ID CHLM_SYNY3 Reviewed; 230 AA. AC Q55467; Q55344; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Magnesium-protoporphyrin O-methyltransferase; DE EC=2.1.1.11; DE AltName: Full=Magnesium-protoporphyrin IX methyltransferase; GN Name=chlM; OrderedLocusNames=slr0525; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8704138; DOI=10.1007/bf00019561; RA Smith C.A., Suzuki J.Y., Bauer C.E.; RT "Cloning and characterization of the chlorophyll biosynthesis gene chlM RT from Synechocystis PCC 6803 by complementation of a bacteriochlorophyll RT biosynthesis mutant of Rhodobacter capsulatus."; RL Plant Mol. Biol. 30:1307-1314(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). CC -!- FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX CC methylester using S-adenosyl-L-methionine as a cofactor. CC -!- CATALYTIC ACTIVITY: CC Reaction=Mg-protoporphyrin IX + S-adenosyl-L-methionine = Mg- CC protoporphyrin IX 13-monomethyl ester + S-adenosyl-L-homocysteine; CC Xref=Rhea:RHEA:17809, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, CC ChEBI:CHEBI:60491, ChEBI:CHEBI:60492; EC=2.1.1.11; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00889}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; chlorophyll CC biosynthesis (light-independent). CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase CC superfamily. Magnesium protoporphyrin O-methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU00889}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L47126; AAA85380.1; -; Genomic_DNA. DR EMBL; BA000022; BAA10812.1; -; Genomic_DNA. DR PIR; S71781; S71781. DR PDB; 4QDJ; X-ray; 1.60 A; A=1-230. DR PDB; 4QDK; X-ray; 1.70 A; A/B=1-230. DR PDBsum; 4QDJ; -. DR PDBsum; 4QDK; -. DR AlphaFoldDB; Q55467; -. DR SMR; Q55467; -. DR IntAct; Q55467; 4. DR STRING; 1148.gene:10500316; -. DR PaxDb; 1148-1001325; -. DR EnsemblBacteria; BAA10812; BAA10812; BAA10812. DR KEGG; syn:slr0525; -. DR eggNOG; COG2227; Bacteria. DR InParanoid; Q55467; -. DR PhylomeDB; Q55467; -. DR BRENDA; 2.1.1.11; 382. DR SABIO-RK; Q55467; -. DR UniPathway; UPA00670; -. DR Proteomes; UP000001425; Chromosome. DR GO; GO:0046406; F:magnesium protoporphyrin IX methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central. DR GO; GO:0036068; P:light-independent chlorophyll biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW. DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW. DR CDD; cd02440; AdoMet_MTases; 1. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR010251; Mg_prot_MeTrfase. DR InterPro; IPR010940; Mg_prot_MeTrfase_C. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR NCBIfam; TIGR02021; BchM-ChlM; 1. DR Pfam; PF07109; Mg-por_mtran_C; 1. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. DR PROSITE; PS51556; SAM_MT_MG_PIX; 1. PE 1: Evidence at protein level; KW 3D-structure; Chlorophyll biosynthesis; Methyltransferase; Photosynthesis; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1..230 FT /note="Magnesium-protoporphyrin O-methyltransferase" FT /id="PRO_0000204421" FT CONFLICT 190 FT /note="A -> V (in Ref. 1; AAA85380)" FT /evidence="ECO:0000305" FT HELIX 8..16 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 19..27 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 35..58 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 65..69 FT /evidence="ECO:0007829|PDB:4QDJ" FT TURN 72..76 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 77..82 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 86..92 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 94..108 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 137..139 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 142..155 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 156..164 FT /evidence="ECO:0007829|PDB:4QDJ" FT HELIX 169..178 FT /evidence="ECO:0007829|PDB:4QDK" FT HELIX 195..204 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 207..216 FT /evidence="ECO:0007829|PDB:4QDJ" FT STRAND 221..229 FT /evidence="ECO:0007829|PDB:4QDJ" SQ SEQUENCE 230 AA; 25081 MW; 166D72CF3DD178A0 CRC64; MTNAALDDKT IVRDYFNSTG FDRWRRIYGD GQVNFVQKDI RVGHQQTVDS VVAWLVADGN LPGLLVCDAG CGVGSLSIPL AQAGALVYGS DISEKMVGEA QQKAQEVLAY GNQPTFMTQD LAQLGGKYDT VICLDVLIHY PTEEASAMIS HLASLADRRL ILSFAPKTLG LTVLKKIGGL FPGPSKTTRA YQHKEADIRK ILGDNGFSIA RTGMTSTRFY YSRILEAVRS //