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Q0BRD2 (Q0BRD2_GRABC) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 43. 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:GbCGDNIH1_1722
OrganismGranulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP] EMBL ABI62620.1
Taxonomic identifier391165 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

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

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 ABI62620.1
   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

Region74 – 8310Important for dimerization By similarity HAMAP MF_00333
Region134 – 1363Substrate binding By similarity HAMAP MF_00333
Region264 – 29936Important for dimerization By similarity HAMAP MF_00333
Region282 – 2876Substrate binding By similarity HAMAP MF_00333

Sites

Active site1321Proton donor By similarity HAMAP MF_00333
Binding site1181Substrate By similarity HAMAP MF_00333
Site1991Important for dimerization By similarity HAMAP MF_00333

Sequences

Sequence LengthMass (Da)Tools
Q0BRD2 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 47DFA1366D9F9E25

FASTA29933,954
        10         20         30         40         50         60 
MTDTVTAPPH EHLKSAARLW FESLRDRICA AFEAIEDDLP PAAPFGDLPP GRFERQPWDR 

        70         80         90        100        110        120 
PTSDGSPGGG GVMSVMRGRV FEKVGVNVST VWGEFSEDFR RQIPGAEHDP RFWASGISLV 

       130        140        150        160        170        180 
AHMRSPHVPA VHMNTRMLVT TKGWFGGGGD LTPMFLDTPE TAEDRESFHA SYRAACDAHD 

       190        200        210        220        230        240 
PALYPKFKQW CDEYFFLPHR GEPRGVGGIF FDHHNTGNAE EDFHFTRDVG EAFLNVYPAI 

       250        260        270        280        290 
VRRRMERPWT EAERHHQLVR RGRYVEFNLL HDRGTLFGLR TGGNTEAILM SMPPEVRWP

« Hide

References

[1]"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis."
Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.
J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000394 Genomic DNA. Translation: ABI62620.1.
RefSeqYP_745543.1. NC_008343.1.

3D structure databases

ProteinModelPortalQ0BRD2.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BRD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4275727.
GenomeReviewsGene locus GbCGDNIH1_1722 in contig CP000394_GR.
KEGGgbe:GbCGDNIH1_1722.
NMPDRfig|391165.8.peg.1670.
PATRIC22079645. VBIGraBet83793_1780.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAGKEPVWW.
PhylomeDBQ0BRD2.
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 nameQ0BRD2_GRABC
AccessionPrimary (citable) accession number: Q0BRD2
Entry history
Integrated into UniProtKB/TrEMBL: October 17, 2006
Last sequence update: October 17, 2006
Last modified: December 14, 2011
This is version 43 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