ID   ACSF_TRIEI              Reviewed;         358 AA.
AC   Q118B4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
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}; OrderedLocusNames=Tery_0728;
OS   Trichodesmium erythraeum (strain IMS101).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Microcoleaceae; Trichodesmium.
OX   NCBI_TaxID=203124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMS101;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Richardson P.;
RT   "Complete sequence of Trichodesmium erythraeum IMS101.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the AcsF family. {ECO:0000255|HAMAP-
CC       Rule:MF_01840}.
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DR   EMBL; CP000393; ABG50160.1; -; Genomic_DNA.
DR   RefSeq; WP_011610553.1; NC_008312.1.
DR   AlphaFoldDB; Q118B4; -.
DR   STRING; 203124.Tery_0728; -.
DR   PRIDE; Q118B4; -.
DR   EnsemblBacteria; ABG50160; ABG50160; Tery_0728.
DR   KEGG; ter:Tery_0728; -.
DR   eggNOG; COG1633; Bacteria.
DR   HOGENOM; CLU_048037_0_0_3; -.
DR   OMA; FHPIFKW; -.
DR   OrthoDB; 366541at2; -.
DR   UniPathway; UPA00670; -.
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; Iron; Metal-binding; NADP; Oxidoreductase;
KW   Photosynthesis.
FT   CHAIN           1..358
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase"
FT                   /id="PRO_1000070557"
SQ   SEQUENCE   358 AA;  42736 MW;  BB0CF4E843525765 CRC64;
     MVNSLKKQTF TEMRPGVKVP AKETILTPRF YTTDFDEMAK MDISVNEDEL MAILEEFRAD
     YNRHHFVRNE EFAQSWDHID GETRRLFVEF LERSCTAEFS GFLLYKELGR RLKNKSPILA
     ECFTLMSRDE ARHAGFLNKA MSDFNLSLDL GFLTKSRKYT FFKPKFIFYA TYLSEKIGYW
     RYITIYRHLE AHPEDRIYPI FRFFENWCQD ENRHGDFFDA IMRARPEFLN DWQAKLWCRF
     FLLSVFATMY LNDIQRADFY ASIGLNACDY DKYVIEKTNE TSGRVFPVIL DVENPEFYAR
     LEFCIKNNEK LTKIANSNNP GFVKFFQKFP LYLSNGWQFL KLYLMKPIET ATMQSSVR