ID   ACSF_GRATL              Reviewed;         349 AA.
AC   Q6B8U1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase {ECO:0000255|HAMAP-Rule:MF_01840};
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase {ECO:0000255|HAMAP-Rule:MF_01840};
DE            EC=1.14.13.81 {ECO:0000255|HAMAP-Rule:MF_01840};
GN   Name=acsF {ECO:0000255|HAMAP-Rule:MF_01840}; Synonyms=ycf59;
GN   OrderedLocusNames=Grc000113;
OS   Gracilaria tenuistipitata var. liui (Red alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gracilariales;
OC   Gracilariaceae; Agarophyton; Agarophyton tenuistipitatum.
OX   NCBI_TaxID=285951;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15638458; DOI=10.1007/s00239-004-2638-3;
RA   Hagopian J.C., Reis M., Kitajima J.P., Bhattacharya D., de Oliveira M.C.;
RT   "Comparative analysis of the complete plastid genome sequence of the red
RT   alga Gracilaria tenuistipitata var. liui provides insights into the
RT   evolution of rhodoplasts and their relationship to other plastids.";
RL   J. Mol. Evol. 59:464-477(2004).
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:0000255|HAMAP-Rule:MF_01840}.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_01840};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01840};
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll
CC       biosynthesis (light-independent). {ECO:0000255|HAMAP-Rule:MF_01840}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01840}.
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DR   EMBL; AY673996; AAT79694.1; -; Genomic_DNA.
DR   RefSeq; YP_063619.1; NC_006137.1.
DR   AlphaFoldDB; Q6B8U1; -.
DR   GeneID; 2943992; -.
DR   UniPathway; UPA00670; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl ester (oxidative) cyclase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Chlorophyll biosynthesis; Chloroplast; Iron; Metal-binding; NADP;
KW   Oxidoreductase; Photosynthesis; Plastid.
FT   CHAIN           1..349
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase"
FT                   /id="PRO_0000217543"
SQ   SEQUENCE   349 AA;  41494 MW;  B383F9E9614DD7EE CRC64;
     MSTSQNLSQT PVKETLLTPR FYTTDFDEMS KLDISSNIDE FEALLQEFRA DYNRQHFIRD
     QEFEQSWNNL DSGTKALFVE FLERSCTAEF SGFLLYKELS RKLDKSNPVI AECFLLMSRD
     EARHAGFLNK AMSDFNLSLD LGFLTKSRKY TFFAPKFIFY ATYLSEKIGY WRYITIYRHL
     EKHPEHRIYP IFKFFENWCQ DENRHGDFFA ALLKSQPQLL NNLEARLWCR FFLLSVFATM
     YLNDFQRSNF YKSIGLDARQ YDMQVIRKTN ESASRIFPVA LNVDQPKFFQ YLDQCAVENK
     KLIEIDQKYN NWFIKKLIKM PIYIKLCSCL IKLYLLPAIP SAHVVSTIR