ID   HPNE_RHOPA              Reviewed;         418 AA.
AC   Q6N3F3;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Hydroxysqualene dehydroxylase {ECO:0000303|PubMed:26258173};
DE            Short=SQase {ECO:0000303|PubMed:26258173};
DE            EC=1.17.8.1 {ECO:0000269|PubMed:26258173};
GN   Name=hpnE {ECO:0000303|PubMed:26258173};
GN   OrderedLocusNames=RPA3741 {ECO:0000312|EMBL:CAE29182.1};
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=26258173; DOI=10.1021/acscentsci.5b00115;
RA   Pan J.J., Solbiati J.O., Ramamoorthy G., Hillerich B.S., Seidel R.D.,
RA   Cronan J.E., Almo S.C., Poulter C.D.;
RT   "Biosynthesis of squalene from farnesyl diphosphate in bacteria: three
RT   steps catalyzed by three enzymes.";
RL   ACS Cent. Sci. 1:77-82(2015).
CC   -!- FUNCTION: Involved in the biosynthesis of the hopanoid precursor
CC       squalene (SQ) from farnesyl diphosphate (FPP). Catalyzes the third
CC       (last) step, the reduction of hydroxysqualene (HSQ) to SQ.
CC       {ECO:0000269|PubMed:26258173}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=FAD + H(+) + H2O + squalene = FADH2 + hydroxysqualene;
CC         Xref=Rhea:RHEA:49088, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15440, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC         ChEBI:CHEBI:88123; EC=1.17.8.1;
CC         Evidence={ECO:0000269|PubMed:26258173};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; hopanoid biosynthesis.
CC       {ECO:0000269|PubMed:26258173}.
CC   -!- SIMILARITY: Belongs to the HpnE 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; BX572605; CAE29182.1; -; Genomic_DNA.
DR   RefSeq; WP_011159279.1; NC_005296.1.
DR   AlphaFoldDB; Q6N3F3; -.
DR   SMR; Q6N3F3; -.
DR   STRING; 258594.RPA3741; -.
DR   PRIDE; Q6N3F3; -.
DR   EnsemblBacteria; CAE29182; CAE29182; RPA3741.
DR   GeneID; 66894847; -.
DR   KEGG; rpa:RPA3741; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_022687_2_1_5; -.
DR   OMA; HSMIFNQ; -.
DR   PhylomeDB; Q6N3F3; -.
DR   BioCyc; MetaCyc:MON-19572; -.
DR   BioCyc; RPAL258594:TX73_RS19095-MON; -.
DR   UniPathway; UPA00337; -.
DR   Proteomes; UP000001426; Chromosome.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; -; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR017830; SQase_HpnE.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR03467; HpnE; 1.
PE   1: Evidence at protein level;
KW   FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT   CHAIN           1..418
FT                   /note="Hydroxysqualene dehydroxylase"
FT                   /id="PRO_0000441695"
SQ   SEQUENCE   418 AA;  43828 MW;  0EDD7A5F5552D45D CRC64;
     MSKTVHVIGA GISGLAAAIR LARAGLTVHV HEAMQQAGGR CRSYFDAQTG LVIDNGNHLL
     LSGNHAACEY ARTIGTEAGL VGPERAEFDF IDLPANARWR LKLGGGKLPL WLFDANSRVP
     DTSIGDYLGL MPLLWAPTTK LIGDTINCSG PLYDRLVAPL LLAALNVDPP EGSAGLAGAV
     VRETLLAGGK ACRPLIARDG LSAVLVEPAV AQLAARGPGV QFGHELRALT PAGDRVGALQ
     FGGEDVVTLG PDDAVVLAVP PRPAASLLPG LKTPQEYRAI VNAHFNYAPP PGMPALTGVI
     GGVVEWLFAF PNRLSVTISN GDRLVDAPRE QLAAEIWGEI CKIAGISANL PPWQIVRERR
     ATFAATPAQN ALRPGPVTQW RNLYLAGDWT DTGLPATIEG SVRSGNRAAD LVLAAGRA