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O66667 (DCUP_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:aq_334
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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 Probable HAMAP MF_00218.

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   Molecular functionDecarboxylase
Lyase
   Technical term3D-structure
Complete proteome
Reference 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 – 338338Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000187580

Regions

Region25 – 295Substrate binding By similarity

Sites

Binding site441Substrate By similarity
Binding site751Substrate By similarity
Binding site1461Substrate By similarity
Binding site2011Substrate By similarity
Binding site3141Substrate By similarity
Site751Transition state stabilizer By similarity

Secondary structure

1 ........................................................ 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O66667 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 92807A91AA2C8F9B

FASTA33838,687
        10         20         30         40         50         60 
MPKNDLLLRS LRGEPIGRFP VWLMRQAGRY MPEYRKIRNR VKNFLELCKN VDLATEISLL 

        70         80         90        100        110        120 
PLKILGVDAI IIFSDILVPL EPLGVKVEFV EGEGPKLSWS GKVSDLKKYD PSQNAYVYEI 

       130        140        150        160        170        180 
IKRVKEAQDE VPVIGFAGAP FTLLSYLIEG GASKDFKSTK LFMWENPKEY KRLMDILTET 

       190        200        210        220        230        240 
VLAYLKEQIK AGADVVQIFD SWVNNLSLED YGEYVYPYVN YLISELKDFS DTPVIYFFRG 

       250        260        270        280        290        300 
SSSFIDLAVD YRADALSVDW SVDIPELFKI YDKGFQGNLE PAVLYASEEV IEEKTLGLLR 

       310        320        330 
RIPVKTRYVF NLGHGLAPDM ELEKVKYLVD LVKSFPLT

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE000657 Genomic DNA. Translation: AAC06624.1.
PIRG70329.
RefSeqNP_213227.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EJAX-ray1.90A/B1-338[»]
ProteinModelPortalO66667.
SMRO66667. Positions 2-338.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1192901.
GenomeReviewsGene locus aq_334 in contig AE000657_GR.
KEGGaae:aq_334.
NMPDRfig|224324.1.peg.242.
PATRIC20958258. VBIAquAeo85532_0267.

Phylogenomic databases

HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBO66667.
ProtClustDBCLSK2299367.

Enzyme and pathway databases

BioCycAAEO224324:AQ_334-MONOMER.

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_AQUAE
AccessionPrimary (citable) accession number: O66667
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 78 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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