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 10-JUN-2026, entry version 92. 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; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales; OC Pseudonocardiaceae; 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=vancomycin aglycone + UDP-alpha-D-glucose = 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}. 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; 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 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:0033072; P:vancomycin biosynthetic process; IDA:UniProtKB. DR CDD; cd03784; GT1_Gtf-like; 1. DR FunFam; 3.40.50.2000:FF:000292; Glycosyltransferase GtfE; 1. DR FunFam; 3.40.50.2000:FF:000009; Sterol 3-beta-glucosyltransferase UGT80A2; 1. DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2. DR InterPro; IPR010610; EryCIII-like_C. DR InterPro; IPR050426; Glycosyltransferase_28. DR InterPro; IPR004276; GlycoTrans_28_N. DR InterPro; IPR002213; UDP_glucos_trans. DR PANTHER; PTHR48050; STEROL 3-BETA-GLUCOSYLTRANSFERASE; 1. DR PANTHER; PTHR48050:SF13; STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2; 1. DR Pfam; PF06722; EryCIII-like_C; 1. DR Pfam; PF03033; Glyco_transf_28; 1. DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1. DR PDBsum; 1IIR; -. 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..162 FT /evidence="ECO:0007829|PDB:1IIR" FT HELIX 163..167 FT /evidence="ECO:0007829|PDB:1IIR" FT HELIX 168..176 FT /evidence="ECO:0007829|PDB:1IIR" FT HELIX 180..182 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 204..207 FT /evidence="ECO:0007829|PDB:1IIR" FT HELIX 220..222 FT /evidence="ECO:0007829|PDB:1IIR" FT HELIX 224..227 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..343 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 //