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A0JYN1 (DCUP_ARTS2) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. 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:Arth_2772
OrganismArthrobacter sp. (strain FB24) [Complete proteome] [HAMAP]
Taxonomic identifier290399 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

Protein attributes

Sequence length345 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 – 345345Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000325624

Regions

Region28 – 325Substrate binding By similarity

Sites

Binding site771Substrate By similarity
Binding site1521Substrate By similarity
Binding site2071Substrate By similarity
Binding site3211Substrate By similarity
Site771Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A0JYN1 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 380768D176241563

FASTA34537,025
        10         20         30         40         50         60 
MDGRTADSPL ITAYRGGKPT RRPVWFMRQA GRSLPEYLKV REGVAMLDSC LRPELASEIT 

        70         80         90        100        110        120 
LQPVRRHDVD AAIFFSDIVI PLKLAGVGVD IVPGVGPVLD KPVRTAEDVA ALPQLTWEAL 

       130        140        150        160        170        180 
EPIREAVRLT VAQLGKTPLI GFAGAPFTLA AYMVEGKPSR DHLGPRTMMH ADPETWNALA 

       190        200        210        220        230        240 
NWAADASGMF LRAQLEAGAS AGQLFDSWAG SLGLADYKRF VAPASARALD HVRHLGAPLI 

       250        260        270        280        290        300 
HFGTGTSELL VAMRDVGVDV VGVDYRLPLD EANRRLGGTV PLQGNIDPAL LSAPWAVLEA 

       310        320        330        340 
HVREVIKAGS FAPGHVLNLG HGVPPETDPD VLTRVVELIH SISPE 

« Hide

References

[1]"Complete sequence of chromosome 1 of Arthrobacter sp. FB24."
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K., Nakatsu C.H., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: FB24.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000454 Genomic DNA. Translation: ABK04151.1.

3D structure databases

ProteinModelPortalA0JYN1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0JYN1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus Arth_2772 in contig CP000454_GR.
KEGGart:Arth_2772.
TIGRArth_2772.

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycASP1667:ARTH_2772-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_ARTS2
AccessionPrimary (citable) accession number: A0JYN1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: December 12, 2006
Last modified: January 25, 2012
This is version 39 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