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Q9ZC86 (HEM6_RICPR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:RP882
OrganismRickettsia prowazekii (strain Madrid E) [Reference proteome] [HAMAP]
Taxonomic identifier272947 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › typhus group ›

Protein attributes

Sequence length279 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-Rule MF_00333

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncoproporphyrinogen oxidase activity

Inferred from electronic annotation. Source: HAMAP

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 – 279279Coproporphyrinogen-III oxidase, aerobic HAMAP-Rule MF_00333
PRO_0000109916

Regions

Region58 – 6710Important for dimerization By similarity
Region118 – 1203Substrate binding By similarity
Region244 – 27936Important for dimerization By similarity
Region262 – 2676Substrate binding By similarity

Sites

Active site1161Proton donor By similarity
Binding site1021Substrate By similarity
Site1791Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZC86 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 334D2FFDA55220AF

FASTA27932,197
        10         20         30         40         50         60 
MNTENKEITS NWFTNLRDLL CKEFEKIEEK YAQIKGLKPA KFVRTSWKRN GGGCGIMSLM 

        70         80         90        100        110        120 
KGEVFEKVGV NISTVFGEFS QEFRSEILGA ELDGKFFATG ISVVAHLKSP LIPAMHFNTR 

       130        140        150        160        170        180 
YIETSKNWFG GGGDLTPFYP EENETAKFHT AFKEACDKYD SSYYPKFKKQ CDEYFYLRHR 

       190        200        210        220        230        240 
KEPRGVGGIF YDYLNSGNFE QDFAFTKDIG KALLSVYPEI VRSKLFLPWT AEQKEYQLIR 

       250        260        270 
RGRYVEFNLL YDRGTKFGLM TDGNVEAILM SLPPVVKFN

« Hide

References

[1]"The genome sequence of Rickettsia prowazekii and the origin of mitochondria."
Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., Kurland C.G.
Nature 396:133-140(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Madrid E.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ235273 Genomic DNA. Translation: CAA15304.1.
PIRH71650.
RefSeqNP_221228.1. NC_000963.1.

3D structure databases

ProteinModelPortalQ9ZC86.
ModBaseSearch...

Protein-protein interaction databases

STRING272947.RP882.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAA15304; CAA15304; CAA15304.
GeneID883468.
KEGGrpr:RP882.
PATRIC17902646. VBIRicPro72556_0922.

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHOG000262768.
KOK00228.
OMAHVPAVHM.
ProtClustDBPRK05330.

Enzyme and pathway databases

UniPathwayUPA00251; UER00322.

Family and domain databases

Gene3D3.40.1500.10. 1 hit.
HAMAPMF_00333. Coprogen_oxidas.
InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
PANTHERPTHR10755. PTHR10755. 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_RICPR
AccessionPrimary (citable) accession number: Q9ZC86
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Rickettsia prowazekii

Rickettsia prowazekii (strain Madrid E): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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