ID   IND2_STRGR              Reviewed;         570 AA.
AC   A0A0D4BSN8;
DT   28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT   27-MAY-2015, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Beta-methylindole-3-pyruvate reductase {ECO:0000303|PubMed:25730866};
DE            EC=1.1.1.397 {ECO:0000269|PubMed:25730866};
DE   AltName: Full=Beta-methylindolepyruvate dehydrogenase {ECO:0000305};
GN   Name=ind2 {ECO:0000303|PubMed:25730866};
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 12648 {ECO:0000312|EMBL:AJT38683.1};
RX   PubMed=25730866; DOI=10.1073/pnas.1419964112;
RA   Du Y.L., Alkhalaf L.M., Ryan K.S.;
RT   "In vitro reconstitution of indolmycin biosynthesis reveals the molecular
RT   basis of oxazolinone assembly.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:2717-2722(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the antibiotic indolmycin, an
CC       inhibitor of the bacterial tryptophan-tRNA synthetases. Catalyzes the
CC       NADH-dependent reduction of beta-methylindolepyruvate to yield
CC       indolmycenate. {ECO:0000269|PubMed:25730866}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S,3R)-2-hydroxy-3-(indol-3-yl)butanoate + NAD(+) = (R)-3-
CC         (indol-3-yl)-2-oxobutanoate + H(+) + NADH; Xref=Rhea:RHEA:10176,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:91180, ChEBI:CHEBI:131783; EC=1.1.1.397;
CC         Evidence={ECO:0000269|PubMed:25730866};
CC   -!- DISRUPTION PHENOTYPE: Cells laking this gene are unable to produce
CC       indolmycenate. {ECO:0000269|PubMed:25730866}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}.
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DR   EMBL; KM596502; AJT38683.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D4BSN8; -.
DR   KEGG; ag:AJT38683; -.
DR   BioCyc; MetaCyc:MON-19775; -.
DR   BRENDA; 1.1.1.397; 12251.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..570
FT                   /note="Beta-methylindole-3-pyruvate reductase"
FT                   /id="PRO_0000443562"
FT   ACT_SITE        306
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P00344"
SQ   SEQUENCE   570 AA;  62085 MW;  5AF1A4B1C1D23B8E CRC64;
     MKLDDKRILI IGAGEVGTAV AEDLVNRSDP TEIIIHTSRQ QTMDMRVGHL KEMAGPRTLL
     TGSWGDIFAP YELTHRSRSE INDRNVRLAL AEFFLQPSGE AQLRRTTIYE LISRHRPHIV
     IDAVNSASVC TYTEDPHQTC GELLDLARGT GGPRTAEAPA ELPAVTPDIA DVATDALLSL
     STPILHRYVD SLRRAMADFQ VERFIKVSTT GLGGMGYNCP YTHGSVTEFG LSDALVGKIG
     SAGVLHQLLW NLHHTAGCDV RLVIPAALIG WESVRHGAYT SRGRPVALQD CSRPLPLHLD
     RPLGEHAAAS SVAEPAAEDE PSAEMVHVPA GDNSTYSRAE MSLSTALGQF ESVTREEVAA
     AVLDTLLGST RFDLFTAMDT ASLQSSYLAA QMRTSTLTSM RQLEKAYDRP SIVSGNLGPT
     ISKDLLELHV LCTAAGSLEQ ARTMSTTVLA SSASALVRED VYLRQQALSI GLAVLLPDDQ
     WLAGPRLSVP SRIDPEAKVT RADIDDWSRQ GWVDLRPARI LHWQENLRRI EQDASAGKTA
     FALDDTAYDV GEVLAYHYKL TGQARRIKGL