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Reviewed, UniProtKB/Swiss-Prot A9HY51 (DCUP_BORPD)

Last modified November 3, 2009. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Uroporphyrinogen decarboxylase
      Short name=URO-D
      Short name=UPD
    EC=4.1.1.37
Gene names
Name: hemE
Ordered Locus Names: Bpet0346
OrganismBordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]
Taxonomic identifier340100 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length358 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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.

Subcellular location

Cytoplasm By similarity.

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 biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionuroporphyrinogen decarboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 358358Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000099974

Regions

Region29 – 335Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1551Substrate By similarity
Binding site2101Substrate By similarity
Binding site3301Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A9HY51-1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: E97E7679AD2FDD31

FASTA35839,043
        10         20         30         40         50         60 
MSAAALKNDV FLRALLRQPV PYTPIWLMRQ AGRYLPEYNA TRARAGSFMG LAQNPDYAAE 

        70         80         90        100        110        120 
VTLQPLARYD LDAAILFSDI LTVPHAMGLG LDFAPGEGPR FARPLRTEDD VARLAVPDME 

       130        140        150        160        170        180 
SLRYVFDAVA VIRRELDGKV PLIGFAGSPW TIACYMVEGR GSDDYRLIKT MLYARPDLLH 

       190        200        210        220        230        240 
RILEVNAQAT LQYLNAQIQA GAQAVMLFDS WGGVLADGLF QQFSLAYTRK VVAGLIREHQ 

       250        260        270        280        290        300 
GRRVPAIVFT KGGGQWLEAI AACGCDAIGL DWTVNLGQAR QRTGDAVALQ GNLDPMTLFG 

       310        320        330        340        350 
GSEAIRAEAR RTLDAFGPVG TGGHVFNLGH GISQYTPPEA VAELVDEVHT YSRALHAK 

« Hide

References

[1]"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae."
Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. expand/collapse author list , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R.
BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AM902716 Genomic DNA. Translation: CAP40678.1.
RefSeqYP_001628949.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5818596.
GenomeReviewsGene locus Bpet0346 in contig AM902716_GR.
KEGGbpt:Bpet0346.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAVFTKGGG.

Family and domain databases

HAMAPMF_00218.
[Tree]
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PANTHERPTHR21091:SF2. HemE. 1 hit.
PfamPF01208. URO-D. 1 hit.
[Graphical view]
ProDomPD003225. Uro_decarbxyls. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01464. hemE. 1 hit.
PROSITEPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCUP_BORPD
AccessionPrimary (citable) accession number: A9HY51
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: November 3, 2009
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents