ID   CRTD_HALJT              Reviewed;         495 AA.
AC   A0A0A1GKA2; M0L809;
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=Carotenoid 3,4-desaturase {ECO:0000303|PubMed:25712483};
DE            EC=1.3.99.37 {ECO:0000269|PubMed:25712483};
DE   AltName: Full=1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase {ECO:0000305};
GN   Name=crtD {ECO:0000303|PubMed:25712483};
GN   Synonyms=c0507 {ECO:0000303|PubMed:25712483};
GN   ORFNames=C444_12917 {ECO:0000312|EMBL:EMA29701.1};
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). CrtD is involved in the desaturation reactions
CC       that form double bonds at C-3,4 of dihydroisopentenyldehydrorhodopin
CC       (DH-IDR) and C-3',4' of dihydrobisanhydrobacterioruberin (DH-BABR) to
CC       yield isopentenyld ehydrorhodopin (IDR) and bisanhydrobacterioruberin
CC       (BABR), respectively. {ECO:0000269|PubMed:25712483}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + dihydroisopentenyldehydrorhodopin = AH2 +
CC         isopentenyldehydrorhodopin; Xref=Rhea:RHEA:46968, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:87162, ChEBI:CHEBI:87163;
CC         EC=1.3.99.37; Evidence={ECO:0000269|PubMed:25712483};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + dihydrobisanhydrobacterioruberin = AH2 +
CC         bisanhydrobacterioruberin; Xref=Rhea:RHEA:46972, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:87121, ChEBI:CHEBI:87161;
CC         EC=1.3.99.37; Evidence={ECO:0000269|PubMed:25712483};
CC   -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305|PubMed:25712483}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate DH-IDR and DH-
CC       BABR. {ECO:0000269|PubMed:25712483}.
CC   -!- SIMILARITY: Belongs to the carotenoid/retinoid oxidoreductase family.
CC       {ECO:0000305}.
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DR   EMBL; LC008542; BAP82509.1; -; Genomic_DNA.
DR   EMBL; AOLY01000037; EMA29701.1; -; Genomic_DNA.
DR   RefSeq; WP_004593284.1; NZ_AOLY01000037.1.
DR   AlphaFoldDB; A0A0A1GKA2; -.
DR   SMR; A0A0A1GKA2; -.
DR   STRING; 1227453.C444_12917; -.
DR   EnsemblBacteria; EMA29701; EMA29701; C444_12917.
DR   KEGG; ag:BAP82509; -.
DR   PATRIC; fig|1227453.3.peg.2543; -.
DR   eggNOG; arCOG01521; Archaea.
DR   OrthoDB; 41143at2157; -.
DR   BioCyc; MetaCyc:MON-20365; -.
DR   BRENDA; 1.3.99.37; 13658.
DR   Proteomes; UP000011524; Unassembled WGS sequence.
DR   GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR014105; Carotenoid/retinoid_OxRdtase.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02734; crtI_fam; 1.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Oxidoreductase.
FT   CHAIN           1..495
FT                   /note="Carotenoid 3,4-desaturase"
FT                   /id="PRO_0000435601"
SQ   SEQUENCE   495 AA;  55506 MW;  AB82F2BDF09A38F4 CRC64;
     MSDLSGEDVT VVGGGIGGLS AACYLADAGA DVSLLEKNEQ LGGRASRLEV DGFRFDMGPS
     WYLMPDVFER FFAYFGKEPR DYYDLQRLDP HYRIFFKDGD QIDVTGDNDE MAQKFEEYEP
     GAGEAFEEYL STSERHYETA MNKFVYQDRS ELRDWVDLDV MTAAPVGLQL IGTMQSHVED
     YFEHPKLQQI MQYTLVFLGG SPRTTPALYN MMSHVDFNLG VYYPDGGVGA VVDGLVELGE
     ELGVTYETDA EVEEISRRKE GFLVETVHGD TTHPDEVVVN ADYAHAEREL LPDHERQYDD
     DYWDDKTYAP SAFLMYMGVE GDVEPLEHHT LVLPTDWDPH FDDIFDEPAW PDDPAYYLCV
     PSKTDDSVAP DGHSNLFVLV PIAPGLHDGD EIRQEYREKV LADIADNTGV DLRDRIVYEK
     QFAVSDFGER YNATEGTALG LAHTLRQTAL LRPNNRSSAV DGLYFTGSFT TPGIGVPMCL
     ISGEHTAEAL IEDIA