ID   AUAG_STIAU              Reviewed;         383 AA.
AC   H1ZZA4;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Aurachin C monooxygenase/isomerase {ECO:0000305};
DE            EC=1.14.13.222 {ECO:0000269|PubMed:22907798};
GN   Name=auaG {ECO:0000303|PubMed:21979787};
OS   Stigmatella aurantiaca.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=41;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC   STRAIN=Sg a15;
RX   PubMed=21979787; DOI=10.1039/c1mb05328k;
RA   Pistorius D., Li Y., Sandmann A., Mueller R.;
RT   "Completing the puzzle of aurachin biosynthesis in Stigmatella aurantiaca
RT   Sg a15.";
RL   Mol. Biosyst. 7:3308-3315(2011).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RC   STRAIN=Sg a15;
RX   PubMed=22907798; DOI=10.1002/anie.201204138;
RA   Katsuyama Y., Harmrolfs K., Pistorius D., Li Y., Mueller R.;
RT   "A semipinacol rearrangement directed by an enzymatic system featuring
RT   dual-function FAD-dependent monooxygenase.";
RL   Angew. Chem. Int. Ed. 51:9437-9440(2012).
CC   -!- FUNCTION: Catalyzes the initial step in the conversion of aurachin C to
CC       aurachin B. Catalyzes the epoxidation of the C(2)-C(3) double bond of
CC       aurachin C, which is followed by a semipinacol rearrangement, causing
CC       migration of the farnesyl group from C(3) to C(4). Accepts both NADH
CC       and NADPH, but has a preference for NADH.
CC       {ECO:0000269|PubMed:22907798}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aurachin C + H(+) + NADPH + O2 = 4-hydroxy-2-methyl-3-oxo-
CC         [(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + H2O + NADP(+);
CC         Xref=Rhea:RHEA:49004, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:90785, ChEBI:CHEBI:90888; EC=1.14.13.222;
CC         Evidence={ECO:0000269|PubMed:22907798};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aurachin C + H(+) + NADH + O2 = 4-hydroxy-2-methyl-3-oxo-
CC         [(2E,6E)-farnesyl]-3,4-dihydroquinoline 1-oxide + H2O + NAD(+);
CC         Xref=Rhea:RHEA:49000, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90785, ChEBI:CHEBI:90888; EC=1.14.13.222;
CC         Evidence={ECO:0000269|PubMed:22907798};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000269|PubMed:22907798};
CC   -!- DISRUPTION PHENOTYPE: Mutant accumulates aurachin D and aurachin C and
CC       does not produce aurachin B and aurachin A.
CC       {ECO:0000269|PubMed:21979787}.
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DR   EMBL; HE580420; CCD27744.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1ZZA4; -.
DR   SMR; H1ZZA4; -.
DR   KEGG; ag:CCD27744; -.
DR   BioCyc; MetaCyc:MON-18340; -.
DR   BRENDA; 1.14.13.222; 5908.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Monooxygenase; NAD; NADP; Oxidoreductase.
FT   CHAIN           1..383
FT                   /note="Aurachin C monooxygenase/isomerase"
FT                   /id="PRO_0000441676"
FT   BINDING         15
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         285
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
FT   BINDING         295..299
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250|UniProtKB:A6T923"
SQ   SEQUENCE   383 AA;  41286 MW;  B715FAC239DA73B6 CRC64;
     MKTGLTVLIA GGGIGGLTLG VALRRAGIAF KIFERAPALL RVGAGISMQS NAMLAFRTLG
     VDTAVAAAGQ EIQGGAILNP RGEEISSMPV SKASAEVGAP MITIHRGRLQ DVLHQIVGDD
     NLVLGAKVEG FRDGPDGLFV RLADGREFQG DLLVGADGLR SAVRAQLLKE PSPRYSGYTS
     WRGVCDVSEG VRRDYTSESW GPGMRFGVVP IGEGQTYWFA TATAPEGGVD HPDARTELLQ
     RFSGWHAPIP QLIENTPSSA IMRTDIHDRV PIRQWVQGRA VLLGDAAHPM TPNMGQGGCQ
     AVEDAVVLAR CLSLEAELPA ALARYQAVRV ERANDFVAGS YRIGQIGQWE NAFACWVREK
     LMRMMSSDRV DARTRRNLQF TPL