RDMC_STREF
ID RDMC_STREF Reviewed; 298 AA.
AC Q54528;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Aclacinomycin methylesterase RdmC;
DE EC=3.1.1.95;
GN Name=rdmC;
OS Streptomyces purpurascens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1924;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25489 / DSM 40310 / JCM 4509 / NBRC 13077 / Maria 515;
RX PubMed=8081500; DOI=10.1099/00221287-140-6-1351;
RA Niemi J., Ylihonko K., Hakala J., Parssinen R., Kopio A., Mantsala P.;
RT "Hybrid anthracycline antibiotics: production of new anthracyclines by
RT cloned genes from Streptomyces purpurascens in Streptomyces galilaeus.";
RL Microbiology 140:1351-1358(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 25489 / DSM 40310 / JCM 4509 / NBRC 13077 / Maria 515;
RX PubMed=7751313; DOI=10.1128/jb.177.10.2942-2945.1995;
RA Niemi J., Mantsala P.;
RT "Nucleotide sequences and expression of genes from Streptomyces
RT purpurascens that cause the production of new anthracyclines in
RT Streptomyces galilaeus.";
RL J. Bacteriol. 177:2942-2945(1995).
RN [3]
RP PROTEIN SEQUENCE OF 2-13, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=ATCC 25489 / DSM 40310 / JCM 4509 / NBRC 13077 / Maria 515;
RX PubMed=11004563; DOI=10.1016/s0167-4838(00)00089-3;
RA Wang Y., Niemi J., Airas K., Ylihonko K., Hakala J., Mantsala P.;
RT "Modifications of aclacinomycin T by aclacinomycin methyl esterase (RdmC)
RT and aclacinomycin-10-hydroxylase (RdmB) from Streptomyces purpurascens.";
RL Biochim. Biophys. Acta 1480:191-200(2000).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH PRODUCT ANALOGS,
RP ACTIVE SITE, AND SUBUNIT.
RX PubMed=12878604; DOI=10.1074/jbc.m304008200;
RA Jansson A., Niemi J., Mantsala P., Schneider G.;
RT "Crystal structure of aclacinomycin methylesterase with bound product
RT analogues: implications for anthracycline recognition and mechanism.";
RL J. Biol. Chem. 278:39006-39013(2003).
CC -!- FUNCTION: Involved in the biosynthesis of the anthracycline
CC aclacinomycin which is an aromatic polyketide antibiotic that exhibits
CC high cytotoxicity and is widely applied in the chemotherapy of a
CC variety of cancers. Catalyzes the removal of the methoxy group from the
CC C-15 position of aclacinomycin T and A to yield 15-
CC demethoxyaclacinomycin T and A, respectively.
CC {ECO:0000269|PubMed:11004563, ECO:0000269|PubMed:7751313}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=aclacinomycin T + H2O = 15-demethylaclacinomycin T + methanol;
CC Xref=Rhea:RHEA:37891, ChEBI:CHEBI:15377, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:74354, ChEBI:CHEBI:77979; EC=3.1.1.95;
CC Evidence={ECO:0000269|PubMed:11004563};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15.5 uM for aclacinomycin T (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:11004563};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11004563};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius. The activity at 30 and 45
CC degrees Celsius is 58% and 87% of the optimal activity, respectively.
CC Exceptionally high temperature stability.
CC {ECO:0000269|PubMed:11004563};
CC -!- PATHWAY: Antibiotic biosynthesis; aclacinomycin biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11004563,
CC ECO:0000269|PubMed:12878604}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Hydrolase RdmC
CC family. {ECO:0000305}.
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DR EMBL; U10405; AAA83422.1; -; Genomic_DNA.
DR PIR; A57139; A57139.
DR PDB; 1Q0R; X-ray; 1.45 A; A=1-298.
DR PDB; 1Q0Z; X-ray; 1.95 A; A=1-298.
DR PDBsum; 1Q0R; -.
DR PDBsum; 1Q0Z; -.
DR AlphaFoldDB; Q54528; -.
DR SMR; Q54528; -.
DR DrugBank; DB04131; 10-(4-Dimethylamino-5-Hydroxy-6-Methyl-Tetrahydro-Pyran-2-Yloxy)-8-Ethyl-1,8,11-Trihydroxy-7,8,9,10-Tetrahydro-Naphthacene-5,12-Dione.
DR DrugBank; DB01806; 10-decarboxymethylaclacinomycin A.
DR ESTHER; strpu-rdmC; Aclacinomycin-methylesterase_RdmC.
DR KEGG; ag:AAA83422; -.
DR BioCyc; MetaCyc:MON-18184; -.
DR BRENDA; 3.1.1.95; 6079.
DR UniPathway; UPA01043; -.
DR EvolutionaryTrace; Q54528; -.
DR GO; GO:0102542; F:aclacinomycin A methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0102530; F:aclacinomycin T methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:UniProtKB.
DR GO; GO:0102543; F:epsilon-rhodomycinone methylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Direct protein sequencing;
KW Hydrolase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11004563"
FT CHAIN 2..298
FT /note="Aclacinomycin methylesterase RdmC"
FT /id="PRO_0000425719"
FT DOMAIN 24..277
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 102
FT /evidence="ECO:0000255"
FT ACT_SITE 248
FT /evidence="ECO:0000255"
FT ACT_SITE 276
FT /evidence="ECO:0000255"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 11..19
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1Q0R"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:1Q0R"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 172..187
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 189..191
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:1Q0R"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 255..261
FT /evidence="ECO:0007829|PDB:1Q0R"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:1Q0R"
FT HELIX 283..296
FT /evidence="ECO:0007829|PDB:1Q0R"
SQ SEQUENCE 298 AA; 31792 MW; 04FB4141C5A6E424 CRC64;
MSERIVPSGD VELWSDDFGD PADPALLLVM GGNLSALGWP DEFARRLADG GLHVIRYDHR
DTGRSTTRDF AAHPYGFGEL AADAVAVLDG WGVDRAHVVG LSMGATITQV IALDHHDRLS
SLTMLLGGGL DIDFDANIER VMRGEPTLDG LPGPQQPFLD ALALMNQPAE GRAAEVAKRV
SKWRILSGTG VPFDDAEYAR WEERAIDHAG GVLAEPYAHY SLTLPPPSRA AELREVTVPT
LVIQAEHDPI APAPHGKHLA GLIPTARLAE IPGMGHALPS SVHGPLAEVI LAHTRSAA
