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Reviewed, UniProtKB/Swiss-Prot Q5P4Q4 (DCUP_AZOSE)

Last modified February 9, 2010. Version 39. 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

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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: AZOSEA15830
ORF Names: ebA2822
OrganismAzoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)) [Complete proteome] [HAMAP]
Taxonomic identifier76114 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Rhodocyclales › Rhodocyclaceae › Aromatoleum

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Protein attributes

Sequence length356 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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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.

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000023872

Regions

Region27 – 315Substrate binding By similarity

Sites

Binding site771Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3271Substrate By similarity
Site771Transition state stabilizer By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5P4Q4-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 510DD5E5EE413EB8

FASTA35639,300
        10         20         30         40         50         60 
MSRLQNDTFL RALLRQPTDY TPLWMMRQAG RYLPEYCETR RRAGSFLDLC KSPALACEVT 

        70         80         90        100        110        120 
LQPLARYDLD AAILFSDILT VPDAMGLGLY FAEGEGPRFE RPLRDEWEIR NLVAPDPHAE 

       130        140        150        160        170        180 
LQYVMDAVAE IRRALGGSVP LIGFSGSPWT LACYMVEGGS SDDYRRIKTM AYTRPDLLHH 

       190        200        210        220        230        240 
VLRVTADSVV AYLNAQIESG AQAVMVFDSW GGVLSEAAYR EFSLPYLERV VAGLIRERDG 

       250        260        270        280        290        300 
ERIPSIVFTK GGGLWLESIA AIGCDAVGLD WTMDIGRARA LVGDKVALQG NLDPAILFAP 

       310        320        330        340        350 
PETIATEAKR VLDAFGPHPG HVFNLGHGIS QFTPPEAVSV LVDTVHQHSR KLRGGR

« Hide

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References

[1]"The genome sequence of an anaerobic aromatic-degrading denitrifying bacterium, strain EbN1."
Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F., Reinhardt R.
Arch. Microbiol. 183:27-36(2005) [PubMed: 15551059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR555306 Genomic DNA. Translation: CAI07708.1.
RefSeqYP_158609.1.

3D structure databases

HSSPHSSP built from PDB template 1R3Q based on UniProtKB P06132.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5P4Q4.

Genome annotation databases

GeneID3179544.
GenomeReviewsGene locus AZOSEA15830 in contig CR555306_GR.
KEGGeba:ebA2822.
NMPDRfig|76114.4.peg.521.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAQIFDTWG.

Enzyme and pathway databases

BioCycASP76114:EBA2822-MONOMER.

Family and domain databases

HAMAPMF_00218. URO-D.
[Tree]
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
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...

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Entry information

Entry nameDCUP_AZOSE
AccessionPrimary (citable) accession number: Q5P4Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: February 9, 2010
This is version 39 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)

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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