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Q81U23 (DCUP_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 69. 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:BA_1070, GBAA_1070, BAS0999
OrganismBacillus anthracis
Taxonomic identifier1392 [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 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
Reference 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_0000187581

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
Q81U23 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: E0745D365C5BD3DF

FASTA34839,194
        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 AEPKAWFALI 

       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 anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed: 12721629] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"Bacillus anthracis comparative genomics."
Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP25050.1.
AE017334 Genomic DNA. Translation: AAT30170.2.
AE017225 Genomic DNA. Translation: AAT53323.1.
RefSeqNP_843564.1. NC_003997.3.
YP_017695.2. NC_007530.2.
YP_027272.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81U23.
SMRQ81U23. Positions 4-345.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000011675; EBBACP00000011431; EBBACG00000011667.
EBBACT00000018430; EBBACP00000018051; EBBACG00000018421.
EBBACT00000021639; EBBACP00000021124; EBBACG00000021630.
GeneID1089006.
2816681.
2848507.
GenomeReviewsGene locus BA_1070 in contig AE016879_GR.
Gene locus BAS0999 in contig AE017225_GR.
Gene locus GBAA_1070 in contig AE017334_GR.
KEGGban:BA_1070.
bar:GBAA_1070.
bat:BAS0999.
TIGRBA_1070.
GBAA_1070.

Phylogenomic databases

GeneTreeEBGT00050000000611.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycBANT260799:BAS0999-MONOMER.
BANT261594:GBAA1070-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_BACAN
AccessionPrimary (citable) accession number: Q81U23
Secondary accession number(s): Q6I2A8, Q6KW39
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: June 1, 2003
Last modified: November 16, 2011
This is version 69 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