ID   ACSF2_THEVB             Reviewed;         354 AA.
AC   Q8DI68;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2 {ECO:0000255|HAMAP-Rule:MF_01840};
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 2 {ECO:0000255|HAMAP-Rule:MF_01840};
DE            EC=1.14.13.81 {ECO:0000255|HAMAP-Rule:MF_01840};
GN   Name=acsF2 {ECO:0000255|HAMAP-Rule:MF_01840}; OrderedLocusNames=tlr1722;
OS   Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC   Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC   Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX   PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA   Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA   Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA   Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the thermophilic cyanobacterium
RT   Thermosynechococcus elongatus BP-1.";
RL   DNA Res. 9:123-130(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: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; BA000039; BAC09274.1; -; Genomic_DNA.
DR   RefSeq; NP_682512.1; NC_004113.1.
DR   RefSeq; WP_011057559.1; NC_004113.1.
DR   AlphaFoldDB; Q8DI68; -.
DR   STRING; 197221.22295448; -.
DR   EnsemblBacteria; BAC09274; BAC09274; BAC09274.
DR   KEGG; tel:tlr1722; -.
DR   PATRIC; fig|197221.4.peg.1803; -.
DR   eggNOG; COG1633; Bacteria.
DR   OMA; ENRHGDC; -.
DR   OrthoDB; 366541at2; -.
DR   UniPathway; UPA00670; -.
DR   Proteomes; UP000000440; 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   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; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Magnesium-protoporphyrin IX monomethyl ester
FT                   [oxidative] cyclase 2"
FT                   /id="PRO_0000217536"
SQ   SEQUENCE   354 AA;  41683 MW;  F341D573D305BCC2 CRC64;
     MVAIAPNPHS GQSVKTIREN LLTPRFYTTD FEQAAKLDLS RQQEQLEAML AEMRADYNRH
     HFVRDDSFKG TWDLLDAQTR KAFIDYLERS CVSEFSGFLL FKELSRKLKD RNPLLAEIFH
     LMARDEARHA GFLNKAMMDF GHAMDLGYLS KTRTYTFFPL PWVLYTVYLS EKIGYWRYII
     IYRHLEKHPE HSFYPLFNYF ERWCQDENRH GDIFKALIHS QPQLIQGWGA KLWMRFFLLT
     VFATHTLTVH ERAKFYEALG LDATAFDREV IAKTNETAAR TFSVVLNVDH PEFYSRLQRC
     VEISNKLQAI EATHQPKWLK ALRKLPHQLA IAGHLLRIYL LPPVNAQQEW GTVH