ID   CTH1_CHLRE              Reviewed;         407 AA.
AC   Q9AR22; Q944P4;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2, chloroplastic;
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 2;
DE            EC=1.14.13.81;
DE   AltName: Full=Copper target homolog 1 protein;
DE   Flags: Precursor;
GN   Name=CTH1;
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 [GENOMIC DNA / MRNA], FUNCTION, AND INDUCTION.
RX   PubMed=11910013; DOI=10.1105/tpc.010420;
RA   Moseley J.L., Page M.D., Alder N.P., Eriksson M., Quinn J., Soto F.,
RA   Theg S.M., Hippler M., Merchant S.;
RT   "Reciprocal expression of two candidate di-iron enzymes affecting
RT   photosystem I and light-harvesting complex accumulation.";
RL   Plant Cell 14:673-688(2002).
CC   -!- FUNCTION: Catalyzes the formation of the isocyclic ring in chlorophyll
CC       biosynthesis. Mediates the cyclase reaction, which results in the
CC       formation of divinylprotochlorophyllide (Pchlide) characteristic of all
CC       chlorophylls from magnesium-protoporphyrin IX 13-monomethyl ester
CC       (MgPMME). {ECO:0000269|PubMed:11910013}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H(+) + Mg-protoporphyrin IX 13-monomethyl ester + 3 NADPH +
CC         3 O2 = 3,8-divinyl protochlorophyllide a + 5 H2O + 3 NADP(+);
CC         Xref=Rhea:RHEA:33235, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58632, ChEBI:CHEBI:60491; EC=1.14.13.81;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- INDUCTION: By Copper and oxygen. {ECO:0000269|PubMed:11910013}.
CC   -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000305}.
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DR   EMBL; AF337037; AAK32149.1; -; mRNA.
DR   EMBL; AF426027; AAL14712.2; -; mRNA.
DR   EMBL; AF337038; AAK32150.1; -; Genomic_DNA.
DR   RefSeq; XP_001691047.1; XM_001690995.1.
DR   RefSeq; XP_001691048.1; XM_001690996.1.
DR   AlphaFoldDB; Q9AR22; -.
DR   STRING; 3055.EDP05494; -.
DR   EnsemblPlants; PNW74783; PNW74783; CHLRE_12g510050v5.
DR   GeneID; 5716556; -.
DR   Gramene; PNW74783; PNW74783; CHLRE_12g510050v5.
DR   KEGG; cre:CHLRE_12g510050v5; -.
DR   eggNOG; ENOG502QRIH; Eukaryota.
DR   HOGENOM; CLU_048037_0_0_1; -.
DR   OrthoDB; 930662at2759; -.
DR   BRENDA; 1.14.13.81; 1318.
DR   UniPathway; UPA00668; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   CDD; cd01047; ACSF; 1.
DR   HAMAP; MF_01840; AcsF; 1.
DR   InterPro; IPR008434; AcsF.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR003251; Rubrerythrin.
DR   PANTHER; PTHR31053; PTHR31053; 1.
DR   Pfam; PF02915; Rubrerythrin; 1.
DR   SUPFAM; SSF47240; SSF47240; 1.
DR   TIGRFAMs; TIGR02029; AcsF; 1.
PE   2: Evidence at transcript level;
KW   Chlorophyll biosynthesis; Chloroplast; Iron; Metal-binding; NADP;
KW   Oxidoreductase; Photosynthesis; Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..407
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase 2, chloroplastic"
FT                   /id="PRO_0000000600"
FT   CONFLICT        18
FT                   /note="P -> L (in Ref. 1; AAL14712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        38
FT                   /note="A -> V (in Ref. 1; AAL14712)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        356
FT                   /note="N -> D (in Ref. 1; AAL14712)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  47482 MW;  4C3A2920C158AA50 CRC64;
     MATMLNKRVT GAFGKQAPVR SARVAAVRPS RSSVRVAATA APQEVEGFKV MRDGIKVASD
     ETLLTPRFYT TDFDEMERLF SLELNKNMDM EEFEAMLNEF KLDYNQRHFV RNETFKEAAE
     KIQGPTRKIF IEFLERSCTA EFSGFLLYKE LGRRLKATNP VVAEIFTLMS RDEARHAGFL
     NKAMSDFNLA LDLGFLTKNR KYTFFKPKFI FYATYLSEKI GYWRYISIYR HLQRNPDNQL
     YPLFEYFENW CQDENRHGDF FTAVLKARPE MVNDWAAKLW SRFFCLSVYI TMYLNDHQRD
     AFYSSLGLNT TQFNQHVIIE TNKSTERIFP AVPDVENPEF FRRMDLLVKY NAQLVNIGSM
     NLPSPIKAIM KAPILERMVA EVFQVFIMTP KESGSYDLDA NKTALVY