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Reviewed, UniProtKB/Swiss-Prot A1TVM0 (DCUP_ACIAC)

Last modified September 1, 2009. Version 22. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Uroporphyrinogen decarboxylase
      Short name=URO-D
      Short name=UPD
    EC=4.1.1.37
Gene names
Name: hemE
Ordered Locus Names: Aave_4469
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length376 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III By similarity.

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.

Subcellular location

Cytoplasm By similarity.

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 biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionuroporphyrinogen decarboxylase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 376376Uroporphyrinogen decarboxylase HAMAP MF_00218
PRO_0000325619

Regions

Region29 – 335Substrate binding By similarity

Sites

Binding site791Substrate By similarity
Binding site1551Substrate By similarity
Binding site2101Substrate By similarity
Binding site3421Substrate By similarity
Site791Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TVM0-1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 4B876CB39FF1667A

FASTA37640,416
        10         20         30         40         50         60 
MSFAPLQNDT FLRACRRQAT DYTPLWLMRQ AGRYLPEYKA TRARAGSFMG LATNVDYATE 

        70         80         90        100        110        120 
VTLQPLERFP LDAAILFSDI LTVPDAMGLG LSFAEGEGPR FARVVRDEAA VAELAVPDME 

       130        140        150        160        170        180 
KLRYVFDAVT SIRRALDGRV PLIGFSGSPW TLACYMVEGS GSDDYRLVKT LMYSRPDLMH 

       190        200        210        220        230        240 
RILAINADAV AAYLNAQIDA GAQAVMVFDS WGGVLADGAF QEFSLAYTTR VLAQLKRTGV 

       250        260        270        280        290        300 
DGTDVPRIVF TKGGALWLED MKGLDCEVLG LDWTANLARA RALVGGAVGG PGKALQGNID 

       310        320        330        340        350        360 
PNVLFAPPEA IAAQARAVLD RFGAPHTDRG TTGPTHIFNL GHGISQHTPP EHVAALVEAV 

       370 
HGHSRAMRAA AGTGRA 

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References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM35008.1. Different initiation.
RefSeqYP_972782.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TVM0.

Genome annotation databases

GeneID4667198.
GenomeReviewsGene locus Aave_4469 in contig CP000512_GR.
KEGGaav:Aave_4469.
NMPDRfig|397945.5.peg.3847.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_00218.
[Tree]
InterProIPR006361. Uroporphyrinogen_deCO2ase_HemE.
IPR000257. Uroporphyrinogen_deCOase.
[Graphical view]
PANTHERPTHR21091:SF2. HemE. 1 hit.
PfamPF01208. URO-D. 1 hit.
[Graphical view]
ProDomPD003225. Uro_decarbxyls. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR01464. hemE. 1 hit.
PROSITEPS00906. UROD_1. 1 hit.
PS00907. UROD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameDCUP_ACIAC
AccessionPrimary (citable) accession number: A1TVM0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: September 1, 2009
This is version 22 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents