GTFD_AMYOR
ID GTFD_AMYOR Reviewed; 408 AA.
AC Q9AFC7;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Devancosaminyl-vancomycin vancosaminetransferase;
DE EC=2.4.1.322;
DE AltName: Full=Devancosamine-vancomycin TDP-vancosaminyltransferase;
DE AltName: Full=Glycosyltransferase GtfD;
GN Name=gtfD;
OS Amycolatopsis orientalis (Nocardia orientalis).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Amycolatopsis.
OX NCBI_TaxID=31958;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 19795 / DSM 40040 / CBS 547.68 / JCM 4235 / KCTC 9412 / NBRC
RC 12806 / NCIMB 12945 / M43-05865;
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 [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH DTDP;
RP DEVANCOAMINYL-VANCOMYCIN AND BETA-D-GLUCOSE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF THR-10 AND ASP-13.
RX PubMed=15122882; DOI=10.1021/bi036130c;
RA Mulichak A.M., Lu W., Losey H.C., Walsh C.T., Garavito R.M.;
RT "Crystal structure of vancosaminyltransferase GtfD from the vancomycin
RT biosynthetic pathway: interactions with acceptor and nucleotide ligands.";
RL Biochemistry 43:5170-5180(2004).
CC -!- FUNCTION: Catalyzes the attachment of L-vancosamine to a
CC monoglucosylated heptapeptide intermediate during the final stage of
CC glycopeptide antibiotic vancomycin biosynthesis.
CC {ECO:0000269|PubMed:11294642, ECO:0000269|PubMed:15122882}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=devancoaminyl-vancomycin + dTDP-beta-L-vancosamine = dTDP +
CC H(+) + vancomycin; Xref=Rhea:RHEA:39891, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:58369, ChEBI:CHEBI:75953, ChEBI:CHEBI:76839,
CC ChEBI:CHEBI:76842; EC=2.4.1.322;
CC Evidence={ECO:0000269|PubMed:15122882};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16.3 uM for devancoaminyl-vancomycin
CC {ECO:0000269|PubMed:15122882};
CC KM=2.0 mM for UDP-L-epivancosamine {ECO:0000269|PubMed:15122882};
CC Note=kcat is 67.6 min (-1).;
CC -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC {ECO:0000269|PubMed:11294642}.
CC -!- MISCELLANEOUS: In A.orientalis different glycosyltransferases are
CC involved in biosynthesis of the vancomycin group of antibiotics. GtfA
CC (AC P96558), GtfB (AC P96559) and GtfC (AC P96560) are involved in
CC biosynthesis of antibiotic chloroeremomycin, while GtfD 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; AF351621; AAK31352.1; -; Genomic_DNA.
DR PDB; 1RRV; X-ray; 2.00 A; A/B=1-408.
DR PDBsum; 1RRV; -.
DR AlphaFoldDB; Q9AFC7; -.
DR SMR; Q9AFC7; -.
DR STRING; 1125971.ASJB01000062_gene4403; -.
DR DrugBank; DB04529; Desvancosaminyl vancomycin.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR KEGG; ag:AAK31352; -.
DR eggNOG; COG1819; Bacteria.
DR BioCyc; MetaCyc:MON-18443; -.
DR BRENDA; 2.4.1.322; 315.
DR UniPathway; UPA00162; -.
DR EvolutionaryTrace; Q9AFC7; -.
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..408
FT /note="Devancosaminyl-vancomycin vancosaminetransferase"
FT /id="PRO_0000430439"
FT BINDING 10..12
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 13
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 76
FT /ligand="devancoaminyl-vancomycin"
FT /ligand_id="ChEBI:CHEBI:75953"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 80
FT /ligand="devancoaminyl-vancomycin"
FT /ligand_id="ChEBI:CHEBI:75953"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 103
FT /ligand="beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:15903"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 246
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 293..296
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:15122882"
FT BINDING 309..314
FT /ligand="dTDP"
FT /ligand_id="ChEBI:CHEBI:58369"
FT /evidence="ECO:0000269|PubMed:15122882"
FT MUTAGEN 10
FT /note="T->A: Strongly decreased activity."
FT /evidence="ECO:0000269|PubMed:15122882"
FT MUTAGEN 13
FT /note="D->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:15122882"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 40..46
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 70..91
FT /evidence="ECO:0007829|PDB:1RRV"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 104..117
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 151..176
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1RRV"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 227..234
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 270..273
FT /evidence="ECO:0007829|PDB:1RRV"
FT TURN 275..278
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 334..343
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1RRV"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 357..367
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 370..379
FT /evidence="ECO:0007829|PDB:1RRV"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:1RRV"
FT HELIX 387..400
FT /evidence="ECO:0007829|PDB:1RRV"
SQ SEQUENCE 408 AA; 42881 MW; 1233D71CD99D1FBD CRC64;
MRVLLSVCGT RGDVEIGVAL ADRLKALGVQ TRMCAPPAAE ERLAEVGVPH VPVGLPQHMM
LQEGMPPPPP EEEQRLAAMT VEMQFDAVPG AAEGCAAVVA VGDLAAATGV RSVAEKLGLP
FFYSVPSPVY LASPHLPPAY DEPTTPGVTD IRVLWEERAA RFADRYGPTL NRRRAEIGLP
PVEDVFGYGH GERPCWPADP VLAPLQPDVD AVQTGAWLLS DERPLPPELE AFLAAGSPPV
HIGFGSSSGR GIADAAKVAV EAIRAQGRRV ILSRGWTELV LPDDRDDCFA IDEVNFQALF
RRVAAVIHHG SAGTEHVATR AGVPQLVIPR NTDQPYFAGR VAALGIGVAH DGPTPTFESL
SAALTTVLAP ETRARAEAVA GMVLTDGAAA AADLVLAAVG REKPAVPA
