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A3PYL0 (DCUP_MYCSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. 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:Mjls_2201
OrganismMycobacterium sp. (strain JLS) [Complete proteome] [HAMAP]
Taxonomic identifier164757 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length354 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 – 354354Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000023922

Regions

Region30 – 345Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3331Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A3PYL0 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 557791BB89C23508

FASTA35437,519
        10         20         30         40         50         60 
MNTRRELPDS PYLAAARGRK PARVPVWFMR QAGRSLPEYR ALRARNTMMQ ACFDADLITE 

        70         80         90        100        110        120 
ITLQPVRRHG VDAAILFSDI VVPLRASGIA LDIVPDVGPV IDHPVRTAAD VAAIRPLERQ 

       130        140        150        160        170        180 
TVEPVEQAVR MLTAALGDVP LIGFAGAPFT LASYLVEGGP SKHHEHTKAM MLGAPDTWHA 

       190        200        210        220        230        240 
LMSALTDVTI AFLQAQVDAG VDAIQVFDSW AGTLSLADYR AYVLPHSARV FQALAPAGVP 

       250        260        270        280        290        300 
MTHFGVGTAE LLGAMSEAIA TSGAPGVVGV DWRTSLTDAA GRVERGSALQ GNLDPVVLLA 

       310        320        330        340        350 
GWPVVERAVR AVVEDGRRAV DAGAAGHVFN LGHGVLPATD PEIVTATVEL VHSL

« Hide

References

[1]"Complete sequence of Mycobacterium sp. JLS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J., Sims R.C., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JLS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000580 Genomic DNA. Translation: ABN97987.1.
RefSeqYP_001070478.1. NC_009077.1.

3D structure databases

ProteinModelPortalA3PYL0.
ModBaseSearch...

Protein-protein interaction databases

STRINGA3PYL0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000051726; EBMYCP00000050007; EBMYCG00000051721.
GeneID4877921.
GenomeReviewsGene locus Mjls_2201 in contig CP000580_GR.
KEGGmjl:Mjls_2201.
PATRIC18090532. VBIMycSp51234_2206.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
GeneTreeEBGT00050000016469.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBA3PYL0.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycMSP164757:MJLS_2201-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_MYCSJ
AccessionPrimary (citable) accession number: A3PYL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 3, 2007
Last modified: January 25, 2012
This is version 35 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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