[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0092-8674(84)90429-X; PubMed=6744416 [NCBI, ExPASy, EBI, Israel, Japan] Youvan D.C., Bylina E.J., Alberti M., Begusch H., Hearst J.E.; "Nucleotide and deduced polypeptide sequences of the photosynthetic reaction-center, B870 antenna, and flanking polypeptides from R. capsulata."; Cell 37:949-957(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19. PubMed=2203738 [NCBI, ExPASy, EBI, Israel, Japan] Yang Z.M., Bauer C.E.; "Rhodobacter capsulatus genes involved in early steps of the bacteriochlorophyll biosynthetic pathway."; J. Bacteriol. 172:5001-5010(1990).
[3]	CHARACTERIZATION. PubMed=8071204 [NCBI, ExPASy, EBI, Israel, Japan] Bollivar D.W., Jiang Z.Y., Bauer C.E., Beale S.I.; "Heterologous expression of the bchM gene product from Rhodobacter capsulatus and demonstration that it encodes S-adenosyl-L-methionine:Mg-protoporphyrin IX methyltransferase."; J. Bacteriol. 176:5290-5296(1994).

Comments

FUNCTION: Converts Mg-protoporphyrin IX to Mg-protoporphyrin IX methylester using S-adenosyl-L-methionine as a cofactor.
CATALYTIC ACTIVITY: S-adenosyl-L-methionine + magnesium protoporphyrin IX = S-adenosyl-L-homocysteine + magnesium protoporphyrin IX 13-methyl ester.
PATHWAY: Porphyrin biosynthesis; bacteriochlorophyll biosynthesis (light-independent).
SIMILARITY: Belongs to the methyltransferase superfamily.
CAUTION: Was originally (Ref.1) thought to be involved in formation of the cyclopentone ring of protochlorophyllide from Mg-protoporphyrin IX monomethyl ester.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z11165; CAA77522.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K01183; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
M34843; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

PIR

A28988; A28988.

3D structure databases

ModBase

P26236.

Ontologies

GO:0046406;	Molecular function: magnesium protoporphyrin IX methyltransferase activity (inferred from electronic annotation from InterPro).
GO:0030494;	Biological process: bacteriochlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0015979;	Biological process: photosynthesis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR010251; BchM_ChlM.
IPR010940; Mg_prot_MeTrfase_C.
Graphical view of domain structure.

Pfam

PF07109; Mg-por_mtran_C; 1.
Pfam graphical view of domain structure.

TIGRFAMs

TIGR02021; BchM-ChlM; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Bacteriochlorophyll biosynthesis; Chlorophyll biosynthesis; Methyltransferase; Photosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 224`	`224`		`Magnesium-protoporphyrin O-methyltransferase.`	`PRO_0000204420`

Sequence information

Length: 224 AA [This is the length of the unprocessed precursor]

Molecular weight: 25225 Da [This is the MW of the unprocessed precursor]

CRC64: B32BB9B3DD3CF9EC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPSDYAEIRN RVEHYFDRTA TRAWARLTTA DEKVSKVRQT VREGRDTMRA VMLSRLPDDL 

        70         80         90        100        110        120 
TGCRVMDAGC GTGLTTVELA RRGADVVAVD ISPQLIDIAK DRLPPELRGK VSFHVGDMAD 

       130        140        150        160        170        180 
PALGQFDYVV AMDSLIYYRA PDIGRVLTEL GKRTHSAIVF TVAPKTAFLM AFWWLGKLFP 

       190        200        210        220 
RSNRSPVMIP HALDKLQRHA GDSLIKIDRV ARGFYISECL EYRP

P26236 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools