVP LVDLKAAVAD EVFGGRGNPD GIHWSFEAHR AVAELMLKGL
AEAGVTQRDS AT
