CHLM_SYNY3
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 03-AUG-2022, entry version 133.
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; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified 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}.
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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; 1148.1001325; -.
DR PaxDb; Q55467; -.
DR PRIDE; Q55467; -.
DR EnsemblBacteria; BAA10812; BAA10812; BAA10812.
DR KEGG; syn:slr0525; -.
DR eggNOG; COG2227; Bacteria.
DR InParanoid; Q55467; -.
DR OMA; LDVFIHY; -.
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 Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR010251; Mg_prot_MeTrfase.
DR InterPro; IPR010940; Mg_prot_MeTrfase_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF07109; Mg-por_mtran_C; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR02021; BchM-ChlM; 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
