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O53231 (DCUP_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 86. 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:Rv2678c, MT2752
ORF Names:MTV010.02c
OrganismMycobacterium tuberculosis
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length357 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.

Miscellaneous

Was identified as a high-confidence drug target. HAMAP MF_00218

Sequence similarities

Belongs to the uroporphyrinogen decarboxylase family.

Sequence caution

The sequence AAK47067.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   Molecular functionDecarboxylase
Lyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processporphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: MTBBASE

   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 – 357357Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000187616

Regions

Region30 – 345Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3361Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
O53231 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: F5F09F1680BDC7B3

FASTA35737,606
        10         20         30         40         50         60 
MSTRRDLPQS PYLAAVTGRK PSRVPVWFMR QAGRSLPEYR ALRERYSMLA ACFEPDVACE 

        70         80         90        100        110        120 
ITLQPIRRYD VDAAILFSDI VVPLRAAGVD LDIVADVGPV IADPVRTAAD VAAMKPLDPQ 

       130        140        150        160        170        180 
AIQPVLVAAS LLVAELGDVP LIGFAGAPFT LASYLVEGGP SRHHAHVKAM MLAEPASWHA 

       190        200        210        220        230        240 
LMAKLTDLTI AFLVGQIDAG VDAIQVFDSW AGALSPIDYR QYVLPHSARV FAALGEHGVP 

       250        260        270        280        290        300 
MTHFGVGTAE LLGAMSEAVT AGERPGRGAV VGVDWRTPLT DAAARVVPGT ALQGNLDPAV 

       310        320        330        340        350 
VLAGWPAVER AARAVVDDGR RAVDAGAAGH IFNLGHGVLP ESDPAVLADL VSLVHSL 

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed: 9634230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
Raman K., Yeturu K., Chandra N.
BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract]
Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX842580 Genomic DNA. Translation: CAA16021.1.
AE000516 Genomic DNA. Translation: AAK47067.1. Different initiation.
PIRG70869.
RefSeqNP_217194.1. NC_000962.2.
NP_337253.1. NC_002755.2.

3D structure databases

ProteinModelPortalO53231.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000001204; EBMYCP00000001204; EBMYCG00000001204.
EBMYCT00000069254; EBMYCP00000067313; EBMYCG00000069249.
GeneID888934.
925549.
GenomeReviewsGene locus MT2752 in contig AE000516_GR.
Gene locus Rv2678c in contig AL123456_GR.
KEGGmtc:MT2752.
mtu:Rv2678c.
PATRIC18127790. VBIMycTub22151_2994.
TIGRMT2752.

Organism-specific databases

TubercuListRv2678c.

Phylogenomic databases

GeneTreeEBGT00050000016469.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBO53231.
ProtClustDBPRK00115.

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_MYCTU
AccessionPrimary (citable) accession number: O53231
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: January 25, 2012
This is version 86 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