BCHM_RHOCA
ID BCHM_RHOCA Reviewed; 224 AA.
AC P26236;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Magnesium-protoporphyrin O-methyltransferase;
DE EC=2.1.1.11;
DE AltName: Full=Magnesium-protoporphyrin IX methyltransferase;
GN Name=bchM;
OS Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=1061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6744416; DOI=10.1016/0092-8674(84)90429-x;
RA Youvan D.C., Bylina E.J., Alberti M., Begusch H., Hearst J.E.;
RT "Nucleotide and deduced polypeptide sequences of the photosynthetic
RT reaction-center, B870 antenna, and flanking polypeptides from R.
RT capsulata.";
RL Cell 37:949-957(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RX PubMed=2203738; DOI=10.1128/jb.172.9.5001-5010.1990;
RA Yang Z.M., Bauer C.E.;
RT "Rhodobacter capsulatus genes involved in early steps of the
RT bacteriochlorophyll biosynthetic pathway.";
RL J. Bacteriol. 172:5001-5010(1990).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8071204; DOI=10.1128/jb.176.17.5290-5296.1994;
RA Bollivar D.W., Jiang Z.Y., Bauer C.E., Beale S.I.;
RT "Heterologous expression of the bchM gene product from Rhodobacter
RT capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-
RT protoporphyrin IX methyltransferase.";
RL J. Bacteriol. 176:5290-5296(1994).
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; bacteriochlorophyll
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 -!- CAUTION: Was originally thought to be involved in formation of the
CC cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX
CC monomethyl ester. {ECO:0000305|PubMed:6744416}.
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DR EMBL; Z11165; CAA77522.1; -; Genomic_DNA.
DR EMBL; K01183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M34843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A28988; A28988.
DR RefSeq; WP_013066405.1; NZ_VIBE01000010.1.
DR AlphaFoldDB; P26236; -.
DR SMR; P26236; -.
DR IntAct; P26236; 1.
DR MINT; P26236; -.
DR GeneID; 31489607; -.
DR OMA; LDVFIHY; -.
DR BRENDA; 2.1.1.11; 5381.
DR UniPathway; UPA00671; -.
DR GO; GO:0046406; F:magnesium protoporphyrin IX methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030494; P:bacteriochlorophyll biosynthetic process; IMP:CACAO.
DR GO; GO:0036070; P:light-independent bacteriochlorophyll 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 InterPro; IPR007848; Small_mtfrase_dom.
DR Pfam; PF07109; Mg-por_mtran_C; 1.
DR Pfam; PF05175; MTS; 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 Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis;
KW Methyltransferase; Photosynthesis; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..224
FT /note="Magnesium-protoporphyrin O-methyltransferase"
FT /id="PRO_0000204420"
SQ SEQUENCE 224 AA; 25225 MW; B32BB9B3DD3CF9EC CRC64;
MPSDYAEIRN RVEHYFDRTA TRAWARLTTA DEKVSKVRQT VREGRDTMRA VMLSRLPDDL
TGCRVMDAGC GTGLTTVELA RRGADVVAVD ISPQLIDIAK DRLPPELRGK VSFHVGDMAD
PALGQFDYVV AMDSLIYYRA PDIGRVLTEL GKRTHSAIVF TVAPKTAFLM AFWWLGKLFP
RSNRSPVMIP HALDKLQRHA GDSLIKIDRV ARGFYISECL EYRP