ID   ACSF2_THEEB             Reviewed;         354 AA.
AC   Q8DI68;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 43.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 2;
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 2;
DE            EC=1.14.13.81;
GN   Name=acsF2; OrderedLocusNames=tlr1722;
OS   Thermosynechococcus elongatus (strain BP-1).
OC   Bacteria; Cyanobacteria; Chroococcales; Thermosynechococcus.
OX   NCBI_TaxID=197221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22225144; 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.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
RA   Shimpo S., Sugimoto M., 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
CC       chlorophyll biosynthesis. Mediates the cyclase reaction, which
CC       results in the formation of divinylprotochlorophyllide (Pchlide)
CC       characteristic of all chlorophylls from magnesium-protoporphyrin
CC       IX 13-monomethyl ester (MgPMME) (By similarity).
CC   -!- CATALYTIC ACTIVITY: Magnesium-protoporphyrin IX 13-monomethyl
CC       ester + NADPH + O(2) = 13(1)-hydroxy-magnesium-protoporphyrin IX
CC       13-monomethyl ester + NADP(+) + H(2)O.
CC   -!- CATALYTIC ACTIVITY: 13(1)-hydroxy-magnesium-protoporphyrin IX 13-
CC       monomethyl ester + NADPH + O(2) = 13(1)-oxo-magnesium-
CC       protoporphyrin IX 13-monomethyl ester + NADP(+) + 2 H(2)O.
CC   -!- CATALYTIC ACTIVITY: 13(1)-oxo-magnesium-protoporphyrin IX 13-
CC       monomethyl ester + NADPH + O(2) = divinylprotochlorophyllide +
CC       NADP(+) + 2 H(2)O.
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- PATHWAY: Porphyrin biosynthesis; chlorophyll biosynthesis (light-
CC       independent).
CC   -!- SIMILARITY: Belongs to the acsF family.
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DR   EMBL; BA000039; BAC09274.1; -; Genomic_DNA.
DR   RefSeq; NP_682512.1; -.
DR   GeneID; 1010584; -.
DR   GenomeReviews; BA000039_GR; tlr1722.
DR   KEGG; tel:tlr1722; -.
DR   NMPDR; fig|197221.1.peg.1721; -.
DR   HOGENOM; Q8DI68; -.
DR   BioCyc; TELO197221:TLR1722-MON; -.
DR   BRENDA; 1.14.13.81; 277225.
DR   GO; GO:0005506; F:iron ion binding; IEA:HAMAP.
DR   GO; GO:0048529; F:magnesium-protoporphyrin IX monomethyl este...; IEA:HAMAP.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0015979; P:photosynthesis; IEA:HAMAP.
DR   HAMAP; MF_01840; -; 1.
DR   InterPro; IPR008434; AcsF.
DR   InterPro; IPR003251; Rubrerythrin.
DR   Pfam; PF02915; Rubrerythrin; 1.
DR   TIGRFAMs; TIGR02029; AcsF; 1.
PE   3: Inferred from homology;
KW   Chlorophyll biosynthesis; Complete proteome; Iron; Metal-binding;
KW   NADP; Oxidoreductase; Photosynthesis.
FT   CHAIN         1    354       Magnesium-protoporphyrin IX monomethyl
FT                                ester [oxidative] cyclase 2.
FT                                /FTId=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
//