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B7UPF2 (DCUP_ECO27) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:E2348C_4304
OrganismEscherichia coli O127:H6 (strain E2348/69 / EPEC) [Complete proteome] [HAMAP]
Taxonomic identifier574521 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length354 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-Rule MF_00218

Catalytic activity

Uroporphyrinogen III = coproporphyrinogen + 4 CO2. HAMAP-Rule MF_00218

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP-Rule 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_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 – 354354Uroporphyrinogen decarboxylase HAMAP-Rule MF_00218
PRO_1000197519

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

Sequences

Sequence LengthMass (Da)Tools
B7UPF2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 604933C50636FD67

FASTA35439,234
        10         20         30         40         50         60 
MTELKNDRYL RALLRQPVDV TPVWMMRQAG RYLPEYKATR AQAGDFMSLC KNAELACEVT 

        70         80         90        100        110        120 
LQPLRRYPLD AAILFSDILT VPDAMGLGLY FEAGEGPRFT SPVTCKADVD KLPIPDPEDE 

       130        140        150        160        170        180 
LGYVMNAVRT IRRELKGEVP LIGFSGSPWT LATYMVEGGS SKAFTVIKKM MYADPQALHA 

       190        200        210        220        230        240 
LLDKLAKSVT LYLNAQIKAG AQAVMIFDTW GGVLTGRDYQ QFSLYYMHKI VDGLLRENDG 

       250        260        270        280        290        300 
RRVPVTLFTK GGGQWLEAMA ETGCDALGLD WTTDIADARR RVGNKVALQG NMDPSMLYAP 

       310        320        330        340        350 
PARIEEEVAS ILAGFGHGEG HVFNLGHGIH QDVPPEHAGV FVEAVHRLSE QYHR

« Hide

References

[1]"Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69."
Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.
J. Bacteriol. 191:347-354(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E2348/69 / EPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM180568 Genomic DNA. Translation: CAS11852.1.
RefSeqYP_002331760.1. NC_011601.1.

3D structure databases

ProteinModelPortalB7UPF2.
SMRB7UPF2. Positions 3-354.
ModBaseSearch...

Protein-protein interaction databases

STRING574521.E2348C_4304.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAS11852; CAS11852; E2348C_4304.
GeneID7065428.
KEGGecg:E2348C_4304.
PATRIC18347884. VBIEscCol90278_4403.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
KOK01599.
OMATLATYMI.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycECOL574521:GJAO-4477-MONOMER.
UniPathwayUPA00251; UER00321.

Family and domain databases

HAMAPMF_00218. URO-D.
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PANTHERPTHR21091:SF2. PTHR21091:SF2. 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_ECO27
AccessionPrimary (citable) accession number: B7UPF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: February 10, 2009
Last modified: May 1, 2013
This is version 34 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

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