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B2T7J6 (DCUP_BURPP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. 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 decarboxylase

Short name=UPD
Short name=URO-D
EC=4.1.1.37
Gene names
Name:hemE
Ordered Locus Names:Bphyt_3890
OrganismBurkholderia phytofirmans (strain DSM 17436 / PsJN) [Complete proteome] [HAMAP]
Taxonomic identifier398527 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderia

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III By similarity. HAMAP MF_00218

Catalytic activity

Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP MF_00218

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP MF_00218

Subunit structure

Homodimer By similarity. HAMAP MF_00218

Subcellular location

Cytoplasm By similarity HAMAP MF_00218.

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processporphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionuroporphyrinogen decarboxylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 366366Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000099977

Regions

Region28 – 325Substrate binding By similarity

Sites

Binding site781Substrate By similarity
Binding site1601Substrate By similarity
Binding site2151Substrate By similarity
Binding site3331Substrate By similarity
Site781Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B2T7J6 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: CB56D9AC7C0D92E7

FASTA36639,949
        10         20         30         40         50         60 
MAHKLLNDTF LRALLRQPTD YTPIWLMRQA GRYLPEYNAT RGRAGSFLGL AKSPAYATEV 

        70         80         90        100        110        120 
TLQPLDRYPL DAAILFSDIL TVPDAMGLGL EFVTGEGPKF VRPVRTEDDV ARLAVPDIDA 

       130        140        150        160        170        180 
TLRYVTDAVR EIRTALTDAQ GRQRVPLIGF SGSPWTLACY MVEGGGSADF RTVKSMLYAR 

       190        200        210        220        230        240 
PDLMHRILDV NARSVAAYLN AQIEAGAQAV MIFDTWGGAL ADGVYQRFSL QYIQQVVSQL 

       250        260        270        280        290        300 
KRDHGGEKVP VITFTKGGGL WLDEIAETGV DAVGLDWTVN LSKARERVGG KVALQGNIDP 

       310        320        330        340        350        360 
SVLFAPPASI RMEARAVLDS FGNHPGHVFN LGHGISQFTP PENVAELVDE VHRHSRAIRS 


GAHAPA 

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References

[1]"Complete sequence of chromosome 1 of Burkholderia phytofirmans PsJN."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Nowak J., Sessitsch A., Lazarovits G., Compant S., Barka E., Tiedje J.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17436 / PsJN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001052 Genomic DNA. Translation: ACD18277.1.
RefSeqYP_001897501.1. NC_010681.1.

3D structure databases

ProteinModelPortalB2T7J6.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2T7J6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6282408.
GenomeReviewsGene locus Bphyt_3890 in contig CP001052_GR.
KEGGbpy:Bphyt_3890.
PATRIC19218405. VBIBurPhy117947_7932.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Family and domain databases

HAMAPMF_00218. URO-D.
[Tree]
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
KOK01599.
PANTHERPTHR21091:SF2. HemE. 1 hit.
PfamPF01208. URO-D. 1 hit.
[Graphical view]
TIGRFAMsTIGR01464. HemE. 1 hit.
PROSITEPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCUP_BURPP
AccessionPrimary (citable) accession number: B2T7J6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families