ID   CAO_DUNSA               Reviewed;         463 AA.
AC   Q9XJ38;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 77.
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;
OS   Dunaliella salina (Green alga) (Protococcus salinus).
OC   Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC   CS clade; Chlamydomonadales; Dunaliellaceae; Dunaliella.
OX   NCBI_TaxID=3046;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 inner membrane; Peripheral
CC       membrane protein. Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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DR   EMBL; AB021312; BAA82481.1; -; mRNA.
DR   AlphaFoldDB; Q9XJ38; -.
DR   SMR; Q9XJ38; -.
DR   BRENDA; 1.14.13.122; 2018.
DR   GO; GO:0009706; C:chloroplast inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010277; F:chlorophyllide a oxygenase [overall] activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
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   Pfam; PF08417; PaO; 1.
DR   Pfam; PF00355; Rieske; 1.
DR   SUPFAM; SSF50022; SSF50022; 1.
DR   PROSITE; PS51296; RIESKE; 1.
PE   2: Evidence at transcript level;
KW   2Fe-2S; Chlorophyll biosynthesis; Chloroplast; Coiled coil; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; NADP; Oxidoreductase; Plastid;
KW   Plastid inner membrane; Thylakoid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..463
FT                   /note="Chlorophyllide a oxygenase, chloroplastic"
FT                   /id="PRO_0000250165"
FT   DOMAIN          134..235
FT                   /note="Rieske"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1..51
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        88..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         175
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         177
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         194
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         197
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT   BINDING         275
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         282
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   463 AA;  51532 MW;  FD37B01A3667DAAE CRC64;
     MQSKLLGLQD EISEARDKLR TSEARVAQNL KRVDELKAEA ASLERMRLAS SSSTDSTVSI
     ASRGGAAVAA TTSVPDHVER EGIQSRVRGS GMASTSYPSH VPQPSQAVRR GPKPKDSRRL
     RSSLELEDGL RNFWYPTEFA KKLEPGMMVP FDLFGVPWVL FRDEHSAPTC IKDSCAHRAC
     PLSLGKVING HVQCPYHGWE FDGSGACTKM PSTRMCHGVG VAALPCVEKD GFVWVWPGDG
     PPPDLPPDFT APPAGYDVHA EIMVDVPVEH GLLMENLLDL AHAPFTHTTT FARGWPIPEA
     VRFHATKMLA GDWDPYPISM SFNPPCIALS TIGLSQPGKI MRGYKAEECK RHLHQLHVCM
     PSKEGHTRLL YRMSLDFWGW AKHVPFVDVL WKKIAGQVLG EDLVLVLGQQ ARMIGGDDTW
     CTPMPYDKLA VRYRRWRNMV ADGEYEEGSR NRCTSQYDSW PDV