ID   ACSF1_THEEB             Reviewed;         380 AA.
AC   Q8DJ05;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   16-JUN-2009, entry version 42.
DE   RecName: Full=Magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase 1;
DE            Short=Mg-protoporphyrin IX monomethyl ester oxidative cyclase 1;
DE            EC=1.14.13.81;
GN   Name=acsF1; OrderedLocusNames=tlr1426;
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; BAC08978.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_682216.1; -.
DR   GeneID; 1011675; -.
DR   GenomeReviews; BA000039_GR; tlr1426.
DR   KEGG; tel:tlr1426; -.
DR   NMPDR; fig|197221.1.peg.1425; -.
DR   HOGENOM; Q8DJ05; -.
DR   BioCyc; TELO197221:TLR1426-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    380       Magnesium-protoporphyrin IX monomethyl
FT                                ester [oxidative] cyclase 1.
FT                                /FTId=PRO_0000217535.
SQ   SEQUENCE   380 AA;  45481 MW;  86C8DC83BBDFAF73 CRC64;
     MVNTVAKPEF EELRPGIKAP AKETILTPRF YTTDFEAMAN MDITENKAEL EAILEEFRCD
     YNRHHFVRDE EFEQSWDHID GETRRLFIEF LERSCTAEFS GFLLYKELSR RLKDRNPLLA
     ECFALMSRDE ARHAGFLNKA MADFNLSLDL GFLTQHRSYT YFEPEFIFYA TYLSEKIGYW
     RYITIYRHLE KHPEHRIYPI FRFFENWCQD ENRHGDFFDA VMRAQPQMLD RPRTFWQKIK
     EIPLSLSGKK WARYFMVCWV PPKLWCRFFL LSVFATMYLN DLQRAKFYTA LGLDAREYDR
     EVIAKTNETA GRVFPVILDV DHPEFYQRLE RCVENNAKLT EIAKQNGGFL KKLPLYLSNV
     WQMIKLFLIP AKEPTRVAVR
//