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Q5FPR2 (Q5FPR2_GLUOX) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
Short name=Coprogen oxidase HAMAP MF_00333
Short name=Coproporphyrinogenase HAMAP MF_00333
EC=1.3.3.3 HAMAP MF_00333
Gene names
Name:hemF HAMAP MF_00333
Ordered Locus Names:GOX1896
OrganismGluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) [Complete proteome] [HAMAP] EMBL AAW61634.1
Taxonomic identifier290633 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Gluconobacter

Protein attributes

Sequence length305 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

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. HAMAP MF_00333

Ontologies

Keywords
   Biological processPorphyrin biosynthesis HAMAP MF_00333
   Cellular componentCytoplasm HAMAP MF_00333
   Molecular functionOxidoreductase HAMAP MF_00333 EMBL AAW61634.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processporphyrin-containing compound biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncoproporphyrinogen oxidase activity

Inferred from electronic annotation. Source: HAMAP

protein homodimerization activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region80 – 8910Important for dimerization By similarity HAMAP MF_00333
Region140 – 1423Substrate binding By similarity HAMAP MF_00333
Region270 – 30536Important for dimerization By similarity HAMAP MF_00333
Region288 – 2936Substrate binding By similarity HAMAP MF_00333

Sites

Active site1381Proton donor By similarity HAMAP MF_00333
Binding site1241Substrate By similarity HAMAP MF_00333
Site2051Important for dimerization By similarity HAMAP MF_00333

Sequences

Sequence LengthMass (Da)Tools
Q5FPR2 [UniParc].

Last modified March 1, 2005. Version 1.
Checksum: 656203121B3DD620

FASTA30534,674
        10         20         30         40         50         60 
MDQISPGFAE TVRPDVPHDA LKQDAKAWFE TLRDRICASY EKLEDEAAEG GSQVLRDRTA 

        70         80         90        100        110        120 
PGRFERTAWS RPEGGSGVMS VMRGRVFEKV GVNVSTVWGE FSPEFRKNIP GADEDPRFFA 

       130        140        150        160        170        180 
TGVSLVAHPC NPHVSAAHFN TRMIITTKGW FGGGGDITPM FPESAEAQSD AAYFHKSFED 

       190        200        210        220        230        240 
ACNRHDPEHY PRFKEWCDRY FHLHHRNEPR GLGGIFYDQF YTGDVDLDFA FTKDVGMAFH 

       250        260        270        280        290        300 
DAYPAVVRRR MFTPWTEADR DAQLIRRGRY VEFNLLHDRG TLFGLKTGGN TEAILMSMPP 


EVRWP

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References

[1]"Complete genome sequence of the acetic acid bacterium Gluconobacter oxydans."
Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F., Ehrenreich A., Gottschalk G., Deppenmeier U.
Nat. Biotechnol. 23:195-200(2005) [PubMed: 15665824] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 621H.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000009 Genomic DNA. Translation: AAW61634.1.
RefSeqYP_192290.1. NC_006677.1.

3D structure databases

ProteinModelPortalQ5FPR2.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3250655.
GenomeReviewsGene locus GOX1896 in contig CP000009_GR.
KEGGgox:GOX1896.
NMPDRfig|290633.1.peg.1835.
PATRIC32611696. VBIGluOxy81109_2186.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG631180.
OMAARICAEL.
ProtClustDBPRK05330.

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 nameQ5FPR2_GLUOX
AccessionPrimary (citable) accession number: Q5FPR2
Entry history
Integrated into UniProtKB/TrEMBL: March 1, 2005
Last sequence update: March 1, 2005
Last modified: December 14, 2011
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info