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P21631 (SUMT_PSEDE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismPseudomonas denitrificans
Taxonomic identifier43306 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length280 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the methylation of both 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

Homodimer. Ref.3

Sequence similarities

Belongs to the precorrin methyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=6.3 µM for S-adenosyl-L-methionine Ref.3

KM=1.0 µM for uroporphyrinogen III

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 280280Uroporphyrinogen-III C-methyltransferase
PRO_0000150372

Regions

Region1 – 248248Uroporphyrinogen-III C-methyltransferase
Region100 – 1023S-adenosyl-L-methionine binding

Sites

Binding site241S-adenosyl-L-methionine; via carbonyl oxygen
Binding site1301S-adenosyl-L-methionine
Binding site1841S-adenosyl-L-methionine; via amide nitrogen

Experimental info

Mutagenesis471D → N: Reduces S-adenosyl-L-methionine binding by about 75%. Causes accumulation of precorrin-1. Ref.3
Mutagenesis491L → A: Reduces S-adenosyl-L-methionine binding by about 50%. Causes slow synthesis of precorrin-2 and accumulation of precorrin-1. Ref.3
Mutagenesis1061F → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. Ref.3
Mutagenesis1301T → A: Strongly reduces S-adenosyl-L-methionine binding. Causes slow synthesis of precorrin-2. Ref.3
Mutagenesis1831Y → A: Strongly reduces S-adenosyl-L-methionine binding. Loss of activity. Ref.3
Mutagenesis1841M → A: Strongly reduces S-adenosyl-L-methionine binding. Causes drastic effects on enzyme activity. Ref.3

Secondary structure

................................................. 280
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21631 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 3D593C535CF0610E

FASTA28029,253
        10         20         30         40         50         60 
MIDDLFAGLP ALEKGSVWLV GAGPGDPGLL TLHAANALRQ ADVIVHDALV NEDCLKLARP 

        70         80         90        100        110        120 
GAVLEFAGKR GGKPSPKQRD ISLRLVELAR AGNRVLRLKG GDPFVFGRGG EEALTLVEHQ 

       130        140        150        160        170        180 
VPFRIVPGIT AGIGGLAYAG IPVTHREVNH AVTFLTGHDS SGLVPDRINW QGIASGSPVI 

       190        200        210        220        230        240 
VMYMAMKHIG AITANLIAGG RSPDEPVAFV CNAATPQQAV LETTLARAEA DVAAAGLEPP 

       250        260        270        280 
AIVVVGEVVR LRAALDWIGA LDGRKLAADP FANRILRNPA 

« Hide

References

[1]"Nucleotide sequence of a Pseudomonas denitrificans 5.4-kilobase DNA fragment containing five cob genes and identification of structural genes encoding S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase and cobyrinic acid a,c-diamide synthase."
Crouzet J., Cauchois L., Blanche F., Debussche L., Thibaut D., Rouyez M.-C., Rigault S., Mayaux J.-F., Cameron B.
J. Bacteriol. 172:5968-5979(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: SC510.
[2]"Purification and characterization of S-adenosyl-L-methionine: uroporphyrinogen III methyltransferase from Pseudomonas denitrificans."
Blanche F., Debussche L., Thibaut D., Crouzet J., Cameron B.
J. Bacteriol. 171:4222-4231(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[3]"Structure/function studies on a S-adenosyl-L-methionine-dependent uroporphyrinogen III C methyltransferase (SUMT), a key regulatory enzyme of tetrapyrrole biosynthesis."
Vevodova J., Graham R.M., Raux E., Schubert H.L., Roper D.I., Brindley A.A., Ian Scott A., Roessner C.A., Stamford N.P.J., Stroupe M.E., Getzoff E.D., Warren M.J., Wilson K.S.
J. Mol. Biol. 344:419-433(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF APOPROTEIN IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, SUBUNIT, KINETIC PARAMETERS, MUTAGENESIS OF ASP-47; LEU-49; PHE-106; THR-130; TYR-183 AND MET-184.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M59236 Genomic DNA. Translation: AAA25773.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S4DX-ray2.70A/B/D/E/F/G/H/I/J/K/L/M1-280[»]
ProteinModelPortalP21631.
SMRP21631. Positions 4-270.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-82.
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...

Other

EvolutionaryTraceP21631.

Entry information

Entry nameSUMT_PSEDE
AccessionPrimary (citable) accession number: P21631
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: October 16, 2013
This is version 77 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways