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A7GM02 (DCUP_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 32. 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:Bcer98_0824
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus 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.

Sequence caution

The sequence ABS21160.1 differs from that shown. Reason: Erroneous initiation.

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_0000325626

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
A7GM02 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 0B66AC5219448E5F

FASTA34839,325
        10         20         30         40         50         60 
MVRNINETFL KACKGERTDY VPAWYMRQAG RSQPEYRKIK EKYSLFEITH NPELCAYVTK 

        70         80         90        100        110        120 
LPVDQYNVDA AILYKDIMSP LPAIGVDVEI KSGIGPVIEN PIRSMQDVEK LGEIHPEEDV 

       130        140        150        160        170        180 
PYILDTIRLL TAEMLDVPLI GFSGAPFTLA SYMIEGGPSR NYHKTKAFMY AEPKAWFALM 

       190        200        210        220        230        240 
DKLSDMVIAY LKAQIQAGAK AVQVFDSWVG TVNVADYRIF IKPAMERIFA QVREMNVPMI 

       250        260        270        280        290        300 
MHGVGAGHLA NEWNDLPLDV VGLDWRLSIE EARTRGIHKA VQGNMDPSLL LAPWNVIEEH 

       310        320        330        340 
VKGILDQGMK QPGYVFNLGH GVFPEVNPDT LKRLTAFIHE YSKEQLAK 

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000764 Genomic DNA. Translation: ABS21160.1. Different initiation.
RefSeqYP_001374155.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GM02.
SMRA7GM02. Positions 6-345.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GM02.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000039259; EBBACP00000038310; EBBACG00000039250.
GeneID5346328.
GenomeReviewsGene locus Bcer98_0824 in contig CP000764_GR.
KEGGbcy:Bcer98_0824.
PATRIC18930051. VBIBacCyt128034_0871.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
GeneTreeEBGT00050000000611.
HOGENOMHBG628392.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycBCER315749:BCER98_0824-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_BACCN
AccessionPrimary (citable) accession number: A7GM02
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: December 14, 2011
This is version 32 of the entry and version 2 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