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BKT_CHLRE
ID   BKT_CHLRE               Reviewed;         444 AA.
AC   Q4VKB4;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Zeaxanthin 4-ketolase {ECO:0000303|PubMed:21398427};
DE            EC=1.14.99.64 {ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
DE   AltName: Full=Beta-carotene 4-ketolase {ECO:0000303|PubMed:15849308};
DE            Short=CrBKT {ECO:0000303|PubMed:21398427};
DE            EC=1.14.99.63 {ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
GN   Name=BKT {ECO:0000303|PubMed:15849308};
GN   Synonyms=CBK1 {ECO:0000312|EMBL:EDO99381.1};
GN   ORFNames=CHLREDRAFT_185186 {ECO:0000312|EMBL:EDO99381.1};
OS   Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX   NCBI_TaxID=3055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=21gr / CC-1690;
RX   PubMed=15849308; DOI=10.1104/pp.104.056069;
RA   Lohr M., Im C.-S., Grossman A.R.;
RT   "Genome-based examination of chlorophyll and carotenoid biosynthesis in
RT   Chlamydomonas reinhardtii.";
RL   Plant Physiol. 138:490-515(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC-503;
RX   PubMed=17932292; DOI=10.1126/science.1143609;
RA   Merchant S.S., Prochnik S.E., Vallon O., Harris E.H., Karpowicz S.J.,
RA   Witman G.B., Terry A., Salamov A., Fritz-Laylin L.K., Marechal-Drouard L.,
RA   Marshall W.F., Qu L.H., Nelson D.R., Sanderfoot A.A., Spalding M.H.,
RA   Kapitonov V.V., Ren Q., Ferris P., Lindquist E., Shapiro H., Lucas S.M.,
RA   Grimwood J., Schmutz J., Cardol P., Cerutti H., Chanfreau G., Chen C.L.,
RA   Cognat V., Croft M.T., Dent R., Dutcher S., Fernandez E., Fukuzawa H.,
RA   Gonzalez-Ballester D., Gonzalez-Halphen D., Hallmann A., Hanikenne M.,
RA   Hippler M., Inwood W., Jabbari K., Kalanon M., Kuras R., Lefebvre P.A.,
RA   Lemaire S.D., Lobanov A.V., Lohr M., Manuell A., Meier I., Mets L.,
RA   Mittag M., Mittelmeier T., Moroney J.V., Moseley J., Napoli C.,
RA   Nedelcu A.M., Niyogi K., Novoselov S.V., Paulsen I.T., Pazour G.J.,
RA   Purton S., Ral J.P., Riano-Pachon D.M., Riekhof W., Rymarquis L.,
RA   Schroda M., Stern D., Umen J., Willows R., Wilson N., Zimmer S.L.,
RA   Allmer J., Balk J., Bisova K., Chen C.J., Elias M., Gendler K., Hauser C.,
RA   Lamb M.R., Ledford H., Long J.C., Minagawa J., Page M.D., Pan J.,
RA   Pootakham W., Roje S., Rose A., Stahlberg E., Terauchi A.M., Yang P.,
RA   Ball S., Bowler C., Dieckmann C.L., Gladyshev V.N., Green P., Jorgensen R.,
RA   Mayfield S., Mueller-Roeber B., Rajamani S., Sayre R.T., Brokstein P.,
RA   Dubchak I., Goodstein D., Hornick L., Huang Y.W., Jhaveri J., Luo Y.,
RA   Martinez D., Ngau W.C., Otillar B., Poliakov A., Porter A., Szajkowski L.,
RA   Werner G., Zhou K., Grigoriev I.V., Rokhsar D.S., Grossman A.R.;
RT   "The Chlamydomonas genome reveals the evolution of key animal and plant
RT   functions.";
RL   Science 318:245-250(2007).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21398427; DOI=10.1093/jxb/err070;
RA   Zhong Y.J., Huang J.C., Liu J., Li Y., Jiang Y., Xu Z.F., Sandmann G.,
RA   Chen F.;
RT   "Functional characterization of various algal carotenoid ketolases reveals
RT   that ketolating zeaxanthin efficiently is essential for high production of
RT   astaxanthin in transgenic Arabidopsis.";
RL   J. Exp. Bot. 62:3659-3669(2011).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22526507; DOI=10.1007/s00425-012-1654-6;
RA   Huang J., Zhong Y., Sandmann G., Liu J., Chen F.;
RT   "Cloning and selection of carotenoid ketolase genes for the engineering of
RT   high-yield astaxanthin in plants.";
RL   Planta 236:691-699(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of ketocarotenoids which are
CC       powerful anti-oxidative molecules (PubMed:21398427, PubMed:22526507).
CC       Catalyzes the conversion of zeaxanthin to astaxanthin via adonixanthin
CC       (PubMed:21398427, PubMed:22526507). Catalyzes the conversion of beta-
CC       carotene to canthaxanthin via echinenone (PubMed:21398427,
CC       PubMed:22526507). {ECO:0000269|PubMed:21398427,
CC       ECO:0000269|PubMed:22526507}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 AH2 + all-trans-adonixanthin + 2 O2 = 2 A + all-trans-
CC         (3S,3'S)-astaxanthin + 3 H2O; Xref=Rhea:RHEA:56772,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:40968, ChEBI:CHEBI:80217;
CC         EC=1.14.99.64; Evidence={ECO:0000269|PubMed:21398427,
CC         ECO:0000269|PubMed:22526507};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56773;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 AH2 + all-trans-zeaxanthin + 2 O2 = 2 A + all-trans-
CC         adonixanthin + 3 H2O; Xref=Rhea:RHEA:56768, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:27547, ChEBI:CHEBI:80217; EC=1.14.99.64;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56769;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 AH2 + echinenone + 2 O2 = 2 A + canthaxanthin + 3 H2O;
CC         Xref=Rhea:RHEA:55664, ChEBI:CHEBI:3362, ChEBI:CHEBI:4746,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:17499; EC=1.14.99.63;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55665;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 AH2 + all-trans-beta-carotene + 2 O2 = 2 A + echinenone + 3
CC         H2O; Xref=Rhea:RHEA:55660, ChEBI:CHEBI:4746, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:17579; EC=1.14.99.63;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55661;
CC         Evidence={ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
CC   -!- PATHWAY: Carotenoid biosynthesis; astaxanthin biosynthesis.
CC       {ECO:0000305}.
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DR   EMBL; AY860820; AAX54908.1; -; mRNA.
DR   EMBL; DS496147; EDO99381.1; -; Genomic_DNA.
DR   RefSeq; XP_001698699.1; XM_001698647.1.
DR   AlphaFoldDB; Q4VKB4; -.
DR   PaxDb; Q4VKB4; -.
DR   EnsemblPlants; PNW83930; PNW83930; CHLRE_04g215000v5.
DR   GeneID; 5724273; -.
DR   Gramene; PNW83930; PNW83930; CHLRE_04g215000v5.
DR   KEGG; cre:CHLRE_04g215000v5; -.
DR   HOGENOM; CLU_617317_0_0_1; -.
DR   InParanoid; Q4VKB4; -.
DR   OrthoDB; 1423104at2759; -.
DR   BioCyc; MetaCyc:MON-17803; -.
DR   BRENDA; 1.14.99.63; 1318.
DR   BRENDA; 1.14.99.64; 1318.
DR   UniPathway; UPA00387; -.
DR   ExpressionAtlas; Q4VKB4; baseline.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IDA:UniProtKB.
DR   GO; GO:0016117; P:carotenoid biosynthetic process; IDA:UniProtKB.
DR   InterPro; IPR005804; FA_desaturase_dom.
DR   InterPro; IPR012171; Fatty_acid_desaturase.
DR   PANTHER; PTHR19353; PTHR19353; 1.
DR   Pfam; PF00487; FA_desaturase; 2.
PE   1: Evidence at protein level;
KW   Carotenoid biosynthesis; Oxidoreductase.
FT   CHAIN           1..444
FT                   /note="Zeaxanthin 4-ketolase"
FT                   /id="PRO_0000452211"
FT   REGION          408..444
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  48360 MW;  F002F394C78D7A22 CRC64;
     MGPGIQPTSA RPCSRTKHSR FALLAAALTA RRVKQFTKQF RSRRMAEDIL KLWQRQYHLP
     REDSDKRTLR ERVHLYRPPR SDLGGIAVAV TVIALWATLF VYGLWFVKLP WALKVGETAT
     SWATIAAVFF SLEFLYTGLF ITTHDAMHGT IALRNRRLND FLGQLAISLY AWFDYSVLHR
     KHWEHHNHTG EPRVDPDFHR GNPNLAVWFA QFMVSYMTLS QFLKIAVWSN LLLLAGAPLA
     NQLLFMTAAP ILSAFRLFYY GTYVPHHPEK GHTGAMPWQV SRTSSASRLQ SFLTCYHFDL
     HWEHHRWPYA PWWELPKCRQ IARGAALAPG PLPVPAAAAA TAATAAAAAA ATGSPAPASR
     AGSASSASAA ASGFGSGHSG SVAAQPLSSL PLLSEGVKGL VEGAMELVAG GSSSGGGGEG
     GKPGAGEHGL LQRQRQLAPV GVMA
 
 
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