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P29928 (SUMT_BACME) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Uroporphyrinogen-III C-methyltransferase

Short name=Urogen III methylase
EC=2.1.1.107
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name=UROM
Gene names
Name:cobA
OrganismBacillus megaterium
Taxonomic identifier1404 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes both methylations at C-2 and C-7 of uroporphyrinogen III leading to precorrin-1 and precorrin-2; their oxidative esterification gives respectively factor I octamethyl ester and sirohydrochlorin.

Catalytic activity

S-adenosyl-L-methionine + uroporphyrinogen III = S-adenosyl-L-homocysteine + precorrin-1.

S-adenosyl-L-methionine + precorrin-1 = S-adenosyl-L-homocysteine + precorrin-2.

Pathway

Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.

Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.

Subunit structure

Monomer Probable.

Sequence similarities

Belongs to the precorrin methyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Uroporphyrinogen-III C-methyltransferase
PRO_0000150369

Regions

Region87 – 893S-adenosyl-L-methionine binding By similarity

Sites

Binding site111S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1171S-adenosyl-L-methionine By similarity
Binding site1701S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P29928 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 97993B56C894F307

FASTA23825,822
        10         20         30         40         50         60 
MGKVYLVGAG PGDPDLITLK GLKAIQQADV ILYDRLVNKD LLEYAKSDAD IIYCGKLPNY 

        70         80         90        100        110        120 
HTLKQETINN FLVKFAKKGK IVTRLKGGDP FVFGRGGEEA EALVQQGISF EIVPGITSGI 

       130        140        150        160        170        180 
AAAAYAGIPV THREYSASFA FVAGHRKDSK HDAIKWDSLA KGVDTLAIYM GVRNLPYICQ 

       190        200        210        220        230 
QLMKHGKTSA TPIALIHWGT CADQRTVTGT LGTIVDIVKE EQIENPSMII VGEVVNFS 

« Hide

References

[1]"Primary structure, expression in Escherichia coli, and properties of S-adenosyl-L-methionine:uroporphyrinogen III methyltransferase from Bacillus megaterium."
Robin C., Blanche F., Cauchois L., Cameron B., Couder M., Crouzet J.
J. Bacteriol. 173:4893-4896(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10778 / DSM 2894 / NCIMB 8508 / NRRL B-938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62881 Genomic DNA. Translation: AAA22317.1.
PIRA42479.

3D structure databases

ProteinModelPortalP29928.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00148; UER00211.
UPA00262; UER00211.

Family and domain databases

Gene3D3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
InterProIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamPF00590. TP_methylase. 1 hit.
[Graphical view]
SUPFAMSSF53790. SSF53790. 1 hit.
TIGRFAMsTIGR01469. cobA_cysG_Cterm. 1 hit.
PROSITEPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSUMT_BACME
AccessionPrimary (citable) accession number: P29928
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 16, 2013
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways