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Q9KDL0 (DCUP_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. 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:BH1202
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length344 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
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 – 344344Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000187583

Regions

Region27 – 315Substrate binding By similarity

Sites

Binding site461Substrate By similarity
Binding site761Substrate By similarity
Binding site1511Substrate By similarity
Binding site2061Substrate By similarity
Binding site3191Substrate By similarity
Site761Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KDL0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FFCA564C50392B51

FASTA34438,901
        10         20         30         40         50         60 
MSNSFNDTFL KACKGEVHDH VPVWYMRQAG RSQPEYRKIK EKYSLFEITK QPELCAYVTK 

        70         80         90        100        110        120 
LPVDQYNNDA AILYKDIMTP LPFIGVDVEI KTGKGPVIDN PIQSYADVER LGTIQPEEDV 

       130        140        150        160        170        180 
PYVLDTIKLL REQLTVPLIS FAGAPFTLAS YMIEGGPSKS YNKTKAFMYA EPKAWHLLMD 

       190        200        210        220        230        240 
KLGEMTITYV KAQIAAGAQA IQIFDSWVGT LNVQDYRVFV KPVMERTFSE LQKEKVPLIM 

       250        260        270        280        290        300 
FGVGASHLVN EWNDLPLDVV GLDWRLQIKE ARELGVTKTV QGNLDPAILL APWEVIEARA 

       310        320        330        340 
KEILDQGLET PNFIFNLGHG VFPEVEPDTL KRLTAFVHEY SANN

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BA000004 Genomic DNA. Translation: BAB04921.1.
PIRB83800.
RefSeqNP_242068.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KDL0.
SMRQ9KDL0. Positions 4-343.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000050588; EBBACP00000049227; EBBACG00000050579.
GeneID894178.
GenomeReviewsGene locus BH1202 in contig BA000004_GR.
KEGGbha:BH1202.
NMPDRfig|272558.1.peg.1202.
PATRIC18939458. VBIBacHal18977_1247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000000611.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBQ9KDL0.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycBHAL272558:BH1202-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_BACHD
AccessionPrimary (citable) accession number: Q9KDL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 72 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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