GTFB_AMYOR
ID GTFB_AMYOR Reviewed; 407 AA.
AC P96559;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Vancomycin aglycone glucosyltransferase;
DE EC=2.4.1.310;
DE AltName: Full=Glycosyltransferase GtfB;
GN Name=gtfB;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9115410; DOI=10.1016/s1074-5521(97)90288-x;
RA Solenberg P.J., Matsushima P., Stack D.R., Wilkie S.C., Thompson R.C.,
RA Baltz R.H.;
RT "Production of hybrid glycopeptide antibiotics in vitro and in Streptomyces
RT toyocaensis.";
RL Chem. Biol. 4:195-202(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RX PubMed=9545426; DOI=10.1016/s1074-5521(98)90060-6;
RA van Wageningen A., Kirkpatrick P., Williams D., Harris B., Kershaw J.,
RA Lennard N., Jones M., Jones S., Solenberg P.;
RT "Sequencing and analysis of genes involved in the biosynthesis of a
RT vancomycin group antibiotic.";
RL Chem. Biol. 5:155-162(1998).
RN [3]
RP FUNCTION.
RX PubMed=11294642; DOI=10.1021/bi010050w;
RA Losey H.C., Peczuh M.W., Chen Z., Eggert U.S., Dong S.D., Pelczer I.,
RA Kahne D., Walsh C.T.;
RT "Tandem action of glycosyltransferases in the maturation of vancomycin and
RT teicoplanin aglycones: novel glycopeptides.";
RL Biochemistry 40:4745-4755(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-13; HIS-125 AND
RP ASP-332.
RX PubMed=11470430; DOI=10.1016/s0969-2126(01)00616-5;
RA Mulichak A.M., Losey H.C., Walsh C.T., Garavito R.M.;
RT "Structure of the UDP-glucosyltransferase GtfB that modifies the
RT heptapeptide aglycone in the biosynthesis of vancomycin group
RT antibiotics.";
RL Structure 9:547-557(2001).
CC -!- FUNCTION: Glucosyltransferase that transfers glucose to the 4-OH-
CC Phegly(4) residue of vancomycin aglycone (AGV) to produce
CC devancoaminyl-vancomycin (DVV) in the biosynthesis of glycopeptide
CC antibiotic chloroeremomycin, a member of the vancomycin group of
CC antibiotics. {ECO:0000269|PubMed:11294642, ECO:0000269|PubMed:9115410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=UDP-alpha-D-glucose + vancomycin aglycone = devancoaminyl-
CC vancomycin + UDP; Xref=Rhea:RHEA:38587, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:75953, ChEBI:CHEBI:77981;
CC EC=2.4.1.310; Evidence={ECO:0000269|PubMed:11470430};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.3 mM for UDP-glucose {ECO:0000269|PubMed:11470430};
CC Note=kcat is 33 min(-1).;
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC {ECO:0000269|PubMed:9545426}.
CC -!- MISCELLANEOUS: In A.orientalis different glycosyltransferases are
CC involved in biosynthesis of the vancomycin group of antibiotics. GtfA
CC (AC P96558), GtfB and GtfC (AC P96560) are involved in biosynthesis of
CC antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE (AC
CC G4V4R9) are involved in biosynthesis of vancomycin.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; U84349; AAB49293.1; -; Genomic_DNA.
DR EMBL; AJ223998; CAA11775.1; -; Genomic_DNA.
DR PIR; T30585; T30585.
DR PDB; 1IIR; X-ray; 1.80 A; A=1-407.
DR PDBsum; 1IIR; -.
DR AlphaFoldDB; P96559; -.
DR SMR; P96559; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:CAA11775; -.
DR BRENDA; 2.4.1.310; 315.
DR UniPathway; UPA00162; -.
DR EvolutionaryTrace; P96559; -.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0030259; P:lipid glycosylation; IEA:InterPro.
DR GO; GO:0033072; P:vancomycin biosynthetic process; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR004276; GlycoTrans_28_N.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF03033; Glyco_transf_28; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Glycosyltransferase; Transferase.
FT CHAIN 1..407
FT /note="Vancomycin aglycone glucosyltransferase"
FT /id="PRO_0000430437"
FT MUTAGEN 13
FT /note="D->A: Decreased kcat, while it does not affect the
FT KM for UDP-glucose."
FT /evidence="ECO:0000269|PubMed:11470430"
FT MUTAGEN 125
FT /note="H->A: No decrease in catalytic rate."
FT /evidence="ECO:0000269|PubMed:11470430"
FT MUTAGEN 332
FT /note="D->A: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:11470430"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 69..90
FT /evidence="ECO:0007829|PDB:1IIR"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 150..176
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:1IIR"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 241..244
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 252..264
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 295..298
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 302..307
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 345..348
FT /evidence="ECO:0007829|PDB:1IIR"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 356..366
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:1IIR"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:1IIR"
SQ SEQUENCE 407 AA; 42666 MW; DDCC0CF29A311201 CRC64;
MRVLLATCGS RGDTEPLVAL AVRVRDLGAD VRMCAPPDCA ERLAEVGVPH VPVGPSARAP
IQRAKPLTAE DVRRFTTEAI ATQFDEIPAA AEGCAAVVTT GLLAAAIGVR SVAEKLGIPY
FYAFHCPSYV PSPYYPPPPL GEPSTQDTID IPAQWERNNQ SAYQRYGGLL NSHRDAIGLP
PVEDIFTFGY TDHPWVAADP VLAPLQPTDL DAVQTGAWIL PDERPLSPEL AAFLDAGPPP
VYLGFGSLGA PADAVRVAID AIRAHGRRVI LSRGWADLVL PDDGADCFAI GEVNHQVLFG
RVAAVIHHGG AGTTHVAARA GAPQILLPQM ADQPYYAGRV AELGVGVAHD GPIPTFDSLS
AALATALTPE THARATAVAG TIRTDGAAVA ARLLLDAVSR EKPTVSA
