BKT3_HAELA
ID BKT3_HAELA Reviewed; 320 AA.
AC Q6J3N5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Beta-carotene 4-ketolase 3 {ECO:0000303|PubMed:16242201};
DE Short=HpBKT3 {ECO:0000303|PubMed:21398427};
DE EC=1.14.99.63 {ECO:0000269|PubMed:16242201, ECO:0000269|PubMed:21398427, ECO:0000269|PubMed:22526507};
GN Name=BKT3 {ECO:0000303|PubMed:16242201};
OS Haematococcus lacustris (Green alga) (Haematococcus pluvialis).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Haematococcaceae; Haematococcus.
OX NCBI_TaxID=44745;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP SALT STRESS.
RC STRAIN=NIES-144 / IAM C-392 / MKF-8;
RX PubMed=16242201; DOI=10.1016/j.jbiotec.2005.09.002;
RA Huang J.C., Chen F., Sandmann G.;
RT "Stress-related differential expression of multiple beta-carotene ketolase
RT genes in the unicellular green alga Haematococcus pluvialis.";
RL J. Biotechnol. 122:176-185(2006).
RN [2]
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 [3]
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:16242201, PubMed:21398427,
CC PubMed:22526507). Catalyzes the conversion of beta-carotene to
CC canthaxanthin via echinenone (PubMed:16242201, PubMed:21398427,
CC PubMed:22526507). {ECO:0000269|PubMed:16242201,
CC 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:16242201, ECO:0000269|PubMed:21398427,
CC ECO:0000269|PubMed:22526507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55665;
CC Evidence={ECO:0000269|PubMed:16242201, ECO:0000269|PubMed:21398427,
CC 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:16242201, ECO:0000269|PubMed:21398427,
CC ECO:0000269|PubMed:22526507};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55661;
CC Evidence={ECO:0000269|PubMed:16242201, ECO:0000269|PubMed:21398427,
CC ECO:0000269|PubMed:22526507};
CC -!- PATHWAY: Carotenoid biosynthesis. {ECO:0000305}.
CC -!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:16242201}.
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DR EMBL; AY603347; AAT35555.1; -; mRNA.
DR AlphaFoldDB; Q6J3N5; -.
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; 2.
DR Pfam; PF00487; FA_desaturase; 2.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Oxidoreductase.
FT CHAIN 1..320
FT /note="Beta-carotene 4-ketolase 3"
FT /id="PRO_0000452212"
SQ SEQUENCE 320 AA; 35894 MW; 194EE30B2888FCDA CRC64;
MHVASALMVE QKGSEAAASS PDVLRAWATQ YHMPSESSDA ARPALKHAYK PPASDAKGIT
MALTIIGTWT AVFLHAIFQI RLPTSMDQLH WLPVSEATAQ LLGGSSSLLH IAAVFIVLEF
LYTGLFITTH DAMHGTIALR NRQLNDLLGN ICISLYAWFD YSMLHRKHWE HHNHTGEVGK
DPDFHKGNPG LVPWFASFMS SYMSLWQFAR LAWWAVVMQM LGAPMANLLV FMAAAPILSA
FRLFYFGTYL PHKPGPGPAA GSQVMAWFRA KTSEASDVMS FLTCYHFDLH WEHHRWPFAP
WWQLPHCRRL SGRGLVPALA