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Q5HNA4 (DCUP_STAEQ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:SERP1368
OrganismStaphylococcus epidermidis (strain ATCC 35984 / RP62A) [Complete proteome] [HAMAP]
Taxonomic identifier176279 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length344 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-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4. HAMAP-Rule MF_00218

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00218

Subcellular location

Cytoplasm By similarity HAMAP-Rule 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_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: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Uroporphyrinogen decarboxylase HAMAP-Rule MF_00218
PRO_0000187646

Regions

Region26 – 305Substrate binding By similarity

Sites

Binding site451Substrate By similarity
Binding site751Substrate By similarity
Binding site1511Substrate By similarity
Binding site2061Substrate By similarity
Binding site3201Substrate By similarity
Site751Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HNA4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 9FC3C1A810EC5AA7

FASTA34438,970
        10         20         30         40         50         60 
MRSKNDTILK AIKGESTSHT PVWFMRQAGR SQPEYRKLKE KYSLFEITHQ PELCAYVTHL 

        70         80         90        100        110        120 
PVDNYQTDAA VLYKDIMTPL KPIGVDVEIK SGIGPVISNP IQTVKDVERL SQIDPKRDVP 

       130        140        150        160        170        180 
YVLDTIKLLT EEKLNVPLIG FTGAPFTLAS YMIEGGPSKN YNFTKAMMYR DEETWFALMN 

       190        200        210        220        230        240 
HLVDISIDYV VAQVEAGAEI IQIFDSWVGA LNVKDYRYYI KPAMNKLISG IKAYYDVPII 

       250        260        270        280        290        300 
LFGVGASHLI NEWNDLPIDV LGLDWRTTIK QADKMGVNKA IQGNLDPSVL LAPWDVIESR 

       310        320        330        340 
LKDILNQGLN RGKHIFNLGH GVFPEVKPET LRKVTEFVHN YTAK 

« Hide

References

[1]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35984 / RP62A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000029 Genomic DNA. Translation: AAW54745.1.
RefSeqYP_188937.1. NC_002976.3.

3D structure databases

ProteinModelPortalQ5HNA4.
SMRQ5HNA4. Positions 5-342.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING176279.SERP1368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW54745; AAW54745; SERP1368.
GeneID3242851.
KEGGser:SERP1368.
PATRIC19613603. VBIStaEpi130894_1336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHOG000253897.
KOK01599.
OMATLATYMI.
OrthoDBEOG6VXF6H.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycSEPI176279:GJJB-1403-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_STAEQ
AccessionPrimary (citable) accession number: Q5HNA4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways