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Q0TF33 (HEM6_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:
Coproporphyrinogen-III oxidase, aerobic
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3
Gene names
Name:hemF
Ordered Locus Names:ECP_2457
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III By similarity. HAMAP MF_00333

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. HAMAP MF_00333

Cofactor

Manganese By similarity. HAMAP MF_00333

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1. HAMAP MF_00333

Subunit structure

Homodimer By similarity. HAMAP MF_00333

Subcellular location

Cytoplasm By similarity HAMAP MF_00333.

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandManganese
   Molecular functionOxidoreductase
   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 functioncoproporphyrinogen oxidase activity

Inferred from electronic annotation. Source: EC

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019469

Regions

Region48 – 5710Important for dimerization By similarity
Region108 – 1103Substrate binding By similarity
Region240 – 27536Important for dimerization By similarity
Region258 – 2636Substrate binding By similarity

Sites

Active site1061Proton donor By similarity
Binding site921Substrate By similarity
Site1751Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TF33 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: DC689C92CD71AE9B

FASTA29934,304
        10         20         30         40         50         60 
MKPDAHQVKQ FLLNLQDTIC QQLSAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV 

        70         80         90        100        110        120 
NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAE 

       130        140        150        160        170        180 
PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR 

       190        200        210        220        230        240 
GIGGLFFDDL NTPDFDHCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY 

       250        260        270        280        290 
VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV

« Hide

References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed: 16879640] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG70446.1.
RefSeqYP_670347.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TF33.
SMRQ0TF33. Positions 8-299.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0TF33.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000045955; EBESCP00000044144; EBESCG00000045005.
GeneID4191706.
GenomeReviewsGene locus ECP_2457 in contig CP000247_GR.
KEGGecp:ECP_2457.
PATRIC18195703. VBIEscCol77757_2488.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
GeneTreeEBGT00050000010136.
HOGENOMHBG631180.
OMAVKAYLLD.
PhylomeDBQ0TF33.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycECOL362663:ECP_2457-MONOMER.

Family and domain databases

HAMAPMF_00333. Coprogen_oxidas.
[Tree]
InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
Gene3DG3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
KOK00228.
PANTHERPTHR10755. Coprogen_oxidas. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PIRSFPIRSF000166. Coproporphyri_ox. 1 hit.
PRINTSPR00073. COPRGNOXDASE.
SUPFAMSSF102886. Coprogen_oxidas. 1 hit.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM6_ECOL5
AccessionPrimary (citable) accession number: Q0TF33
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: January 25, 2012
This is version 40 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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