BRP_HALSA
ID BRP_HALSA Reviewed; 359 AA.
AC Q9HPU7;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 25-MAY-2022, entry version 75.
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=VNG_1465G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
RN [2]
RP FUNCTION, ROLE IN BACTERIORHODOPSIN AND RETINAL PRODUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=MPK1;
RX PubMed=11092896; DOI=10.1074/jbc.m009492200;
RA Peck R.F., Echavarri-Erasun C., Johnson E.A., Ng W.V., Kennedy S.P.,
RA Hood L., DasSarma S., Krebs M.P.;
RT "brp and blh are required for synthesis of the retinal cofactor of
RT bacteriorhodopsin in Halobacterium salinarum.";
RL J. Biol. Chem. 276:5739-5744(2001).
CC -!- FUNCTION: Is required for retinal production and bacteriorhodopsin
CC biogenesis. Probably catalyzes the cleavage of beta-carotene at its
CC central double bond (15,15') to yield two molecules of all-trans-
CC retinal. {ECO:0000269|PubMed:11092896}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking brp gene display a 4-fold decrease
CC in bacteriorhodopsin levels compared with wild-type, whereas
CC bacterioopsin levels are normal. Moreover, the beta-carotene level is
CC increased by 3.8-fold, whereas that of retinal is decreased by 3.7-
CC fold. Deletion of both brp and blh completely abolishes
CC bacteriorhodopsin and retinal production, again without affecting
CC bacterioopsin accumulation, and the level of beta-carotene is increased
CC by 5.3-fold. {ECO:0000269|PubMed:11092896}.
CC -!- SIMILARITY: Belongs to the Brp/Blh beta-carotene diooxygenase family.
CC {ECO:0000255|HAMAP-Rule:MF_02093, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG19770.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004437; AAG19770.1; ALT_INIT; Genomic_DNA.
DR PIR; F84300; F84300.
DR RefSeq; WP_012289335.1; NC_002607.1.
DR AlphaFoldDB; Q9HPU7; -.
DR STRING; 64091.VNG_1465G; -.
DR PaxDb; Q9HPU7; -.
DR EnsemblBacteria; AAG19770; AAG19770; VNG_1465G.
DR GeneID; 5953583; -.
DR KEGG; hal:VNG_1465G; -.
DR PATRIC; fig|64091.14.peg.1120; -.
DR HOGENOM; CLU_068196_0_0_2; -.
DR OrthoDB; 35188at2157; -.
DR Proteomes; UP000000554; 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 GO; GO:0042574; P:retinal metabolic process; IMP:UniProtKB.
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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Probable beta-carotene 15,15'-dioxygenase Brp"
FT /id="PRO_0000408496"
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
