BLH_HALSA
ID BLH_HALSA Reviewed; 345 AA.
AC Q9HNE6;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable beta-carotene 15,15'-dioxygenase Blh {ECO:0000305};
DE EC=1.13.11.63 {ECO:0000255|HAMAP-Rule:MF_02093};
DE AltName: Full=Brp-like homolog;
GN Name=blh; OrderedLocusNames=VNG_2136G;
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: Appears to partially substitute for Brp function in retinal
CC biosynthesis during bacteriorhodopsin production. Probably catalyzes
CC the cleavage of beta-carotene at its central double bond (15,15') to
CC yield two molecules of all-trans-retinal.
CC {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: In-frame deletion of blh reduces
CC bacteriorhodopsin accumulation on solid medium but not in liquid.
CC However, deletion of both brp and blh completely abolishes
CC bacteriorhodopsin and retinal production in liquid medium, without
CC affecting bacterioopsin accumulation, and the level of beta-carotene is
CC increased 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=AAG20274.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AE004437; AAG20274.1; ALT_INIT; Genomic_DNA.
DR PIR; F84363; F84363.
DR AlphaFoldDB; Q9HNE6; -.
DR STRING; 64091.VNG_2136G; -.
DR PaxDb; Q9HNE6; -.
DR EnsemblBacteria; AAG20274; AAG20274; VNG_2136G.
DR KEGG; hal:VNG_2136G; -.
DR PATRIC; fig|64091.14.peg.1633; -.
DR HOGENOM; CLU_068196_0_0_2; -.
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..345
FT /note="Probable beta-carotene 15,15'-dioxygenase Blh"
FT /id="PRO_0000408498"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT BINDING 121
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT BINDING 253
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02093"
SQ SEQUENCE 345 AA; 36507 MW; BE9C555F5F99E00C CRC64;
MGASPVALTP LTARARRTLA RPALALGWVA ISIAALPAIT GVSLSPTARY APLVASAVVF
GMPHGAIDYL ALPRAVTGTV TVRWLAVVGV LYLVLGGGYA AAWFFAPVPA AFAFVAITWL
HWGQGDLYPL LDFLDVDYLD TRPRRAATVL IRGGLPMLVP LLGFPERYRS VVDAFAAPFG
GSVGDLAVFD PRVRLWLGVA FAAATVAVLA AGRRRTHSPG AWRVDAAETL LLWVFFFVVP
PVFAVGVYFC VWHSVRHVAR AIAVDGSVHP SLRAGDILGP LARFGVEAAP MTAAALALGG
VLWWAVPNPP TTLESGAALY LVLIAVLTLP HVAVVTWMDR VQGVL
