ID   AUAH_STIAU              Reviewed;         334 AA.
AC   H1ZZB0;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Aurachin B dehydrogenase {ECO:0000305};
DE            EC=1.1.1.394 {ECO:0000269|PubMed:22907798};
GN   Name=auaH {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 MUTAGENESIS OF SER-111 AND TYR-139.
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 final step in the conversion of aurachin C to
CC       aurachin B. Catalyzes the reduction of 4-hydroxy-2-methyl-3-oxo-4-
CC       ((2E,6E)-farnesyl)-3,4-dihydroquinoline-1-oxide to form 2-methyl-1-oxo-
CC       4-((2E,6E)-farnesyl)-3,4-dihydroquinoline-3,4-diol, which then
CC       undergoes a spontaneous dehydration to form aurachin B. Accepts both
CC       NADH and NADPH, but has a preference for NADH.
CC       {ECO:0000269|PubMed:22907798}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aurachin B + H2O + NAD(+) = 4-hydroxy-2-methyl-3-oxo-[(2E,6E)-
CC         farnesyl]-3,4-dihydroquinoline 1-oxide + NADH; Xref=Rhea:RHEA:48720,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:90784, ChEBI:CHEBI:90785; EC=1.1.1.394;
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}.
CC   -!- SIMILARITY: Belongs to the 3-beta-HSD 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; HE580421; CCD27750.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1ZZB0; -.
DR   SMR; H1ZZB0; -.
DR   KEGG; ag:CCD27750; -.
DR   BioCyc; MetaCyc:MON-18338; -.
DR   BRENDA; 1.1.1.394; 5908.
DR   GO; GO:0003854; F:3-beta-hydroxy-delta5-steroid dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0006694; P:steroid biosynthetic process; IEA:InterPro.
DR   InterPro; IPR002225; 3Beta_OHSteriod_DH/Estase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01073; 3Beta_HSD; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..334
FT                   /note="Aurachin B dehydrogenase"
FT                   /id="PRO_0000441677"
FT   ACT_SITE        139
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:22907798"
FT   MUTAGEN         111
FT                   /note="S->A: Does not produce aurachin B."
FT                   /evidence="ECO:0000269|PubMed:22907798"
FT   MUTAGEN         139
FT                   /note="Y->F: Does not produce aurachin B."
FT                   /evidence="ECO:0000269|PubMed:22907798"
SQ   SEQUENCE   334 AA;  35918 MW;  36425CA3666E6D73 CRC64;
     MRTFVTGGSG YLGRNLLSAL VARGISVRAL VRSEEAAQKV QALGAQPILG TLEHRETLKE
     GMAGCDVLFH AAALTSARAT DAEFHRANVL GTETVLAAAR DARIQRMVHV STEAVLADGR
     PLLQVDESHP LPKRPFAGYP ATKAQAEQLV LQANGPGFTT VVVRPRFIWG ADDTAFLPQL
     IDAIRTKRFR WVDGGRYLTS TCHVANVCEG MLLAAERGPG GEVYFLTDGA PVELRSFLTL
     LLETQGIKAE VGNIPFQAAR AAAHLGESLW RALVPQARAP ALRLAVYLLG REVTLNDDKA
     RRELGYAGRV THQQGLDALR QAGPAGQGAM PHRA