ID ACSF_RHOPS Reviewed; 367 AA. AC Q132P2; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 1. DT 04-NOV-2008, entry version 17. DE RecName: Full=Aerobic magnesium-protoporphyrin IX monomethyl ester [oxidative] cyclase; DE Short=Aerobic Mg-protoporphyrin IX monomethyl ester oxidative cyclase; DE EC=1.14.13.81; GN Name=acsF; OrderedLocusNames=RPD_3726; OS Rhodopseudomonas palustris (strain BisB5). OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bradyrhizobiaceae; Rhodopseudomonas. OX NCBI_TaxID=316057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N., RA Lykidis A., Oda Y., Harwood C.S., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris BisB5."; RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases. 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; bacteriochlorophyll biosynthesis CC (light-independent). CC -!- SIMILARITY: Belongs to the acsF family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000283; ABE40947.1; -; Genomic_DNA. DR RefSeq; YP_570848.1; -. DR GeneID; 4024242; -. DR GenomeReviews; CP000283_GR; RPD_3726. DR KEGG; rpd:RPD_3726; -. DR HOGENOM; Q132P2; -. DR BioCyc; RPAL316057:RPD_3726-MON; -. 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:0030494; P:bacteriochlorophyll 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; IPR012347; Ferritin_rel. DR InterPro; IPR003251; Rubrerythrin. DR Gene3D; G3DSA:1.20.1260.10; Ferritin_rel; 1. DR Pfam; PF02915; Rubrerythrin; 1. DR TIGRFAMs; TIGR02029; AcsF; 1. PE 3: Inferred from homology; KW Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; KW Complete proteome; Iron; Metal-binding; NADP; Oxidoreductase; KW Photosynthesis. FT CHAIN 1 367 Aerobic magnesium-protoporphyrin IX FT monomethyl ester [oxidative] cyclase. FT /FTId=PRO_1000070551. SQ SEQUENCE 367 AA; 42709 MW; 67A5DB88D338C05E CRC64; MIPMEGGAQG ALRTNSRPAI KGSVDSLNIA KEDTILTPRF YTTDYAAMDK LDVSLVRSEW NAMMNEMRAD YNKAHFKKTD EFLESDLDKL PPELLIEFKD FLVSSLTAEF SGCVLYSEIK KRIKNPEIRE LFGLLSRDEA RHAGFINEIL KDHGIGVDLS FLTKVKKYTY FRPKFIFYAT YLSEKIGYAR YITIYRQMER HPERRFHPIF KWFERWCNDE FRHGEAFALL MRADPSLLRG VNKLWIRFFL LAVFATMYVR DHMRPAFYDA LGVDATDYDM QVFRVTTEIS KQVFPVMINL DDPRFLAGLE RLRKVSEKIA ESRSQGFVGK LKRPLYAASA AIAFGRLFLL PAKRNELPRV IGLRPAW //