OCTT_MYCHD
ID OCTT_MYCHD Reviewed; 240 AA.
AC K5BJH8;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 25-MAY-2022, entry version 39.
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 ORFNames=C731_2896 {ECO:0000312|EMBL:EKF23139.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
RX PubMed=23209251; DOI=10.1128/jb.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849;
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). Can also use hexanoyl-CoA
CC as acyl donor in vitro. DGG is the preferred acceptor, but to a lesser
CC extent, GG (glucosylglycerate) can be used as substrate. DGG and GG are
CC the two earliest intermediates in MGLP biosynthesis.
CC {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=9.5 mM for diglucosylglycerate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26324178};
CC KM=6.6 mM for glucosylglycerate (at 37 degrees Celsius)
CC {ECO:0000269|PubMed:26324178};
CC KM=0.06 mM for octanoyl-CoA (when DGG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC KM=0.01 uM for octanoyl-CoA (when GG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC KM=0.02 uM for hexanoyl-CoA (when DGG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC KM=0.01 uM for hexanoyl-CoA (when GG is used as cosubstrate, at 37
CC degrees Celsius) {ECO:0000269|PubMed:26324178};
CC Vmax=134 nmol/min/mg enzyme with diglucosylglycerate and octanoyl-CoA
CC as substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178};
CC Vmax=32 nmol/min/mg enzyme with glucosylglycerate and octanoyl-CoA as
CC substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178};
CC Vmax=41 nmol/min/mg enzyme with diglucosylglycerate and hexanoyl-CoA
CC as substrates (at 37 degrees Celsius) {ECO:0000269|PubMed:26324178};
CC pH dependence:
CC Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:26324178};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. Activity sharply decreases
CC above this temperature. {ECO:0000269|PubMed:26324178};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:26324178}.
CC -!- SIMILARITY: Belongs to the OctT acyltransferase family. {ECO:0000305}.
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DR EMBL; AMRA01000080; EKF23139.1; -; Genomic_DNA.
DR AlphaFoldDB; K5BJH8; -.
DR STRING; 1122247.C731_2896; -.
DR EnsemblBacteria; EKF23139; EKF23139; C731_2896.
DR PATRIC; fig|1122247.3.peg.2780; -.
DR eggNOG; COG2755; Bacteria.
DR OMA; IMSGRGN; -.
DR BRENDA; 2.3.1.273; 15810.
DR SABIO-RK; K5BJH8; -.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR GO; GO:0016414; F:O-octanoyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IDA:UniProtKB.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..240
FT /note="Diglucosylglycerate octanoyltransferase"
FT /id="PRO_0000436911"
SQ SEQUENCE 240 AA; 26579 MW; 415157E0571C13CF CRC64;
MSGRRPTLLV FCDSLSYYGP RGGLPADDPR IWPNIVASQL DWDVELIGRV GWTSRDVWWA
ATQDPRAWAA LPRAGAVIFA TGGMDSLPSP LPTALRELIR YIRPPWLRRR VRDLYGWLQP
RLSPVSRNAL PPHLTAEYLE MTRGAIDFNR PGIPVVAALP SVHIADSYGR AHHGREATAR
AITEWARQHG VVLVDLKAAV ADQVLNGRGN PDGIHWNFEA HQAVAELMLK ALAEAGVPCR
