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Q6F9M1 (DCUP_ACIAD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. 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:ACIAD2474
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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_1000023865

Regions

Region27 – 315Substrate binding By similarity

Sites

Binding site771Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3301Substrate By similarity
Site771Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6F9M1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: CCBA59B7286B7F0D

FASTA35839,558
        10         20         30         40         50         60 
MTALKNDRFL RALLREPVDT TPVWMMRQAG RYLPEYRETR AQAGDFLSLC KNTEFACEVT 

        70         80         90        100        110        120 
LQPLRRYDLD AAILFSDILT IPDALGLGLY FETGEGPKFK KTIRTEQDVL NLPNFNAKSD 

       130        140        150        160        170        180 
LDYVMNAVTT IHSALGGQVP LIGFSGSPWT LATYMVEGGS SKDFRYTKHM MYSQPEVLHA 

       190        200        210        220        230        240 
LLDRLAVAVI DYLNAQIDAG AQAVQIFDSW GGALAHREYT EFSLNYMRKI VAGLQREKDG 

       250        260        270        280        290        300 
RRIPVILFTK GGGQWLEPMI ATGADAIGLD WTTPLNVARK TVAGRVALQG NLDPAVLYGS 

       310        320        330        340        350 
AASIEKSVKA MLDDAYANGE TTGYIANLGH GITQWVDPSQ PKIFVDTVHE YSAKYLGS

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ADP1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR543861 Genomic DNA. Translation: CAG69243.1.
RefSeqYP_047065.1. NC_005966.1.

3D structure databases

HSSPHSSP built from PDB template 1R3Q based on UniProtKB P06132.
ProteinModelPortalQ6F9M1.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6F9M1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2879990.
GenomeReviewsGene locus ACIAD2474 in contig CR543861_GR.
KEGGaci:ACIAD2474.
NMPDRfig|62977.3.peg.2074.
PATRIC20742566. VBIAciSp98416_2225.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBQ6F9M1.
ProtClustDBPRK00115.

Enzyme and pathway databases

BioCycASP62977:ACIAD2474-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_ACIAD
AccessionPrimary (citable) accession number: Q6F9M1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 51 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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