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A0LUP4 (DCUP_ACIC1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:Acel_1382
OrganismAcidothermus cellulolyticus (strain ATCC 43068 / 11B) [Complete proteome] [HAMAP]
Taxonomic identifier351607 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesFrankineaeAcidothermaceaeAcidothermus

Protein attributes

Sequence length368 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 – 368368Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_1000058637

Regions

Region30 – 345Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1541Substrate By similarity
Binding site2091Substrate By similarity
Binding site3201Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A0LUP4 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 43A0496BBAC6DFB4

FASTA36839,356
        10         20         30         40         50         60 
MADVLPRSDG ALLRVCRGEP APVTPVWFMR QAGRALPEYR AARGETPMLQ ACLDRDLIVE 

        70         80         90        100        110        120 
LTLQPVRRYR VDAAILFSDI TVPLALSGVS LRIEPGVGPV FDQPVRRAAD VARIRPLDRG 

       130        140        150        160        170        180 
SMTPIVEAVR LLVGELAGIP LIGFAGAPFT LASYLVEGGP SRDHAVTKAL MYSDPATWHA 

       190        200        210        220        230        240 
LLDRLADISR EFLLAQIDAG VSVVQVFDSW AGALHPDDYR RYVAPHSGKL LAGLPVPRIH 

       250        260        270        280        290        300 
FGVGTGELLP QFRAVGADVV GVDWRVPLDV AARRIGADAV VQGNLDPAVV FAPWPVLEAA 

       310        320        330        340        350        360 
VRDVLIRGRA ARGHIFNLGH GVLPSTDPGV LAAIVDFVHA WSADRSARGV PTAVDRFGSE 


HPAAEAAG 

« Hide

References

[1]"Complete sequence of Acidothermus cellulolyticus 11B."
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., Zharchuk I., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Berry A.M., Adney W.S., Normand P., Leu D., Pujic P., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43068 / 11B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000481 Genomic DNA. Translation: ABK53154.1.
RefSeqYP_873140.1. NC_008578.1.

3D structure databases

ProteinModelPortalA0LUP4.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0LUP4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4485870.
GenomeReviewsGene locus Acel_1382 in contig CP000481_GR.
KEGGace:Acel_1382.
PATRIC20673278. VBIAciCel132453_1467.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0407.
HOGENOMHBG628392.
OMAPRIHFGV.
PhylomeDBA0LUP4.

Enzyme and pathway databases

BioCycACEL351607:ACEL_1382-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_ACIC1
AccessionPrimary (citable) accession number: A0LUP4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 12, 2006
Last modified: December 14, 2011
This is version 36 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