REBO_LENAE
ID REBO_LENAE Reviewed; 473 AA.
AC Q8KHS0;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Flavin-dependent L-tryptophan oxidase RebO;
DE EC=1.4.3.23 {ECO:0000269|PubMed:15743957, ECO:0000269|PubMed:16313168, ECO:0000269|PubMed:25837855};
DE AltName: Full=L-amino acid oxidase protein;
DE Short=L-AAO;
DE Flags: Precursor;
GN Name=rebO; Synonyms=rbmB;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hyun C.-G., Bililign T., Liao J., Thorson J.S.;
RT "The Biosynthesis of Indolocarbazoles in a Heterologous E. coli Host.";
RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN THE REBECCAMYCIN
RP BIOSYNTHESIS.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14763561; DOI=10.7164/antibiotics.56.950;
RA Onaka H., Taniguchi S., Ikeda H., Igarashi Y., Furumai T.;
RT "pTOYAMAcos, pTYM18, and pTYM19, actinomycete-Escherichia coli integrating
RT vectors for heterologous gene expression.";
RL J. Antibiot. 56:950-956(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR, AND
RP SUBUNIT.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Onaka H.;
RT "Biosynthesis of heterocyclic antibiotics in actinomycetes and an approach
RT to synthesize the natural compounds.";
RL Nihon Hosenkin Gakkaishi 20:62-71(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Asamizu S., Kato Y., Igarashi Y., Furumai T., Onaka H.;
RT "Direct formation of chromopyrrolic acid from indole-3-pyruvic acid by
RT StaD, a novel hemoprotein in indolocarbazole biosynthesis.";
RL Tetrahedron Lett. 47:473-475(2006).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, AND SUBUNIT.
RX PubMed=16313168; DOI=10.1021/bi051706e;
RA Howard-Jones A.R., Walsh C.T.;
RT "Enzymatic generation of the chromopyrrolic acid scaffold of rebeccamycin
RT by the tandem action of RebO and RebD.";
RL Biochemistry 44:15652-15663(2005).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 39243 / DSM 44217 / BCRC 13729 / KCTC 9384;
RX PubMed=25837855; DOI=10.1016/j.abb.2015.03.020;
RA Spolitak T., Ballou D.P.;
RT "Evidence for catalytic intermediates involved in generating the
RT chromopyrrolic acid scaffold of rebeccamycin by RebO and RebD.";
RL Arch. Biochem. Biophys. 573:111-119(2015).
CC -!- FUNCTION: Involved in the biosynthesis of the indolocarbazole antitumor
CC agent rebeccamycin. It generates the imine form of 7-chloroindole 3-
CC pyruvate (7Cl-IPA) from 7-chloro-L-tryptophan (7Cl-Trp), with
CC concomitant two-electron reduction of O(2) to H(2)O(2). The enzyme is
CC also active with L-tryptophan as substrate.
CC {ECO:0000269|PubMed:12619684, ECO:0000269|PubMed:15743957,
CC ECO:0000269|PubMed:16313168, ECO:0000269|PubMed:25837855}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=7-chloro-L-tryptophan + O2 = 3-(7-chloroindol-3-yl)-2-
CC iminopropanoate + H2O2; Xref=Rhea:RHEA:27302, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:58713, ChEBI:CHEBI:59194; EC=1.4.3.23;
CC Evidence={ECO:0000269|PubMed:15743957, ECO:0000269|PubMed:16313168,
CC ECO:0000269|PubMed:25837855};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-tryptophan + O2 = 2-iminio-3-(indol-3-yl)propanoate + H2O2;
CC Xref=Rhea:RHEA:49024, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57912, ChEBI:CHEBI:59193; EC=1.4.3.23;
CC Evidence={ECO:0000269|PubMed:15743957, ECO:0000269|PubMed:16313168,
CC ECO:0000269|PubMed:25837855};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:15743957, ECO:0000269|PubMed:16313168};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.088 mM for 7-chloro-L-tryptophan (at pH 7.8)
CC {ECO:0000269|PubMed:15743957};
CC KM=1.43 mM for 1-methyl-L-tryptophan (at pH 7.8)
CC {ECO:0000269|PubMed:15743957};
CC KM=1.53 mM for L-tryptophan (at pH 7.8)
CC {ECO:0000269|PubMed:15743957};
CC KM=1.84 mM for 5-fluoro-L-tryptophan (at pH 7.8)
CC {ECO:0000269|PubMed:15743957};
CC Note=kcat is 12.12 min(-1), 1.53 min(-1), 14.32 min(-1), and 39.82
CC min(-1) for L-tryptophan, 1-methyl-L-tryptophan, 5-fluoro-L-
CC tryptophan and 7-chloro-L-tryptophan, respectively (at pH 7.8).;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15743957,
CC ECO:0000269|PubMed:16313168}.
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. RebO
CC subfamily. {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; AF534707; AAN01208.1; -; Genomic_DNA.
DR EMBL; AB090952; BAC10674.1; -; Genomic_DNA.
DR EMBL; AB071405; BAC15750.1; -; Genomic_DNA.
DR EMBL; AJ414559; CAC93714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KHS0; -.
DR SMR; Q8KHS0; -.
DR KEGG; ag:BAC10674; -.
DR BioCyc; MetaCyc:MON-15086; -.
DR BRENDA; 1.4.3.23; 4340.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0016641; F:oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor; IDA:UniProtKB.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW FAD; Flavoprotein; Oxidoreductase; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..473
FT /note="Flavin-dependent L-tryptophan oxidase RebO"
FT /id="PRO_0000424086"
FT BINDING 15..16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 35..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 61..64
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 444
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 451..456
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 51897 MW; 727B07D8920BDF87 CRC64;
MSRGHKKITV LGAGVAGLVA AHELEELGHE VEVLEGSDRL GGRVHTHRFG EGGSVPFVEL
GAMRIPTKHR HTIDYIGKLG LTPKLKEFKT LFSDDGAYHT TSAGFVRVRD AAKVLVDEFR
LLMSGRDLRE ETILFGAWLT AVGDAIAPAD FRAALRTDFT ADLLEVVDRI DLDPFLVGAA
RDQFDLHAFF AAHPEVRTSC TGKLNRFVDD ILDETSPRLL RLEGGMDQLV DALVERIRGD
IRTGHEVSAI DVREDHVAVT VHNGHGVNTL RSDHVLCTIP FSVLRNLRLT GLSTDKLEII
HDVKYWSATK VAFRCREPFW ERDGINGGAS FGGGRIRQTY YPPVEGDPTR GAVLLASYTM
GDDADVLGGM PEAQRHEVVL DEVGRMHPEL HEPGMVVEAV SRAWGEDRWS NGAGVTRWGK
DVAACEEERD RAARPEGRLY FAGEHCSSTT AWIDGAVESA LAAVRAIEAG DGR
