ERYC3_SACEN
ID ERYC3_SACEN Reviewed; 421 AA.
AC A4F7P3; O33935; O54224;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=3-alpha-mycarosylerythronolide B desosaminyl transferase;
DE EC=2.4.1.278;
DE AltName: Full=Desosaminyl transferase EryCIII;
DE AltName: Full=Erythromycin biosynthesis protein CIII;
DE Flags: Precursor;
GN Name=eryCIII; OrderedLocusNames=SACE_0726;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=9353926; DOI=10.1099/00221287-143-10-3251;
RA Summers R.G., Donadio S., Staver M.J., Wendt-Pienkowski E.,
RA Hutchinson C.R., Katz L.;
RT "Sequencing and mutagenesis of genes from the erythromycin biosynthetic
RT gene cluster of Saccharopolyspora erythraea that are involved in L-mycarose
RT and D-desosamine production.";
RL Microbiology 143:3251-3262(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=9563840; DOI=10.1007/s004380050680;
RA Salah-Bey K., Doumith M., Michel J.M., Haydock S., Cortes J., Leadlay P.F.,
RA Raynal M.C.;
RT "Targeted gene inactivation for the elucidation of deoxysugar biosynthesis
RT in the erythromycin producer Saccharopolyspora erythraea.";
RL Mol. Gen. Genet. 257:542-553(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=15303858; DOI=10.1021/ja048836f;
RA Lee H.Y., Chung H.S., Hang C., Khosla C., Walsh C.T., Kahne D., Walker S.;
RT "Reconstitution and characterization of a new desosaminyl transferase,
RT EryCIII, from the erythromycin biosynthetic pathway.";
RL J. Am. Chem. Soc. 126:9924-9925(2004).
RN [5]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=16218575; DOI=10.1021/ja053704n;
RA Yuan Y., Chung H.S., Leimkuhler C., Walsh C.T., Kahne D., Walker S.;
RT "In vitro reconstitution of EryCIII activity for the preparation of
RT unnatural macrolides.";
RL J. Am. Chem. Soc. 127:14128-14129(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) IN COMPLEX WITH ERYCII, AND SUBUNIT.
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=22056329; DOI=10.1016/j.jmb.2011.10.036;
RA Moncrieffe M.C., Fernandez M.J., Spiteller D., Matsumura H., Gay N.J.,
RA Luisi B.F., Leadlay P.F.;
RT "Structure of the glycosyltransferase EryCIII in complex with its
RT activating P450 homologue EryCII.";
RL J. Mol. Biol. 415:92-101(2012).
CC -!- FUNCTION: Catalyzes the conversion of alpha-L-mycarosylerythronolide B
CC into erythromycin D in the erythromycin biosynthesis pathway.
CC {ECO:0000269|PubMed:15303858}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-alpha-L-mycarosylerythronolide B + dTDP-alpha-D-desosamine
CC = dTDP + erythromycin D + H(+); Xref=Rhea:RHEA:32091,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28343, ChEBI:CHEBI:58369,
CC ChEBI:CHEBI:63260, ChEBI:CHEBI:63677; EC=2.4.1.278;
CC Evidence={ECO:0000269|PubMed:15303858};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for 3-alpha-mycarosylerythronolide B
CC {ECO:0000269|PubMed:16218575};
CC Note=kcat is 1 min(-1).;
CC -!- PATHWAY: Antibiotic biosynthesis; erythromycin biosynthesis.
CC {ECO:0000269|PubMed:15303858}.
CC -!- SUBUNIT: Heterotetramer composed of EryCII and EryCIII.
CC {ECO:0000269|PubMed:22056329}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC {ECO:0000305}.
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DR EMBL; U77454; AAB84067.1; -; Genomic_DNA.
DR EMBL; Y14332; CAA74710.1; -; Genomic_DNA.
DR EMBL; AM420293; CAM00067.1; -; Genomic_DNA.
DR RefSeq; WP_009950402.1; NZ_PDBV01000001.1.
DR PDB; 2YJN; X-ray; 3.09 A; A=1-421.
DR PDBsum; 2YJN; -.
DR AlphaFoldDB; A4F7P3; -.
DR SMR; A4F7P3; -.
DR STRING; 405948.SACE_0726; -.
DR CAZy; GT1; Glycosyltransferase Family 1.
DR EnsemblBacteria; CAM00067; CAM00067; SACE_0726.
DR KEGG; sen:SACE_0726; -.
DR eggNOG; COG1819; Bacteria.
DR HOGENOM; CLU_000537_7_4_11; -.
DR OMA; AHNTHYY; -.
DR OrthoDB; 1485440at2; -.
DR BioCyc; MetaCyc:MON-17080; -.
DR UniPathway; UPA00240; -.
DR Proteomes; UP000006728; Chromosome.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR CDD; cd03784; GT1_Gtf-like; 1.
DR InterPro; IPR010610; DUF1205.
DR InterPro; IPR030953; Glycosyl_450act.
DR InterPro; IPR002213; UDP_glucos_trans.
DR Pfam; PF06722; DUF1205; 1.
DR TIGRFAMs; TIGR04516; glycosyl_450act; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..421
FT /note="3-alpha-mycarosylerythronolide B desosaminyl
FT transferase"
FT /id="PRO_0000418493"
FT CONFLICT 179
FT /note="D -> G (in Ref. 1; AAB84067)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="D -> H (in Ref. 1; AAB84067)"
FT /evidence="ECO:0000305"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 18..26
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 40..44
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 68..74
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 180..191
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 272..276
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 288..291
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 345..357
FT /evidence="ECO:0007829|PDB:2YJN"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:2YJN"
FT TURN 365..367
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 384..398
FT /evidence="ECO:0007829|PDB:2YJN"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:2YJN"
SQ SEQUENCE 421 AA; 45929 MW; E295A5A8CAF72BD1 CRC64;
MRVVFSSMAS KSHLFGLVPL AWAFRAAGHE VRVVASPALT EDITAAGLTA VPVGTDVDLV
DFMTHAGHDI IDYVRSLDFS ERDPATLTWE HLLGMQTVLT PTFYALMSPD TLIEGMVSFC
RKWRPDLVIW EPLTFAAPIA AAVTGTPHAR LLWGPDITTR ARQNFLGLLP DQPEEHREDP
LAEWLTWTLE KYGGPAFDEE VVVGQWTIDP APAAIRLDTG LKTVGMRYVD YNGPSVVPEW
LHDEPERRRV CLTLGISSRE NSIGQVSIEE LLGAVGDVDA EIIATFDAQQ LEGVANIPDN
VRTVGFVPMH ALLPTCAATV HHGGPGSWHT AAIHGVPQVI LPDGWDTGVR AQRTQEFGAG
IALPVPELTP DQLRESVKRV LDDPAHRAGA ARMRDDMLAE PSPAEVVGIC EELAAGRREP
R
