CAO_CHLRE
ID CAO_CHLRE Reviewed; 645 AA.
AC Q9ZWM5; Q4VKB8;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 114.
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 Chlamydomonas reinhardtii (Chlamydomonas smithii).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9770552; DOI=10.1073/pnas.95.21.12719;
RA Tanaka A., Ito H., Tanaka R., Tanaka N., Yoshida K., Okada K.;
RT "Chlorophyll a oxygenase (CAO) is involved in chlorophyll b formation from
RT chlorophyll a.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:12719-12723(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=CC-124;
RX PubMed=15849308; DOI=10.1104/pp.104.056069;
RA Lohr M., Im C.-S., Grossman A.R.;
RT "Genome-based examination of chlorophyll and carotenoid biosynthesis in
RT Chlamydomonas reinhardtii.";
RL Plant Physiol. 138:490-515(2005).
RN [3]
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).
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
CC {ECO:0000269|PubMed:15086960}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15086960}. Plastid, chloroplast thylakoid membrane
CC {ECO:0000269|PubMed:15086960}; Peripheral membrane protein
CC {ECO:0000269|PubMed:15086960}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA33964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB015139; BAA33964.1; ALT_FRAME; mRNA.
DR EMBL; AY860816; AAX54904.1; -; mRNA.
DR RefSeq; XP_001690175.1; XM_001690123.1.
DR AlphaFoldDB; Q9ZWM5; -.
DR SMR; Q9ZWM5; -.
DR STRING; 3055.EDP09913; -.
DR EnsemblPlants; PNW88760; PNW88760; CHLRE_01g043350v5.
DR GeneID; 5715613; -.
DR Gramene; PNW88760; PNW88760; CHLRE_01g043350v5.
DR KEGG; cre:CHLRE_01g043350v5; -.
DR eggNOG; ENOG502QS20; Eukaryota.
DR HOGENOM; CLU_027465_1_0_1; -.
DR OMA; TKQCATH; -.
DR OrthoDB; 1199207at2759; -.
DR BRENDA; 1.14.13.122; 1318.
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 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; 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 ?..645
FT /note="Chlorophyllide a oxygenase, chloroplastic"
FT /id="PRO_0000250166"
FT DOMAIN 305..406
FT /note="Rieske"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 105..218
FT /evidence="ECO:0000255"
FT BINDING 346
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 348
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 365
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 368
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00628"
FT BINDING 446
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 450
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 453
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 458
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT CONFLICT 341
FT /note="C -> Y (in Ref. 1; BAA33964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 72106 MW; 4F795BAF7D9213E4 CRC64;
MLPASLQRKA AAVGGRGPTN QSRVAVRVSA QPKEAPPAST PIVEDPESKF RRYGKHFGGI
HKLSMDWLDS VPRVRVRTKD SRQLDDMLEL AVLNERLAGR LEPWQARQKL EYLRKRRKNW
ERIFEYVTRQ DAAATLAMIE EANRKVEESL SEEAREKTAV GDLRDQLESL RAQVAQAQER
LAMTQSRVEQ NLQRVNELKA EATTLERMRK ASDLDIKERE RIAISTVAAK GPASSSSSAA
AVSAPATSAT LTVERPAATT VTQEVPSTSY GTPVDRAPRR SKAAIRRSRG LESSMEIEEG
LRNFWYPAEF SARLPKDTLV PFELFGEPWV MFRDEKGQPS CIRDECAHRG CPLSLGKVVE
GQVMCPYHGW EFNGDGACTK MPSTPFCRNV GVAALPCAEK DGFIWVWPGD GLPAETLPDF
AQPPEGFLIH AEIMVDVPVE HGLLIENLLD LAHAPFTHTS TFARGWPVPD FVKFHANKAL
SGFWDPYPID MAFQPPCMTL STIGLAQPGK IMRGVTASQC KNHLHQLHVC MPSKKGHTRL
LYRMSLDFLP WMRHVPFIDR IWKQVAAQVL GEDLVLVLGQ QDRMLRGGSN WSNPAPYDKL
AVRYRRWRNG VNAEVARVRA GEPPSNPVAM SAGEMFSVDE DDMDN
