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A5G1D5 (DCUP_ACICJ) 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:Acry_2475
OrganismAcidiphilium cryptum (strain JF-5) [Complete proteome] [HAMAP]
Taxonomic identifier349163 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Acidiphilium

Protein attributes

Sequence length358 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 – 358358Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000325617

Regions

Region28 – 325Substrate binding By similarity

Sites

Binding site781Substrate By similarity
Binding site1541Substrate By similarity
Binding site2081Substrate By similarity
Binding site3241Substrate By similarity
Site781Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A5G1D5 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 07F7C4B4FD93F9EE

FASTA35838,724
        10         20         30         40         50         60 
MTGQRAEKPV LRVLGGEAVW PPPVWLMRQA GRYLPEYRKL REKAGNFIAL CTTPPLATEV 

        70         80         90        100        110        120 
TLQPVRRFGM DAAILFSDIL ILPWALGQKL RFAEGEGPRL ERIDGLAGLE ALDPAALRQG 

       130        140        150        160        170        180 
TEPVMETVSR VRAELPPETT LIGFAGSPFT VACYMIDGRG GDFPLTREVA YADPALLAAV 

       190        200        210        220        230        240 
IETVTTATID YLSWQIEAGA DCVMLFDSWA GLLPPDLFRA HVIHPTARIV EQLRVRHPGV 

       250        260        270        280        290        300 
KVIGFPRLGG LMTLPYIADT GVDAVGMDTS VDPVALARLA PRRVAFQGNL DPLLLRAGGI 

       310        320        330        340        350 
SLGQAVERIA RGLEGHPHIF NLGHGIVPDT PPEHVAAVIE RLRSLEPGEL EESALAAT

« Hide

References

[1]"Complete sequence of chromosome of Acidiphilium cryptum JF-5."
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Magnuson T., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JF-5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000697 Genomic DNA. Translation: ABQ31667.1.
RefSeqYP_001235586.1. NC_009484.1.

3D structure databases

ProteinModelPortalA5G1D5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5G1D5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5161335.
GenomeReviewsGene locus Acry_2475 in contig CP000697_GR.
KEGGacr:Acry_2475.
PATRIC20650042. VBIAciCry6074_2982.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAPRIHFGV.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycACRY349163:ACRY_2475-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_ACICJ
AccessionPrimary (citable) accession number: A5G1D5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: June 12, 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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