CAO_ORYSJ
ID CAO_ORYSJ Reviewed; 541 AA.
AC Q8S7E1; Q0IVJ5; Q336Q7; Q336Q8; Q7XC03; Q9FYV0; Q9XJ40;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Chlorophyllide a oxygenase, chloroplastic;
DE Short=Chlorophyll a oxygenase;
DE EC=1.14.13.122;
DE AltName: Full=Chlorophyll b synthase;
DE Flags: Precursor;
GN Name=CAO; Synonyms=LLS1; OrderedLocusNames=Os10g0567400, LOC_Os10g41780;
GN ORFNames=OsJ_32509 {ECO:0000312|EMBL:EEE51429.1}, OSJNBa0057L21.2;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Hwacheong, and cv. Ilpoom;
RA Jwa N.-S., Park S.-G., Park C.-H., Kim S.-O., Ahn I.-P., Park S.-Y.,
RA Yoon C.-H., Lee Y.-H.;
RT "Cloning and expression of a rice cDNA encoding a Lls1 homolog of maize.";
RL Plant Pathol. J. 16:151-155(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 186-541 (ISOFORM 1).
RX PubMed=10408441; DOI=10.1038/22101;
RA Tomitani A., Okada K., Miyashita H., Matthijs H.C.P., Ohno T., Tanaka A.;
RT "Chlorophyll b and phycobilins in the common ancestor of cyanobacteria and
RT chloroplasts.";
RL Nature 400:159-162(1999).
CC -!- FUNCTION: Catalyzes a two-step oxygenase reaction involved in the
CC synthesis of chlorophyll b. Acts specifically on the non-esterified
CC chlorophyllide a and not on chlorophyll a.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chlorophyllide a + 2 H(+) + 2 NADPH + 2 O2 = chlorophyllide b
CC + 3 H2O + 2 NADP(+); Xref=Rhea:RHEA:30359, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:83348, ChEBI:CHEBI:83356;
CC EC=1.14.13.122;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane; Peripheral
CC membrane protein. Plastid, chloroplast thylakoid membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8S7E1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8S7E1-2; Sequence=VSP_020614;
CC -!- TISSUE SPECIFICITY: Expressed in leaves and germinating seedlings, but
CC not in sheaths and roots. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Down-regulated by treatment with H(2)O(2).
CC {ECO:0000269|Ref.1}.
CC -!- DOMAIN: Consists of three domains A, B and C. The C-terminal C domain
CC possesses catalytic function while the N-terminal A domain confers
CC protein instability in response to chlorophyll b accumulation.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG03051.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP55073.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF284781; AAG03051.1; ALT_FRAME; mRNA.
DR EMBL; AC087599; AAL79703.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP55073.2; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000086; ABB48002.2; -; Genomic_DNA.
DR EMBL; DP000086; ABB48003.2; -; Genomic_DNA.
DR EMBL; AP008216; BAF27270.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12123.1; -; Genomic_DNA.
DR EMBL; AP014966; BAT12124.1; -; Genomic_DNA.
DR EMBL; CM000147; EEE51429.1; -; Genomic_DNA.
DR EMBL; AK065124; BAG89371.1; -; mRNA.
DR EMBL; AK067730; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB021310; BAA82479.1; -; mRNA.
DR RefSeq; XP_015614086.1; XM_015758600.1. [Q8S7E1-1]
DR AlphaFoldDB; Q8S7E1; -.
DR SMR; Q8S7E1; -.
DR STRING; 4530.OS10T0567400-01; -.
DR PaxDb; Q8S7E1; -.
DR PRIDE; Q8S7E1; -.
DR EnsemblPlants; Os10t0567400-01; Os10t0567400-01; Os10g0567400. [Q8S7E1-1]
DR EnsemblPlants; Os10t0567400-02; Os10t0567400-02; Os10g0567400. [Q8S7E1-2]
DR GeneID; 4349433; -.
DR Gramene; Os10t0567400-01; Os10t0567400-01; Os10g0567400. [Q8S7E1-1]
DR Gramene; Os10t0567400-02; Os10t0567400-02; Os10g0567400. [Q8S7E1-2]
DR KEGG; osa:4349433; -.
DR eggNOG; ENOG502QS20; Eukaryota.
DR InParanoid; Q8S7E1; -.
DR OMA; CCIEGVG; -.
DR OrthoDB; 1199207at2759; -.
DR BRENDA; 1.14.13.122; 8948.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR ExpressionAtlas; Q8S7E1; baseline and differential.
DR Genevisible; Q8S7E1; OS.
DR GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0015995; P:chlorophyll biosynthetic process; IBA:GO_Central.
DR Gene3D; 2.102.10.10; -; 1.
DR InterPro; IPR013626; PaO.
DR InterPro; IPR017941; Rieske_2Fe-2S.
DR InterPro; IPR036922; Rieske_2Fe-2S_sf.
DR InterPro; IPR015881; Ring-hydroxy_dOase_2Fe2S_BS.
DR InterPro; IPR044043; VanA_C_cat.
DR Pfam; PF08417; PaO; 1.
DR Pfam; PF00355; Rieske; 1.
DR Pfam; PF19112; VanA_C; 1.
DR SUPFAM; SSF50022; SSF50022; 1.
DR PROSITE; PS51296; RIESKE; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Alternative splicing; Chlorophyll biosynthesis; Chloroplast;
KW Coiled coil; Iron; Iron-sulfur; Membrane; Metal-binding; NADP;
KW Oxidoreductase; Plastid; Reference proteome; Thylakoid; Transit peptide.
FT TRANSIT 1..?
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN ?..541
FT /note="Chlorophyllide a oxygenase, chloroplastic"
FT /id="PRO_0000250164"
FT DOMAIN 220..320
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 178..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 114..151
FT /evidence="ECO:0000255"
FT COMPBIAS 178..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 263
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 280
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 283
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 359
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 363
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..25
FT /note="MTTVASLSLLPHLLIKPSFRCCSRK -> MVTLLIETTQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12869764"
FT /id="VSP_020614"
FT CONFLICT 179
FT /note="E -> K (in Ref. 7; AK067730)"
FT /evidence="ECO:0000305"
FT CONFLICT 186..189
FT /note="STSS -> PTRP (in Ref. 8; BAA82479)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="D -> G (in Ref. 7; AK067730)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="L -> V (in Ref. 1; AAG03051)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60855 MW; DE7EFE9CCF68AB21 CRC64;
MTTVASLSLL PHLLIKPSFR CCSRKGVGRY GGIKVYAVLG DDGADYAKNN AWEALFHVDD
PGPRVPIAKG KFLDVNQALE VVRFDIQYCD WRARQDLLTI MVLHNKVVEV LNPLAREFKS
IGTLRKELAE LQEELAKAHN QVHLSETRVS SALDKLAQME TLVNDRLLQD GGSSASTAEC
TSLAPSTSSA SRVVNKKPPR RSLNVSGPVQ PYNPSLKNFW YPVAFSSDLK DDTMVPIDCF
EEQWVIFRGK DGRPGCVMNT CAHRACPLHL GSVNEGRIQC PYHGWEYSTD GKCEKMPSTK
MLNVRIRSLP CFEQEGMVWI WPGNDPPKST IPSLLPPSGF TIHAEIVMEL PVEHGLLLDN
LLDLAHAPFT HTSTFAKGWS VPSLVKFLTP SSGLQGYWDP YPIDMEFRPP CMVLSTIGIS
KPGKLEGKST KQCSTHLHQL HICLPSSRNK TRLLYRMSLD FAPWIKHVPF MHILWSHFAE
KVLNEDLRLV LGQQERMING ANVWNWPVSY DKLGIRYRLW RDAIERGVDR LPFSNQSESG
S
