Skip Header

Contribute Send feedback
Read comments (?) or add your own

A0PT34 (DCUP_MYCUA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 37. 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
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:MUL_3312
OrganismMycobacterium ulcerans (strain Agy99) [Complete proteome] [HAMAP]
Taxonomic identifier362242 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length353 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 – 353353Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000023925

Regions

Region30 – 345Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3321Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A0PT34 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 43518760BC754FE2

FASTA35337,550
        10         20         30         40         50         60 
MSTRRDLPQS PYLAAVAGRK PSRVPVWFMR QAGRSLPEYR ALRRQHSMLA ACFEPEVACE 

        70         80         90        100        110        120 
VTMQPIRRYH VDAAILFSDI VVPLRAAGVD LDIVADVGPV IAAPVRTVAD VDAIKPIDSQ 

       130        140        150        160        170        180 
SIAPVLDAVE LLVAELGDTP LIGFAGAPFT LASYLVEGGP SRHHARTKAM MLAEPATWHA 

       190        200        210        220        230        240 
LMTKLTDLTI EFLLGQIRAG VDAIQVFDSW AGMLSLADYR QYALPHSARV FATLAEHGVP 

       250        260        270        280        290        300 
MTHFGVGTAE LLGAMSEAVK PGTAKVVGVD WRTALADAAA RVQPGTALQG NLDPVVLLAG 

       310        320        330        340        350 
WPAVERAARA VVDDGRRAVD AGAAGYVFNL GHGVLPQTDP GVLTDLVSLV HSL

« Hide

References

[1]"Reductive evolution and niche adaptation inferred from the genome of Mycobacterium ulcerans, the causative agent of Buruli ulcer."
Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M. expand/collapse author list , Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.
Genome Res. 17:192-200(2007) [PubMed: 17210928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Agy99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000325 Genomic DNA. Translation: ABL05503.1.
RefSeqYP_906974.1. NC_008611.1.

3D structure databases

ProteinModelPortalA0PT34.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0PT34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000073447; EBMYCP00000071452; EBMYCG00000073442.
GeneID4554326.
GenomeReviewsGene locus MUL_3312 in contig CP000325_GR.
KEGGmul:MUL_3312.
PATRIC18174050. VBIMycUlc37413_3852.

Organism-specific databases

GenoListMUL_3312.
CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
GeneTreeEBGT00050000016469.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBA0PT34.
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_MYCUA
AccessionPrimary (citable) accession number: A0PT34
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 37 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents