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REBG_LENAE
ID   REBG_LENAE              Reviewed;         421 AA.
AC   Q8KHE4; Q9S595;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=4'-demethylrebeccamycin synthase;
DE            EC=4.3.3.5;
DE   AltName: Full=Arcyriaflavin A N-glycosyltransferase;
GN   Name=rebG; Synonyms=rbmA;
OS   Lentzea aerocolonigenes (Lechevalieria aerocolonigenes) (Saccharothrix
OS   aerocolonigenes).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; Lentzea.
OX   NCBI_TaxID=68170;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=10866221; DOI=10.7164/antibiotics.53.393;
RA   Ohuchi T., Ikeda-Araki A., Watanabe-Sakamoto A., Kojiri K., Nagashima M.,
RA   Okanishi M., Suda H.;
RT   "Cloning and expression of a gene encoding N-glycosyltransferase (ngt) from
RT   Saccarothrix aerocolonigenes ATCC39243.";
RL   J. Antibiot. 53:393-403(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=11983340; DOI=10.1016/s1074-5521(02)00126-6;
RA   Sanchez C., Butovich I.A., Brana A.F., Rohr J., Mendez C., Salas J.A.;
RT   "The biosynthetic gene cluster for the antitumor rebeccamycin:
RT   characterization and generation of indolocarbazole derivatives.";
RL   Chem. Biol. 9:519-531(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=12617516; DOI=10.7164/antibiotics.55.1063;
RA   Onaka H., Taniguchi S., Igarashi Y., Furumai T.;
RT   "Cloning of the staurosporine biosynthetic gene cluster from Streptomyces
RT   sp. TP-A0274 and its heterologous expression in Streptomyces lividans.";
RL   J. Antibiot. 55:1063-1071(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=12512086; DOI=10.1002/cbic.200390004;
RA   Hyun C.G., Bililign T., Liao J., Thorson J.S.;
RT   "The biosynthesis of indolocarbazoles in a heterologous E. coli host.";
RL   ChemBioChem 4:114-117(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=15743957; DOI=10.1128/jb.187.6.2084-2092.2005;
RA   Nishizawa T., Aldrich C.C., Sherman D.H.;
RT   "Molecular analysis of the rebeccamycin L-amino acid oxidase from
RT   Lechevalieria aerocolonigenes ATCC 39243.";
RL   J. Bacteriol. 187:2084-2092(2005).
RN   [6]
RP   FUNCTION.
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=12619684; DOI=10.1271/bbb.67.127;
RA   Onaka H., Taniguchi S., Igarashi Y., Furumai T.;
RT   "Characterization of the biosynthetic gene cluster of rebeccamycin from
RT   Lechevalieria aerocolonigenes ATCC 39243.";
RL   Biosci. Biotechnol. Biochem. 67:127-138(2003).
RN   [7]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX   PubMed=16575939; DOI=10.1002/cbic.200500504;
RA   Zhang C., Albermann C., Fu X., Peters N.R., Chisholm J.D., Zhang G.,
RA   Gilbert E.J., Wang P.G., Van Vranken D.L., Thorson J.S.;
RT   "RebG- and RebM-catalyzed indolocarbazole diversification.";
RL   ChemBioChem 7:795-804(2006).
CC   -!- FUNCTION: Catalyzes the penultimate step in the biosynthesis of
CC       rebeccamycin, an indolocarbazole alkaloid that inhibits topoisomerase
CC       1. Has a wide substrate range, including staurosporine aglycone, EJG-
CC       III-108A, J-104303, 6-N-methyl-arcyriaflavin and indolo-[2,3-a]-
CC       carbazole. {ECO:0000269|PubMed:10866221, ECO:0000269|PubMed:12619684}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4'-demethylrebeccamycin + H2O = beta-D-glucose +
CC         dichloroarcyriaflavin A; Xref=Rhea:RHEA:27397, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15903, ChEBI:CHEBI:330772, ChEBI:CHEBI:595389;
CC         EC=4.3.3.5; Evidence={ECO:0000269|PubMed:16575939};
CC   -!- PATHWAY: Alkaloid biosynthesis.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AB023953; BAA83130.1; -; Genomic_DNA.
DR   EMBL; AJ414559; CAC93713.1; -; Genomic_DNA.
DR   EMBL; AB071405; BAC15749.1; -; Genomic_DNA.
DR   EMBL; AF534707; AAN01207.1; -; Genomic_DNA.
DR   EMBL; AB090952; BAC10673.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KHE4; -.
DR   SMR; Q8KHE4; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; ag:BAC10673; -.
DR   BioCyc; MetaCyc:MON-15083; -.
DR   BRENDA; 4.3.3.5; 4340.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   InterPro; IPR006326; UDPGT_MGT-like.
DR   Pfam; PF00201; UDPGT; 1.
DR   TIGRFAMs; TIGR01426; MGT; 1.
PE   1: Evidence at protein level;
KW   Lyase.
FT   CHAIN           1..421
FT                   /note="4'-demethylrebeccamycin synthase"
FT                   /id="PRO_0000424220"
FT   CONFLICT        270..275
FT                   /note="ANDAER -> GQRRGT (in Ref. 1; BAA83130)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="Missing (in Ref. 1; BAA83130)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        350
FT                   /note="A -> R (in Ref. 1; BAA83130)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414..421
FT                   /note="VDLIEGLV -> ST (in Ref. 1; BAA83130)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   421 AA;  46021 MW;  B4D74C14DAD0BBD9 CRC64;
     MGARVLVATT PGDGHVNPMV PVAQEMVSRG HEVRWYTGKA FRSTVERTGA RHEPMRDAHD
     FGGMPREEAF PQHAGLTGIT GMIAGFRDIF IEPAADQMTD LLALLEDFPA DVLVTDETFF
     GAGFVSERTG IPVAWIATSI YVFSSRDTAP LGLGLPPSSS RLGRLRNTVL KQLTDRVVMR
     DLRRHADVVR DRVGLPRIRK GAFENIMRTP DLYLLGTVPS FEYPRGDMPP EVRFVGPFVS
     PAPPDFTPPA WWGELDSGRP VVHVTQGTVA NDAERLLLPA IRALAAEDVL VVATTGAPLE
     LEPMPANVRV ERFIPHHALL PHVDAMVTNG GYGGVNTALA HGVPLVVAAA TEEKHEVAAR
     VSWSGAGVHL KKRRLSERDI RRAVRAVLDE PRFRVHAARL RDEYAARDAV VDAVDLIEGL
     V
 
 
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