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Q73C99 (DCUP_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:BCE_1167
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length348 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 – 348348Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000023873

Regions

Region27 – 315Substrate binding By similarity

Sites

Binding site461Substrate By similarity
Binding site761Substrate By similarity
Binding site1521Substrate By similarity
Binding site2071Substrate By similarity
Binding site3201Substrate By similarity
Site761Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73C99 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: FF9BE196880FD69A

FASTA34839,212
        10         20         30         40         50         60 
MVRTINETFL KACRGERTDY VPAWYMRQAG RSQPEYRKIK EKYSLFEITH NPELCAYVTK 

        70         80         90        100        110        120 
LPVDQYNVDA AILYKDIMSP LPAIGVDVEI KSGIGPVIDN PIRSLQDVEK LGEINPEDDV 

       130        140        150        160        170        180 
PYILDTIRLL TTEMLDVPLI GFSGAPFTLA SYMIEGGPSR NYHNTKAFMY AEPKAWFALM 

       190        200        210        220        230        240 
DKLADMVITY LKAQINAGAK AVQIFDSWVG TVNVADYRVF IKPAMERIFA EVRTMGVPMI 

       250        260        270        280        290        300 
MHGVGAAHLV NEWHDLPLDV VGLDWRLPIE EARARGVHKA VQGNMDPSFL LAPWSVIEEH 

       310        320        330        340 
VKGILDQGMK QPGYIFNLGH GVFPEVNPDT LKRLTTFIHE YSKGQLAK

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017194 Genomic DNA. Translation: AAS40097.1.
RefSeqNP_977489.1. NC_003909.8.

3D structure databases

HSSPHSSP built from PDB template 1R3S based on UniProtKB P06132.
ProteinModelPortalQ73C99.
SMRQ73C99. Positions 4-345.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ73C99.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000024755; EBBACP00000024105; EBBACG00000024746.
GeneID2750779.
GenomeReviewsGene locus BCE_1167 in contig AE017194_GR.
KEGGbca:BCE_1167.
PATRIC18851202. VBIBacCer118379_1106.
TIGRBCE_1167.

Phylogenomic databases

eggNOGCOG0407.
GeneTreeEBGT00050000000611.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycBCER405917:BCE_1167-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_BACC1
AccessionPrimary (citable) accession number: Q73C99
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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