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Q5HTL9 (DCUP_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 45. 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:CJE1379
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length340 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 – 340340Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000023893

Regions

Region21 – 255Substrate binding By similarity

Sites

Binding site711Substrate By similarity
Binding site1481Substrate By similarity
Binding site2031Substrate By similarity
Binding site3161Substrate By similarity
Site711Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HTL9 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 7411DCDE7E7C9F75

FASTA34038,908
        10         20         30         40         50         60 
MIFIDACFKK PTPYTPIWMM RQAGRYLPEY MEVRKQAGDF LSLCKDYKKA SEVSLQPIDI 

        70         80         90        100        110        120 
LDVDAAIIFS DILVVPLEMG MNLRFEKGEG PVFDNPISTL EDLEKLDDQN AHKKLNYVYD 

       130        140        150        160        170        180 
ALKLTREKLS QNKALIGFCG SPWTIATYMI EGSGSKNYAK CKKMLYQNPE LLHKILNKLT 

       190        200        210        220        230        240 
QVLKLYLEEQ IKAGANAIQI FDSWASALEY DKFFEFSFNY MLEISNFIKS KYPNIPVILF 

       250        260        270        280        290        300 
PKGISGYLDR IDGNFDVFGV DWSTPLDLAR DKLSHKYTLQ GNMEPCRLYD KNAIKEGVGK 

       310        320        330        340 
ILKTMQNKAH IFNLGHGILP DIPVENAKYF IKLVQESSAK

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed: 15660156] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000025 Genomic DNA. Translation: AAW35699.1.
RefSeqYP_179366.1. NC_003912.7.

3D structure databases

HSSPHSSP built from PDB template 1R3S based on UniProtKB P06132.
ProteinModelPortalQ5HTL9.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HTL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3231885.
GenomeReviewsGene locus CJE1379 in contig CP000025_GR.
KEGGcjr:CJE1379.
NMPDRfig|195099.3.peg.1418.
PATRIC20044558. VBICamJej134361_1396.
TIGRCJE1379.

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycCJEJ195099:CJE_1379-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_CAMJR
AccessionPrimary (citable) accession number: Q5HTL9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 15, 2005
Last modified: January 25, 2012
This is version 45 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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