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HPNE_SINFN
ID   HPNE_SINFN              Reviewed;         417 AA.
AC   P55349;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Hydroxysqualene dehydroxylase {ECO:0000250|UniProtKB:Q6N3F3};
DE            Short=SQase {ECO:0000250|UniProtKB:Q6N3F3};
DE            EC=1.17.8.1 {ECO:0000250|UniProtKB:Q6N3F3};
GN   OrderedLocusNames=NGR_a00450; ORFNames=y4aB;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG   Plasmid sym pNGR234a.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=9163424; DOI=10.1038/387394a0;
RA   Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA   Perret X.;
RT   "Molecular basis of symbiosis between Rhizobium and legumes.";
RL   Nature 387:394-401(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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:0000250|UniProtKB:Q6N3F3}.
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:0000250|UniProtKB:Q6N3F3};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; hopanoid biosynthesis.
CC       {ECO:0000250|UniProtKB:Q6N3F3}.
CC   -!- SIMILARITY: Belongs to the HpnE family. {ECO:0000305}.
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DR   EMBL; U00090; AAB91600.1; -; Genomic_DNA.
DR   RefSeq; NP_443762.1; NC_000914.2.
DR   RefSeq; WP_010875087.1; NC_000914.2.
DR   AlphaFoldDB; P55349; -.
DR   SMR; P55349; -.
DR   STRING; 394.NGR_a00450; -.
DR   EnsemblBacteria; AAB91600; AAB91600; NGR_a00450.
DR   KEGG; rhi:NGR_a00450; -.
DR   PATRIC; fig|394.7.peg.42; -.
DR   eggNOG; COG1233; Bacteria.
DR   HOGENOM; CLU_022687_2_1_5; -.
DR   OMA; HSMIFNQ; -.
DR   OrthoDB; 630753at2; -.
DR   UniPathway; UPA00337; -.
DR   Proteomes; UP000001054; Plasmid sym pNGR234a.
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   3: Inferred from homology;
KW   FAD; Flavoprotein; Oxidoreductase; Plasmid; Reference proteome.
FT   CHAIN           1..417
FT                   /note="Hydroxysqualene dehydroxylase"
FT                   /id="PRO_0000200797"
SQ   SEQUENCE   417 AA;  44583 MW;  E4522F97C6B53C60 CRC64;
     MPKNVHIIGA GISGLSAAVQ LSNAGLPVHV YEATQQAGGR CRSFFDSATN LTIDNGNHLV
     LSGNQYVRNY ARAIGTESGL VGPTSAKFPF VDISTVQRWQ VDLGGGRLPT WVFHKARRVP
     DTRLWDYLKL APILWAGADE LVGNTIPCNG TLYRRLVRPL LLAALNCDPP EGSAGLAGAI
     VRETLLAGGE ACRPLVARDG LSAVLVEPAV KLLERRGATV RLSHKLRKLA KSAEIISELD
     FGDDKIAVGP DDAVILAVPP RAAATLLPGL KTPTEFRAVV NAHFRFDPPV GADPILGVVG
     GLVEWLFAYP QRLSVTISNG DRLLDIPREE VVRVIWRDVC EAGGISGELP PWQIVCERRA
     TFQATPEQNA LRPGPVTGCK NLFLAGDWTA TGLPATIEGS VRSGNRAADL ALSETNT
 
 
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