ID   BRP_HALS3               Reviewed;         359 AA.
AC   B0R5N7; Q47973;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Probable beta-carotene 15,15'-dioxygenase Brp {ECO:0000305};
DE            EC=1.13.11.63 {ECO:0000255|HAMAP-Rule:MF_02093};
DE   AltName: Full=Bacteriorhodopsin-related protein;
GN   Name=brp; OrderedLocusNames=OE_3102R;
OS   Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=478009;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=6093059; DOI=10.1093/nar/12.20.7949;
RA   Betlach M., Friedman J., Boyer H.W., Pfeifer F.;
RT   "Characterization of a halobacterial gene affecting bacterio-opsin gene
RT   expression.";
RL   Nucleic Acids Res. 12:7949-7959(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29341 / DSM 671 / R1;
RX   PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA   Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA   Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT   "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT   R1 compared to that of strain NRC-1.";
RL   Genomics 91:335-346(2008).
CC   -!- FUNCTION: Catalyzes the cleavage of beta-carotene at its central double
CC       bond (15,15') to yield two molecules of all-trans-retinal.
CC       {ECO:0000255|HAMAP-Rule:MF_02093}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=all-trans-beta-carotene + O2 = 2 all-trans-retinal;
CC         Xref=Rhea:RHEA:32887, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579,
CC         ChEBI:CHEBI:17898; EC=1.13.11.63; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_02093};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02093};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_02093,
CC       ECO:0000305}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_02093, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Brp/Blh beta-carotene diooxygenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02093, ECO:0000305}.
CC   -!- CAUTION: Was originally thought to regulate bop expression
CC       (PubMed:6093059). However, this seems to result from a polar effect on
CC       the downstream gene bat, which forms a transcription unit with brp.
CC       {ECO:0000305|PubMed:6093059}.
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DR   EMBL; X01081; CAA25558.1; -; Genomic_DNA.
DR   EMBL; AM774415; CAP14054.1; -; Genomic_DNA.
DR   PIR; T44816; T44816.
DR   RefSeq; WP_012289335.1; NC_010364.1.
DR   AlphaFoldDB; B0R5N7; -.
DR   EnsemblBacteria; CAP14054; CAP14054; OE_3102R.
DR   GeneID; 5953583; -.
DR   KEGG; hsl:OE_3102R; -.
DR   HOGENOM; CLU_068196_0_0_2; -.
DR   OMA; HGGYEHF; -.
DR   Proteomes; UP000001321; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0003834; F:beta-carotene 15,15'-dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010436; F:carotenoid dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016121; P:carotene catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02093; Beta_carotene_diox; 1.
DR   InterPro; IPR022270; Blh_monoox.
DR   Pfam; PF15461; BCD; 1.
DR   TIGRFAMs; TIGR03753; blh_monoox; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Dioxygenase; Iron; Membrane; Metal-binding; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..359
FT                   /note="Probable beta-carotene 15,15'-dioxygenase Brp"
FT                   /id="PRO_0000408497"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        194..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        293..313
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
SQ   SEQUENCE   359 AA;  37569 MW;  7FE6AE9AC6DB3082 CRC64;
     MSNRSQFVPS WLVPEAAGDL PLTVSRLSLL ALAAAFAVGY GAGFAVPLEV QAGVYLLGMV
     AMNLPHGGYE HFENLRRRAA SFQGKYIVAY LVGIAAFGAL FFVAPVAGLG LAVTVAVAKG
     GFGGVQSMDA LYGTDHLRTR PQRWLAAVVR GGAVMVVPML FWTDVFYAFS SVMISIFDPS
     AVSALGGDIA TRRLVLGGGY GALVVAHLGL GYRRAAGTGS FLADAAETLL LIAYFALVPV
     VIAVGLYFPL WYSARQVARS SAVDDTAMTQ ADATGMLDAL DADDPARATL ASWAVLIVGS
     VATFGLAAVL WLLSPQPLGG GGILVGLVAF WSIFVSIIAL PHVVVGGWLD RTRGIWYVP