CAO_ARATH
ID CAO_ARATH Reviewed; 536 AA.
AC Q9MBA1; Q0WQP6; Q3ECX2; Q3ECX3; Q9SPF2; Q9XJ37;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Chlorophyllide a oxygenase, chloroplastic;
DE Short=Chlorophyll a oxygenase;
DE EC=1.14.13.122 {ECO:0000269|PubMed:10758481};
DE AltName: Full=Chlorophyll b synthase;
DE Short=AtCAO;
DE Flags: Precursor;
GN Name=CAO; Synonyms=CHL; OrderedLocusNames=At1g44446; ORFNames=T18F15.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), MUTANTS CHL-2 AND CHL-3, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10468639; DOI=10.1073/pnas.96.18.10507;
RA Espineda C.E., Linford A.S., Devine D., Brusslan J.A.;
RT "The AtCAO gene, encoding chlorophyll a oxygenase, is required for
RT chlorophyll b synthesis in Arabidopsis thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10507-10511(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10758481; DOI=10.1046/j.1365-313x.2000.00672.x;
RA Oster U., Tanaka R., Tanaka A., Ruediger W.;
RT "Cloning and functional expression of the gene encoding the key enzyme for
RT chlorophyll b biosynthesis (CAO) from Arabidopsis thaliana.";
RL Plant J. 21:305-310(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP CHARACTERIZATION.
RX PubMed=14716565; DOI=10.1007/s00425-003-1181-6;
RA Nagata N., Satoh S., Tanaka R., Tanaka A.;
RT "Domain structures of chlorophyllide a oxygenase of green plants and
RT Prochlorothrix hollandica in relation to catalytic functions.";
RL Planta 218:1019-1025(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=15086960; DOI=10.1186/1471-2229-4-5;
RA Eggink L.L., LoBrutto R., Brune D.C., Brusslan J., Yamasato A., Tanaka A.,
RA Hoober J.K.;
RT "Synthesis of chlorophyll b: localization of chlorophyllide a oxygenase and
RT discovery of a stable radical in the catalytic subunit.";
RL BMC Plant Biol. 4:5-5(2004).
RN [10]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=15805480; DOI=10.1105/tpc.105.031518;
RA Yamasato A., Nagata N., Tanaka R., Tanaka A.;
RT "The N-terminal domain of chlorophyllide a oxygenase confers protein
RT instability in response to chlorophyll b accumulation in Arabidopsis.";
RL Plant Cell 17:1585-1597(2005).
RN [11]
RP MUTAGENESIS OF 97-GLN--HIS-106.
RX PubMed=19843523; DOI=10.1074/jbc.m109.008144;
RA Sakuraba Y., Tanaka R., Yamasato A., Tanaka A.;
RT "Determination of a chloroplast degron in the regulatory domain of
RT chlorophyllide a oxygenase.";
RL J. Biol. Chem. 284:36689-36699(2009).
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 {ECO:0000269|PubMed:10758481}.
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; Evidence={ECO:0000269|PubMed:10758481};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane
CC {ECO:0000269|PubMed:15086960}; Peripheral membrane protein. Plastid,
CC chloroplast thylakoid membrane {ECO:0000269|PubMed:15086960};
CC Peripheral membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9MBA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9MBA1-2; Sequence=VSP_017073, VSP_017074;
CC Name=3;
CC IsoId=Q9MBA1-3; Sequence=VSP_017071, VSP_017072;
CC -!- INDUCTION: By light. Probable feedback regulation.
CC {ECO:0000269|PubMed:10468639}.
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.
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DR EMBL; AB021316; BAA82484.1; -; mRNA.
DR EMBL; AF177200; AAD54323.1; -; Genomic_DNA.
DR EMBL; AB030565; BAA90462.1; -; Genomic_DNA.
DR EMBL; AC084807; AAK43487.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32034.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32035.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32036.1; -; Genomic_DNA.
DR EMBL; AY128357; AAM91560.1; -; mRNA.
DR EMBL; BT002075; AAN72086.1; -; mRNA.
DR EMBL; AK228645; BAF00553.1; -; mRNA.
DR PIR; T52458; T52458.
DR RefSeq; NP_175088.1; NM_103548.5. [Q9MBA1-1]
DR RefSeq; NP_973969.1; NM_202240.2. [Q9MBA1-2]
DR RefSeq; NP_973970.1; NM_202241.2. [Q9MBA1-3]
DR AlphaFoldDB; Q9MBA1; -.
DR SMR; Q9MBA1; -.
DR BioGRID; 26254; 1.
DR STRING; 3702.AT1G44446.1; -.
DR PaxDb; Q9MBA1; -.
DR PRIDE; Q9MBA1; -.
DR ProteomicsDB; 239124; -. [Q9MBA1-1]
DR EnsemblPlants; AT1G44446.1; AT1G44446.1; AT1G44446. [Q9MBA1-1]
DR EnsemblPlants; AT1G44446.2; AT1G44446.2; AT1G44446. [Q9MBA1-2]
DR EnsemblPlants; AT1G44446.3; AT1G44446.3; AT1G44446. [Q9MBA1-3]
DR GeneID; 841029; -.
DR Gramene; AT1G44446.1; AT1G44446.1; AT1G44446. [Q9MBA1-1]
DR Gramene; AT1G44446.2; AT1G44446.2; AT1G44446. [Q9MBA1-2]
DR Gramene; AT1G44446.3; AT1G44446.3; AT1G44446. [Q9MBA1-3]
DR KEGG; ath:AT1G44446; -.
DR Araport; AT1G44446; -.
DR TAIR; locus:2823671; AT1G44446.
DR eggNOG; ENOG502QS20; Eukaryota.
DR HOGENOM; CLU_027465_1_0_1; -.
DR InParanoid; Q9MBA1; -.
DR PhylomeDB; Q9MBA1; -.
DR BioCyc; ARA:AT1G44446-MON; -.
DR BioCyc; MetaCyc:AT1G44446-MON; -.
DR BRENDA; 1.14.13.122; 399.
DR UniPathway; UPA00668; -.
DR PRO; PR:Q9MBA1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MBA1; baseline and differential.
DR Genevisible; Q9MBA1; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009706; C:chloroplast inner membrane; IDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042651; C:thylakoid membrane; IDA:TAIR.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IDA:TAIR.
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; IMP:TAIR.
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 1: Evidence at protein 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..36
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 37..536
FT /note="Chlorophyllide a oxygenase, chloroplastic"
FT /id="PRO_0000045788"
FT DOMAIN 221..321
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT COILED 123..150
FT /evidence="ECO:0000255"
FT BINDING 262
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 264
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 281
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 284
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 364
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 372
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT VAR_SEQ 384..433
FT /note="SLVKFLTPTSGLQGYWDPYPIDMEFKPPCIVLSTIGISKPGKLEGKSTQQ
FT -> RFLLTLITLFSAKMKLGLSFLFLVLQFGEVFNTYLGSPRILGSISNRYGI (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017071"
FT VAR_SEQ 434..536
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_017072"
FT VAR_SEQ 484..511
FT /note="LNEDLRLVLGQQERMLNGANIWNLPVAY -> KVHHKWIDHLQPSSQSCFLS
FT YRFYISRS (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017073"
FT VAR_SEQ 512..536
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017074"
FT MUTAGEN 97..106
FT /note="Missing: Increased stability of the protein."
FT /evidence="ECO:0000269|PubMed:19843523"
FT MUTAGEN 274
FT /note="V->E: In chl-2; reduced level of chlorophyll b."
FT MUTAGEN 334..335
FT /note="SL->VA: In chl-3; reduced level of chlorophyll b."
FT MUTAGEN 336..375
FT /note="Missing: In chl-3; absence of chlorophyll b."
FT CONFLICT 115
FT /note="P -> R (in Ref. 2; AAD54323)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="L -> F (in Ref. 1; BAA82484)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="Y -> C (in Ref. 1; BAA82484)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 536 AA; 60331 MW; E28640DB19F8C3FB CRC64;
MNAAVFSPSA LSLPISFSKT RSSFLSRKKG VKGEFRVFAV FGDESGLVEK KSQWRPLFDV
EDPRSKAPPY KGKFLDVNQA IEVARFDIQY LDWRARQDLL TIMILHDKVV DVLNPLAREY
KSIGTVKKEL AGLQEELSKA HQQVHISEAR VSTALDKLAH MEELVNDRLL PGRVVTELDK
PSSSTTASAV ELDREKTNTG AKSLNVSGPV PPYSPHLKNF WYPVAFTADL KHDTMVPIEC
FEQPWVIFRG EDGKPGCVRN TCAHRACPLD LGTVNEGRIQ CPYHGWEYST DGECKKMPST
KLLKVKIKSL PCLEQEGMIW IWPGDEPPAP ILPSLQPPSG FLIHAELVMD LPVEHGLLLD
NLLDLAHAPF THTSTFAKGW SVPSLVKFLT PTSGLQGYWD PYPIDMEFKP PCIVLSTIGI
SKPGKLEGKS TQQCATHLHQ LHVCLPSSKN KTRLLYRMSL DFAPILKNLP FMEHLWRHFA
EQVLNEDLRL VLGQQERMLN GANIWNLPVA YDKLGVRYRL WRNAVDRGDD KLPFSG
