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B1XAA7 (HEM6_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:ECDH10B_2601
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [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_1000119799

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
B1XAA7 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 53667E5C7B6D0198

FASTA29934,323
        10         20         30         40         50         60 
MKPDAHQVKQ FLLNLQDTIC QQLTAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV 

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

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

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

       250        260        270        280        290 
VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed: 18245285] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000948 Genomic DNA. Translation: ACB03587.1.
RefSeqYP_001731365.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1XAA7.
SMRB1XAA7. Positions 8-299.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1XAA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000011405; EBESCP00000010933; EBESCG00000010467.
GeneID6060058.
GenomeReviewsGene locus ECDH10B_2601 in contig CP000948_GR.
KEGGecd:ECDH10B_2601.
PATRIC18465085. VBIEscCol59506_2622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000010136.
HOGENOMHBG631180.
OMAVKAYLLD.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycECOL316385:ECDH10B_2601-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_ECODH
AccessionPrimary (citable) accession number: B1XAA7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
This is version 30 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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