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Q51701 (NIRE_PARDP) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 76. 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:nirE
Ordered Locus Names:Pden_2488
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. Inactivation of uroporphyrinogen-III methyltransferase results in the loss of nitrite and nitric oxide reductase activities, but not of nitrous oxide reductase activity. Likely involved in heme D1 biosynthesis.

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

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

Sequence similarities

Belongs to the precorrin methyltransferase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processsiroheme biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionprecorrin-2 dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

uroporphyrin-III C-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Uroporphyrinogen-III C-methyltransferase
PRO_0000150385

Regions

Region116 – 1183S-adenosyl-L-methionine binding By similarity

Sites

Binding site401S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1461S-adenosyl-L-methionine By similarity
Binding site1991S-adenosyl-L-methionine; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q51701 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AA319E29BAC6C461

FASTA28730,029
        10         20         30         40         50         60 
MAGKTVTNGA AQGKAARSGA DGAVRGKAGM GRVDLIGAGP GDPELLTLRA LRLLQQADVV 

        70         80         90        100        110        120 
VHDRLVSDEV MACIPAHVRR IPVGKAAGFH PVPQEQINAL LVELGLSGLT VARLKGGDPT 

       130        140        150        160        170        180 
IFGRGGEEFE AVTRAGIPCD YVPGITAAQG AAVSARFPLT HRGLATGLRH VTGHRARDAA 

       190        200        210        220        230        240 
LDLDWASLAD PQTTLAIYMG AANMAEIARE LIRHGMPADL PVLAVSQAST PQEQRLHATL 

       250        260        270        280 
QDIAAALARK PLPAPVLFIV GHVAAMAEDC ALPQELYRPE WRLVAHG 

« Hide

References

« Hide 'large scale' references
[1]"Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans."
de Boer A.P.N., Reijnders W.N.M., Kuenen J.G., Stouthamer A.H., van Spanning R.J.M.
Antonie Van Leeuwenhoek 66:111-127(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05002 Genomic DNA. Translation: AAA93119.1.
CP000489 Genomic DNA. Translation: ABL70575.1.
RefSeqYP_916271.1. NC_008686.1.

3D structure databases

ProteinModelPortalQ51701.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_2488.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL70575; ABL70575; Pden_2488.
GeneID4580126.
KEGGpde:Pden_2488.
PATRIC22856097. VBIParDen97112_2413.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0007.
HOGENOMHOG000290519.
KOK02303.
OMASESWTAS.
OrthoDBEOG6DRPFR.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-2529-MONOMER.
UniPathwayUPA00262; 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 nameNIRE_PARDP
AccessionPrimary (citable) accession number: Q51701
Secondary accession number(s): A1B4Y1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 13, 2013
This is version 76 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