ID   BACC_BACAM              Reviewed;         254 AA.
AC   Q8KWS9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Dihydroanticapsin 7-dehydrogenase {ECO:0000250|UniProtKB:P39640};
DE            EC=1.1.1.385 {ECO:0000250|UniProtKB:P39640};
DE   AltName: Full=Bacilysin biosynthesis oxidoreductase BacC {ECO:0000303|PubMed:15609023};
GN   Name=bacC {ECO:0000303|PubMed:15609023};
OS   Bacillus amyloliquefaciens (Bacillus velezensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=1390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN BACILYSIN PRODUCTION, AND
RP   GENE NAME.
RC   STRAIN=ATCC 15841;
RX   PubMed=15609023; DOI=10.1007/s00203-004-0743-8;
RA   Steinborn G., Hajirezaei M.-R., Hofemeister J.;
RT   "bac genes for recombinant bacilysin and anticapsin production in Bacillus
RT   host strains.";
RL   Arch. Microbiol. 183:71-79(2005).
CC   -!- FUNCTION: Part of the bacABCDEFG operon responsible for the
CC       biosynthesis of bacilysin, an irreversible inactivator of the
CC       glutaminase domain of glucosamine synthetase. Catalyzes the
CC       dehydrogenation of the C7-hydroxyl group in the 4S-tetrahydrotyrosine
CC       (4S-H4Tyr) to yield anticapsin (epoxycyclohexanonyl-Ala).
CC       {ECO:0000250|UniProtKB:P39640}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-dihydroanticapsin + NAD(+) = H(+) + L-anticapsin + NADH;
CC         Xref=Rhea:RHEA:44628, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945, ChEBI:CHEBI:84310, ChEBI:CHEBI:84358;
CC         EC=1.1.1.385; Evidence={ECO:0000250|UniProtKB:P39640};
CC   -!- PATHWAY: Antibiotic biosynthesis; bacilysin biosynthesis.
CC       {ECO:0000305|PubMed:15609023}.
CC   -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC       family. {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; AF396779; AAM90575.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KWS9; -.
DR   SMR; Q8KWS9; -.
DR   STRING; 692420.BAMF_3605; -.
DR   eggNOG; COG1028; Bacteria.
DR   UniPathway; UPA00100; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR002347; SDR_fam.
DR   PRINTS; PR00081; GDHRDH.
DR   PRINTS; PR00080; SDRFAMILY.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; NAD; Oxidoreductase.
FT   CHAIN           1..254
FT                   /note="Dihydroanticapsin 7-dehydrogenase"
FT                   /id="PRO_0000054521"
FT   ACT_SITE        152
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10001"
FT   BINDING         9..31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P16544"
SQ   SEQUENCE   254 AA;  27368 MW;  733246D08156704E CRC64;
     MNLTDKTVLI TGGASGIGYA AVQAFLNQQA NVVVADIDEA QGEAMIRKEN NDRLHFVQTD
     ITNEPACQNA ILSAVDKFGG LDVLINNAGI EIVAPIHEME LSDWNKVLNV NLTGMFLMSK
     HALKYMLKSG KGNIINTCSV GGVVAWPDIP AYNASKGGVL QTDAFYRPSI IAKHNIRVNC
     VCPGIIDTPL NEKSFLENNE GTLEEIKKEK AKVNPLLRLG KPEEIANVML FLASDLSSYM
     TGSAITADGG YTAQ