ID   HPNE_ZYMMO              Reviewed;         414 AA.
AC   Q5NP65; Q56996;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
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:9714766};
GN   OrderedLocusNames=ZMO0871 {ECO:0000312|EMBL:AAV89495.1};
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=264203;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=7894707; DOI=10.1099/00221287-141-1-155;
RA   Reipen I.G., Poralla K., Sahm H., Sprenger G.A.;
RT   "Zymomonas mobilis squalene-hopene cyclase gene (shc): cloning, DNA
RT   sequence analysis, and expression in Escherichia coli.";
RL   Microbiology 141:155-161(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PATHWAY.
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=9714766; DOI=10.1016/s0005-2760(98)00064-2;
RA   Perzl M., Reipen I.G., Schmitz S., Poralla K., Sahm H., Sprenger G.A.,
RA   Kannenberg E.L.;
RT   "Cloning of conserved genes from Zymomonas mobilis and Bradyrhizobium
RT   japonicum that function in the biosynthesis of hopanoid lipids.";
RL   Biochim. Biophys. Acta 1393:108-118(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RA   Um H.W.;
RT   "Sequence analysis of 43F4 fosmid clone of Zymomonas mobilis.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA   Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA   Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA   Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(2005).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
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, ECO:0000269|PubMed:9714766}.
CC   -!- SIMILARITY: Belongs to the HpnE family. {ECO:0000305}.
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DR   EMBL; X80766; CAA56748.1; -; Genomic_DNA.
DR   EMBL; AJ001401; CAA04734.1; -; Genomic_DNA.
DR   EMBL; AF203881; AAF12830.1; -; Genomic_DNA.
DR   EMBL; AE008692; AAV89495.1; -; Genomic_DNA.
DR   PIR; S52618; S52618.
DR   RefSeq; WP_011240737.1; NZ_CP035711.1.
DR   AlphaFoldDB; Q5NP65; -.
DR   SMR; Q5NP65; -.
DR   STRING; 264203.ZMO0871; -.
DR   EnsemblBacteria; AAV89495; AAV89495; ZMO0871.
DR   GeneID; 58026675; -.
DR   KEGG; zmo:ZMO0871; -.
DR   eggNOG; COG1232; Bacteria.
DR   HOGENOM; CLU_022687_2_1_5; -.
DR   OMA; HSMIFNQ; -.
DR   OrthoDB; 630753at2; -.
DR   BRENDA; 1.17.8.1; 6765.
DR   UniPathway; UPA00337; -.
DR   Proteomes; UP000001173; 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..414
FT                   /note="Hydroxysqualene dehydroxylase"
FT                   /id="PRO_0000441696"
FT   CONFLICT        350
FT                   /note="E -> K (in Ref. 1; CAA56748, 2; CAA04734 and 3;
FT                   AAF12830)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   414 AA;  45492 MW;  A580CA564259ED04 CRC64;
     MSVTHIIGAG LAGLSAAVAI THAGGRVKIY EASAMAGGRA RSYHDKKLGI EIDNGNHMLL
     SGNHSAKTYL KRIGAEHRFK SPKEAAFSFC DLSDKERFTI KLSNGPLPWW VLCAKSRVPH
     SKAKDYLALL SLLLADHNTK IGDLVPDNTA LWRKLLDPFF VSVLNTPARE GAACLAAAVI
     RETLMKGGKA CIPRIAYPNL ASSFIDPALD YLKARGVEVD FRNRLRQIHF SGQDVASLEF
     AHQDVKLGKG DKVIIALPAW VVQSLIPDIE TPDKYQAIIN AHFLMKPTAA MPHIMGVVGG
     TADWIFTFEN RISVTISAAN HLLALEKEEL VKRIWDDIQT VYAFKQDMPE WQVVTEKRAT
     FEATVEQNNR RPPAVTAWNN LFLAGNWVRT GLPATIESAI RSGQTAADLA LSHS