CRUF_HALJT
ID CRUF_HALJT Reviewed; 293 AA.
AC A0A0A1GNF2; M0L9D2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Bisanhydrobacterioruberin hydratase {ECO:0000303|PubMed:25712483};
DE EC=4.2.1.161 {ECO:0000269|PubMed:25712483};
GN Name=cruF {ECO:0000303|PubMed:25712483};
GN Synonyms=c0505 {ECO:0000303|PubMed:25712483};
GN ORFNames=C444_12927 {ECO:0000312|EMBL:EMA29703.1};
OS Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032
OS / NCIMB 13157 / TR-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=1227453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25712483; DOI=10.1128/jb.02523-14;
RA Yang Y., Yatsunami R., Ando A., Miyoko N., Fukui T., Takaichi S.,
RA Nakamura S.;
RT "Complete biosynthetic pathway of the C50 carotenoid bacterioruberin from
RT lycopene in the extremely halophilic archaeon Haloarcula japonica.";
RL J. Bacteriol. 197:1614-1623(2015).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- FUNCTION: Involved in the biosynthesis of the acyclic C50 carotenoid
CC bacterioruberin (BR). Catalyzes the reaction that introduces hydroxyl
CC groups to C3'' and C3''' of bisanhydrobacterioruberin (BABR) to
CC generate BR. {ECO:0000269|PubMed:25712483}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=bacterioruberin = bisanhydrobacterioruberin + 2 H2O;
CC Xref=Rhea:RHEA:38375, ChEBI:CHEBI:15377, ChEBI:CHEBI:49388,
CC ChEBI:CHEBI:87121; EC=4.2.1.161;
CC Evidence={ECO:0000269|PubMed:25712483};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305|PubMed:25712483}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate BABR.
CC {ECO:0000269|PubMed:25712483}.
CC -!- SIMILARITY: Belongs to the BABR hydratase family. {ECO:0000305}.
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DR EMBL; LC008544; BAP82511.1; -; Genomic_DNA.
DR EMBL; AOLY01000037; EMA29703.1; -; Genomic_DNA.
DR RefSeq; WP_004593286.1; NZ_AOLY01000037.1.
DR AlphaFoldDB; A0A0A1GNF2; -.
DR STRING; 1227453.C444_12927; -.
DR EnsemblBacteria; EMA29703; EMA29703; C444_12927.
DR KEGG; ag:BAP82511; -.
DR PATRIC; fig|1227453.3.peg.2545; -.
DR eggNOG; arCOG02835; Archaea.
DR OrthoDB; 77334at2157; -.
DR BioCyc; MetaCyc:MON-20364; -.
DR BRENDA; 4.2.1.161; 13658.
DR Proteomes; UP000011524; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IDA:UniProtKB.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR017823; CruF.
DR InterPro; IPR007354; CruF-like.
DR PANTHER; PTHR39419; PTHR39419; 1.
DR Pfam; PF04240; Caroten_synth; 1.
DR TIGRFAMs; TIGR03460; crt_membr_arch; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Lyase; Membrane; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..293
FT /note="Bisanhydrobacterioruberin hydratase"
FT /id="PRO_0000435600"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 66..86
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 293 AA; 32402 MW; E1BAC8BF9526E547 CRC64;
MGSGKDRTLA GWTLPETKTD ATAQFDRFVT ENRFTIAVVF PLVGAVTLLA SAEGLLPDPL
AFNPYFVLFG TFVMRLPLVA GIFPLVDRRA GLALVALTLY SYGIELVGVR TGWPYGEFTY
GVDLGPMLLG DVPFGLPVFF FPLVLNAYLL VLLLLGNRAA STTVRLLSTL ATVMLVDLVL
DPGAVAIGFW IYEMPQFYGV PWQNYAGWLL SGSVAVLLFD FGFDRAGLRR RLRDCPFMLD
DLVSFVLLWG GINLFYTNWV PFGLAALLGA GLLWTDRFDF DLSETRLGRA VWR