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Q8FY24 (DCUP_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BR2066, BS1330_I2060
OrganismBrucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]
Taxonomic identifier204722 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length341 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 Probable 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 – 341341Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000187590

Regions

Region23 – 275Substrate binding By similarity

Sites

Binding site421Substrate By similarity
Binding site731Substrate By similarity
Binding site1481Substrate By similarity
Binding site2031Substrate By similarity
Binding site3181Substrate By similarity
Site731Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FY24 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: DA4873C2CA945A82

FASTA34137,831
        10         20         30         40         50         60 
MNRKVLKVID GETVFPPPIW MMRQAGRYLP EYRETRKKAG SFLDLCYSPD LAVEVTLQPI 

        70         80         90        100        110        120 
RRFGFDAAIL FSDILVVPHA LGRDLRFEEG KGPLMTPIDA DEIFWLETEG VAKRLEPVYE 

       130        140        150        160        170        180 
TVRLVREQLP DETTLLGFCG APWTVATYMI AGHGTPDQAP ARLFAYRFPE AFEKLLNDLA 

       190        200        210        220        230        240 
DVSAEYLIEQ LGAGADAVQI FDSWSGVLDE DCFERFCIRP VARIVQKVRA VYPQARIIGF 

       250        260        270        280        290        300 
PKGAGMLYAG YREKTGVDML GLDWSVPLSF AALLQEEGAV QGNLDPLRVV AGGNALDEGV 

       310        320        330        340 
DAILERMGQG PLVFNLGHGI TPQAPIENVQ RMIDRVRGGK S 

« Hide

References

[1]"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts."
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. expand/collapse author list , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed: 12271122] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.
[2]"Revised genome sequence of Brucella suis 1330."
Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.
J. Bacteriol. 193:6410-6410(2011) [PubMed: 22038969] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 1330.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014291 Genomic DNA. Translation: AAN30956.1.
CP002997 Genomic DNA. Translation: AEM19373.1.
RefSeqNP_699041.1. NC_004310.3.

3D structure databases

ProteinModelPortalQ8FY24.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1167769.
GenomeReviewsGene locus BR2066 in contig AE014291_GR.
KEGGbms:BR2066.
PATRIC17792559. VBIBruSui107850_2100.
TIGRBR2066.

Phylogenomic databases

HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBQ8FY24.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycBSUI204722:BR_2066-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_BRUSU
AccessionPrimary (citable) accession number: Q8FY24
Secondary accession number(s): G0K914
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Brucella suis

Brucella suis (strain 1330): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families