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Protein

Uroporphyrinogen-III C-methyltransferase

Gene

cobA

Organism
Bacillus megaterium
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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 activityi

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:iadenosylcobalamin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.
Proteins known to be involved in this subpathway in this organism are:
  1. Uroporphyrinogen-III C-methyltransferase (cobA)
This subpathway is part of the pathway adenosylcobalamin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway adenosylcobalamin biosynthesis and in Cofactor biosynthesis.

Pathway:isiroheme biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes precorrin-2 from uroporphyrinogen III.
Proteins known to be involved in this subpathway in this organism are:
  1. Uroporphyrinogen-III C-methyltransferase (cobA)
This subpathway is part of the pathway siroheme biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes precorrin-2 from uroporphyrinogen III, the pathway siroheme biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei11 – 111S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei117 – 1171S-adenosyl-L-methionineBy similarity
Binding sitei170 – 1701S-adenosyl-L-methionine; via amide nitrogenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cobalamin biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00148; UER00211.
UPA00262; UER00211.

Names & Taxonomyi

Protein namesi
Recommended name:
Uroporphyrinogen-III C-methyltransferase (EC:2.1.1.107)
Short name:
Urogen III methylase
Alternative name(s):
SUMT
Uroporphyrinogen III methylase
Short name:
UROM
Gene namesi
Name:cobA
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 238238Uroporphyrinogen-III C-methyltransferasePRO_0000150369Add
BLAST

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

STRINGi545693.BMQ_4928.

Structurei

3D structure databases

ProteinModelPortaliP29928.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni87 – 893S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Belongs to the precorrin methyltransferase family.Curated

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
PROSITEiPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29928-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKVYLVGAG PGDPDLITLK GLKAIQQADV ILYDRLVNKD LLEYAKSDAD
60 70 80 90 100
IIYCGKLPNY HTLKQETINN FLVKFAKKGK IVTRLKGGDP FVFGRGGEEA
110 120 130 140 150
EALVQQGISF EIVPGITSGI AAAAYAGIPV THREYSASFA FVAGHRKDSK
160 170 180 190 200
HDAIKWDSLA KGVDTLAIYM GVRNLPYICQ QLMKHGKTSA TPIALIHWGT
210 220 230
CADQRTVTGT LGTIVDIVKE EQIENPSMII VGEVVNFS
Length:238
Mass (Da):25,822
Last modified:April 1, 1993 - v1
Checksum:i97993B56C894F307
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62881 Genomic DNA. Translation: AAA22317.1.
PIRiA42479.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62881 Genomic DNA. Translation: AAA22317.1.
PIRiA42479.

3D structure databases

ProteinModelPortaliP29928.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi545693.BMQ_4928.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00148; UER00211.
UPA00262; UER00211.

Family and domain databases

Gene3Di3.30.950.10. 1 hit.
3.40.1010.10. 1 hit.
InterProiIPR000878. 4pyrrol_Mease.
IPR014777. 4pyrrole_Mease_sub1.
IPR014776. 4pyrrole_Mease_sub2.
IPR006366. CobA/CysG_C.
IPR003043. Uropor_MeTrfase_CS.
[Graphical view]
PfamiPF00590. TP_methylase. 1 hit.
[Graphical view]
SUPFAMiSSF53790. SSF53790. 1 hit.
TIGRFAMsiTIGR01469. cobA_cysG_Cterm. 1 hit.
PROSITEiPS00839. SUMT_1. 1 hit.
PS00840. SUMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiSUMT_BACME
AccessioniPrimary (citable) accession number: P29928
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: June 24, 2015
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.