CCS_CAPAN
ID CCS_CAPAN Reviewed; 498 AA.
AC Q42435; A0A089N971; A0A089NBH9; A0A1U8H3A2; Q39470;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 12-AUG-2020, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Capsanthin/capsorubin synthase, chromoplastic {ECO:0000303|PubMed:7920703};
DE EC=5.3.99.8 {ECO:0000269|PubMed:7920703};
DE Flags: Precursor;
GN Name=CCS {ECO:0000303|PubMed:7920703};
GN ORFNames=T459_18053 {ECO:0000312|EMBL:PHT80001.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Yolo Wonder;
RX PubMed=8147854; DOI=10.1006/bbrc.1994.1350;
RA Deruere J., Bouvier F., Steppuhn J., Klein A., Camara B., Kuntz M.;
RT "Structure and expression of two plant genes encoding chromoplast-specific
RT proteins: occurrence of partially spliced transcripts.";
RL Biochem. Biophys. Res. Commun. 199:1144-1150(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Lamuyo;
RX PubMed=7920703; DOI=10.1046/j.1365-313x.1994.6010045.x;
RA Bouvier F., Huqueney P., d'Harlinque A., Kuntz M., Camara B.;
RT "Xanthophyll biosynthesis in chromoplasts: isolation and molecular cloning
RT of an enzyme catalyzing the conversion of 5,6-epoxycarotenoid into
RT ketocarotenoid.";
RL Plant J. 6:45-54(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Yolo Wonder;
RX PubMed=7874747; DOI=10.1007/bf00309944;
RA Houln G., Schantz M.L., Meyer B., Pozueta-Romero J., Schantz R.;
RT "A chromoplast-specific protein in Capsicum annuum: characterization and
RT expression of the corresponding gene.";
RL Curr. Genet. 26:524-527(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rodriguez-Uribe L., O'Connell M.A.;
RT "Capsaicinoid and carotenoid composition and genetic diversity in new
RT Mexican Capsicum annuum L. landraces.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pericarp;
RX PubMed=25617324; DOI=10.1016/j.plantsci.2014.12.014;
RA Kilcrease J., Rodriguez-Uribe L., Richins R.D., Arcos J.M., Victorino J.,
RA O'Connell M.A.;
RT "Correlations of carotenoid content and transcript abundances for fibrillin
RT and carotenogenic enzymes in Capsicum annum fruit pericarp.";
RL Plant Sci. 232:57-66(2015).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24441736; DOI=10.1038/ng.2877;
RA Kim S., Park M., Yeom S.I., Kim Y.M., Lee J.M., Lee H.A., Seo E., Choi J.,
RA Cheong K., Kim K.T., Jung K., Lee G.W., Oh S.K., Bae C., Kim S.B.,
RA Lee H.Y., Kim S.Y., Kim M.S., Kang B.C., Jo Y.D., Yang H.B., Jeong H.J.,
RA Kang W.H., Kwon J.K., Shin C., Lim J.Y., Park J.H., Huh J.H., Kim J.S.,
RA Kim B.D., Cohen O., Paran I., Suh M.C., Lee S.B., Kim Y.K., Shin Y.,
RA Noh S.J., Park J., Seo Y.S., Kwon S.Y., Kim H.A., Park J.M., Kim H.J.,
RA Choi S.B., Bosland P.W., Reeves G., Jo S.H., Lee B.W., Cho H.T., Choi H.S.,
RA Lee M.S., Yu Y., Do Choi Y., Park B.S., van Deynze A., Ashrafi H., Hill T.,
RA Kim W.T., Pai H.S., Ahn H.K., Yeam I., Giovannoni J.J., Rose J.K.,
RA Soerensen I., Lee S.J., Kim R.W., Choi I.Y., Choi B.S., Lim J.S., Lee Y.H.,
RA Choi D.;
RT "Genome sequence of the hot pepper provides insights into the evolution of
RT pungency in Capsicum species.";
RL Nat. Genet. 46:270-278(2014).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Zunla-1;
RX PubMed=24591624; DOI=10.1073/pnas.1400975111;
RA Qin C., Yu C., Shen Y., Fang X., Chen L., Min J., Cheng J., Zhao S., Xu M.,
RA Luo Y., Yang Y., Wu Z., Mao L., Wu H., Ling-Hu C., Zhou H., Lin H.,
RA Gonzalez-Morales S., Trejo-Saavedra D.L., Tian H., Tang X., Zhao M.,
RA Huang Z., Zhou A., Yao X., Cui J., Li W., Chen Z., Feng Y., Niu Y., Bi S.,
RA Yang X., Li W., Cai H., Luo X., Montes-Hernandez S., Leyva-Gonzalez M.A.,
RA Xiong Z., He X., Bai L., Tan S., Tang X., Liu D., Liu J., Zhang S.,
RA Chen M., Zhang L., Zhang L., Zhang Y., Liao W., Zhang Y., Wang M., Lv X.,
RA Wen B., Liu H., Luan H., Zhang Y., Yang S., Wang X., Xu J., Li X., Li S.,
RA Wang J., Palloix A., Bosland P.W., Li Y., Krogh A., Rivera-Bustamante R.F.,
RA Herrera-Estrella L., Yin Y., Yu J., Hu K., Zhang Z.;
RT "Whole-genome sequencing of cultivated and wild peppers provides insights
RT into Capsicum domestication and specialization.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5135-5140(2014).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334;
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF
RP ASP-127; GLU-128; ASP-259; GLU-295; GLU-296; GLU-332 AND HIS-360.
RX PubMed=20460582; DOI=10.1104/pp.110.155440;
RA Mialoundama A.S., Heintz D., Jadid N., Nkeng P., Rahier A., Deli J.,
RA Camara B., Bouvier F.;
RT "Characterization of plant carotenoid cyclases as members of the
RT flavoprotein family functioning with no net redox change.";
RL Plant Physiol. 153:970-979(2010).
CC -!- FUNCTION: Catalyzes the conversion of the ubiquitous 5,6-
CC epoxycarotenoids, antheraxanthin and violaxanthin, into capsanthin and
CC capsorubin, respectively. {ECO:0000269|PubMed:20460582,
CC ECO:0000269|PubMed:7920703}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-violaxanthin = all-trans-capsorubin;
CC Xref=Rhea:RHEA:21752, ChEBI:CHEBI:3378, ChEBI:CHEBI:35288;
CC EC=5.3.99.8; Evidence={ECO:0000269|PubMed:7920703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21753;
CC Evidence={ECO:0000269|PubMed:7920703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-antheraxanthin = all-trans-capsanthin;
CC Xref=Rhea:RHEA:17373, ChEBI:CHEBI:3375, ChEBI:CHEBI:27867;
CC EC=5.3.99.8; Evidence={ECO:0000269|PubMed:7920703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17374;
CC Evidence={ECO:0000269|PubMed:7920703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-violaxanthin = (5R,6S)-5,6-epoxi-capsanthin;
CC Xref=Rhea:RHEA:49320, ChEBI:CHEBI:35288, ChEBI:CHEBI:91165;
CC Evidence={ECO:0000269|PubMed:20460582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49321;
CC Evidence={ECO:0000269|PubMed:20460582};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5R,6S)-5,6-epoxi-capsanthin = all-trans-capsorubin;
CC Xref=Rhea:RHEA:49324, ChEBI:CHEBI:3378, ChEBI:CHEBI:91165;
CC Evidence={ECO:0000269|PubMed:20460582};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49325;
CC Evidence={ECO:0000269|PubMed:20460582};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:20460582};
CC Note=Binds 1 FAD per subunit non-covalently.
CC {ECO:0000269|PubMed:20460582};
CC -!- COFACTOR:
CC Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC Evidence={ECO:0000269|PubMed:20460582};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for NADPH {ECO:0000269|PubMed:20460582};
CC -!- PATHWAY: Carotenoid biosynthesis; capsanthin biosynthesis; capsanthin
CC from antheraxanthin: step 1/1. {ECO:0000305}.
CC -!- PATHWAY: Carotenoid biosynthesis; capsorubin biosynthesis; capsorubin
CC from violaxanthin: step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20460582}.
CC -!- SUBCELLULAR LOCATION: Plastid, chromoplast
CC {ECO:0000305|PubMed:7920703}.
CC -!- SIMILARITY: Belongs to the lycopene cyclase family. {ECO:0000305}.
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DR EMBL; X77289; CAA54495.1; -; Genomic_DNA.
DR EMBL; X76165; CAA53759.1; -; mRNA.
DR EMBL; X78030; CAA54961.1; -; Genomic_DNA.
DR EMBL; KM037687; AIQ82715.1; -; Genomic_DNA.
DR EMBL; KM037690; AIQ82718.1; -; Genomic_DNA.
DR EMBL; KM037689; AIQ82717.1; -; Genomic_DNA.
DR EMBL; KM037688; AIQ82716.1; -; Genomic_DNA.
DR EMBL; KM037692; AIQ82719.1; -; Genomic_DNA.
DR EMBL; KM037693; AIQ82720.1; -; Genomic_DNA.
DR EMBL; KM037694; AIQ82721.1; -; Genomic_DNA.
DR EMBL; KM037695; AIQ82722.1; -; Genomic_DNA.
DR EMBL; KM037696; AIQ82723.1; -; Genomic_DNA.
DR EMBL; KM037697; AIQ82724.1; -; Genomic_DNA.
DR EMBL; KM037698; AIQ82725.1; -; Genomic_DNA.
DR EMBL; KM037699; AIQ82726.1; -; Genomic_DNA.
DR EMBL; KM037700; AIQ82727.1; -; Genomic_DNA.
DR EMBL; KM037701; AIQ82728.1; -; Genomic_DNA.
DR EMBL; KM037702; AIQ82729.1; -; Genomic_DNA.
DR EMBL; KM037703; AIQ82730.1; -; Genomic_DNA.
DR EMBL; KM037704; AIQ82731.1; -; Genomic_DNA.
DR EMBL; KM037705; AIQ82732.1; -; Genomic_DNA.
DR EMBL; KM262815; AIX02795.1; -; mRNA.
DR EMBL; KM262816; AIX02796.1; -; mRNA.
DR EMBL; AYRZ02000006; PHT80001.1; -; Genomic_DNA.
DR PIR; S51511; S51511.
DR PIR; S71511; S71511.
DR RefSeq; NP_001311998.1; NM_001325069.1.
DR AlphaFoldDB; Q42435; -.
DR SMR; Q42435; -.
DR STRING; 4072.A0A089N971; -.
DR SwissLipids; SLP:000001510; -.
DR EnsemblPlants; PHT80001; PHT80001; T459_18053.
DR GeneID; 107875664; -.
DR Gramene; PHT80001; PHT80001; T459_18053.
DR KEGG; ag:CAA53759; -.
DR KEGG; cann:107875664; -.
DR OMA; YHRVWNG; -.
DR OrthoDB; 815606at2759; -.
DR BioCyc; MetaCyc:MON-12145; -.
DR BRENDA; 5.3.99.8; 1169.
DR BRENDA; 5.5.1.19; 1169.
DR UniPathway; UPA00806; UER00774.
DR UniPathway; UPA00807; UER00775.
DR Proteomes; UP000189700; Genome assembly.
DR Proteomes; UP000222542; Chromosome 6.
DR GO; GO:0009509; C:chromoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0052727; F:capsanthin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0052728; F:capsorubin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016117; P:carotenoid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010108; Lycopene_cyclase_b/e.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01790; carotene-cycl; 1.
PE 1: Evidence at protein level;
KW Carotenoid biosynthesis; Chromoplast; Flavoprotein; Isomerase; NAD;
KW Oxidoreductase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..52
FT /note="Chromoplast"
FT /evidence="ECO:0000255"
FT CHAIN 53..498
FT /note="Capsanthin/capsorubin synthase, chromoplastic"
FT /id="PRO_0000018436"
FT MOTIF 293..297
FT /note="FLEET motif"
FT /evidence="ECO:0000305|PubMed:20460582"
FT BINDING 84..112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MUTAGEN 127
FT /note="D->A: Reduces catalytic activity 1.5-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 128
FT /note="E->A: Reduces catalytic activity 23-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 259
FT /note="D->A: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 295
FT /note="E->A,K,R: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 296
FT /note="E->A,K,R: Almost abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 332
FT /note="E->A: Reduces catalytic activity 10-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 360
FT /note="H->A: Abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 360
FT /note="H->K: Reduces catalytic activity 3-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT MUTAGEN 360
FT /note="H->R: Reduces catalytic activity 4-fold."
FT /evidence="ECO:0000269|PubMed:20460582"
FT CONFLICT 79
FT /note="R -> G (in Ref. 1; CAA54495, 2; CAA53759, 3;
FT CAA54961, 4; AIQ82715/AIQ82716/AIQ82717/AIQ82718 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> R (in Ref. 3; CAA54961)"
FT /evidence="ECO:0000305"
FT CONFLICT 378..380
FT /note="AEA -> LRP (in Ref. 3; CAA54961)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..408
FT /note="PSD -> LRH (in Ref. 3; CAA54961)"
FT /evidence="ECO:0000305"
FT CONFLICT 458..497
FT /note="ELAVLSLYLFGHASNLARLDIVTKCTVPLVKLLGNLAIES -> RTCCTQFV
FT PFWTC (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 56758 MW; 110DFE717670F2E1 CRC64;
METLLKPFPS PLLSIPTPNM YSFKHNSTFP NPTKQKDSRK FHYRNKSSTH FCSFLDLAPT
SKPESLDVNI SWVDTDLDRA EFDVIIIGTG PAGLRLAEQV SKYGIKVCCV DPSPLSMWPN
NYGVWVDEFE KLGLEDCLDH KWPVSCVHIS DHKTKYLDRP YGRVSRKKLK LKLLNSCVEN
RVKFYKAKVL KVKHEEFESS IVCDDGRKIS GSLIVDASGY ASDFIEYDKP RNHGYQVAHG
ILAEVDNHPF DLDKMMLMDW RDSHLGNEPY LRVKNTKEPT FLYAMPFDRN LVFLEETSLV
SRPMLSYMEV KRRMVARLRH LGIKVRSVLE EEKCVITMGG PLPRIPQNVM AIGGTSGIVH
PSSGYMVARS MALAPVLAEA IVESLGSTRM IRGSQLYHRV WNGLWPSDRR RVRECYCFGM
ETLLKLDLEG TRRLFDAFFD VDPKYWHGFL SSRLSVKELA VLSLYLFGHA SNLARLDIVT
KCTVPLVKLL GNLAIESL
