ID   ACSF_PROMP              Reviewed;         390 AA.
AC   Q7V1M1;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=PMM0844;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548174; CAE19303.1; -; Genomic_DNA.
DR   RefSeq; WP_011132478.1; NC_005072.1.
DR   AlphaFoldDB; Q7V1M1; -.
DR   STRING; 59919.PMM0844; -.
DR   EnsemblBacteria; CAE19303; CAE19303; PMM0844.
DR   KEGG; pmm:PMM0844; -.
DR   eggNOG; COG1633; Bacteria.
DR   HOGENOM; CLU_048037_0_0_3; -.
DR   OMA; FHPIFKW; -.
DR   OrthoDB; 366541at2; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000001026; Chromosome.
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   Gene3D; 1.20.1260.10; -; 1.
DR   HAMAP; MF_01840; AcsF; 1.
DR   InterPro; IPR008434; AcsF.
DR   InterPro; IPR012347; Ferritin-like.
DR   InterPro; IPR009078; Ferritin-like_SF.
DR   InterPro; IPR003251; Rubrerythrin.
DR   PANTHER; PTHR31053; PTHR31053; 2.
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..390
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase"
FT                   /id="PRO_0000217532"
SQ   SEQUENCE   390 AA;  45980 MW;  A55456142B4B34BF CRC64;
     MAQQTIESNN KKSVNRGKDI AKDTILTPNF YTTDFEAMEK MDLSINEDEL EAICEEFRKD
     YNRHHFVRNK EFEGAADKID AETRELFVDF LEGSCTSEFS GFLLYKELSK RIKDKNPLLA
     ECFAHMARDE ARHAGFLNKS MNDFGLQLDL GFLTANKDYT YFAPRAIFYA TYISEKIGYW
     RYIAIYRHLE KNPSGKIFPL FNFFENWCQD ENRHGDFFDA LMKAQPRTVK SLSQKIEIFG
     YTLKHPIFDY YHRFRYFLNN HPIVSKLWSR FFLLAVFATM YIRDLGTKRN FYGALGLNAR
     EYDQFVINKT NETSAKVFPV VLNVYDKSFY KRLDRIVENG TRLSEIDKKE NPNVIKVLSK
     LPIFISNGYQ LIRLYLLKPL ESDDFQPSIR