RNTF_MYCTO
ID RNTF_MYCTO Reviewed; 449 AA.
AC P9WN08; L0TBE0; P95130; Q50455; Q50456; Q7D6C8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=PGL/p-HBAD biosynthesis rhamnosyltransferase;
DE EC=2.4.1.-;
GN OrderedLocusNames=MT3038;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Catalyzes the transfer of the first rhamnosyl residue on p-
CC hydroxybenzoic acid or phenolphthiocerol derivatives to form, after O-
CC methylation at position 2 of the sugar unit, mono-O-methyl-glycosyl-p-
CC hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-
CC phenolphthiocerol dimycocerosate (also called mycoside B) during p-
CC hydroxybenzoic acid derivatives (p-HBAD) and glycosylated
CC phenolphthiocerol dimycocerosates (PGL) biosynthesis. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {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; AE000516; AAK47364.1; -; Genomic_DNA.
DR PIR; G70670; G70670.
DR RefSeq; WP_003414922.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WN08; -.
DR SMR; P9WN08; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblBacteria; AAK47364; AAK47364; MT3038.
DR KEGG; mtc:MT3038; -.
DR PATRIC; fig|83331.31.peg.3279; -.
DR HOGENOM; CLU_692271_0_0_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF00201; UDPGT; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..449
FT /note="PGL/p-HBAD biosynthesis rhamnosyltransferase"
FT /id="PRO_0000427209"
SQ SEQUENCE 449 AA; 49433 MW; 205FDB0855C0A109 CRC64;
MRVSCVYATA SRWGGPPVAS EVRGDAAIST TPDAAPGLAA RRRRILFVAE AVTLAHVVRP
FALAQSLDPS RYEVHFACDP RYNQLLGPLP FRHHAIHTIP SERFFGNLTQ GRFYAMRTLR
KYVEADLRVL DEIAPDLVVG DLRISLSVSA RLAGIPYIAI ANAYWSPYAQ RRFPLPDVIW
TRLFGVRLVK LLYRLERPLL FALQCMPLNW VRRRHGLSSL GWNLCRIFTD GDHTLYADVP
ELMPTYDLPA NHEYLGPVLW SPAGKPPTWW DSLPTDRPIV YATLGTSGGR NLLQLVLNAL
AELPVTVIAA TAGRSDLKTV PANAFVADYL PGEAAAARSA VVVCNGGSLT TQQALVAGVP
VIGVAGNLDQ HLNMEAVERA GAGVLLRTER LKSQRVAGAV MQVISRSEYR QAAARLADAF
GRDRVGFPQH VENALRLMPE NRPRTWLAS