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Q0BD83 (HEM6_BURCM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Bamb_2334
OrganismBurkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]
Taxonomic identifier339670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length306 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.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   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 – 306306Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019457

Regions

Region55 – 6410Important for dimerization By similarity
Region115 – 1173Substrate binding By similarity
Region247 – 28236Important for dimerization By similarity
Region265 – 2706Substrate binding By similarity

Sites

Active site1131Proton donor By similarity
Binding site991Substrate By similarity
Site1821Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0BD83 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 2B485B3C606CF0F8

FASTA30634,461
        10         20         30         40         50         60 
MTDSTYDVPR VRTYLQGLQA RIADALGALD GTPLATDAWQ RGPEERLRGG GCTRILEGGR 

        70         80         90        100        110        120 
VFERAGIGFS DVAGDALPPS ASAARPQLAG RGFEALGVSL VLHPRNPYCP TVHMNVRMLI 

       130        140        150        160        170        180 
ATKPGEAPIF WFGGGMDLTP VYPFEDDARH FHQVCKDALD PFGAELYPRF KTWCDEYFFL 

       190        200        210        220        230        240 
KHRNETRGIG GIFFDDFSEP GFERSFEMMQ SVGDAFLNAY LPIVERRAAL PYGERERDFQ 

       250        260        270        280        290        300 
AYRRGRYVEF NLVFDRGTLF GLQSGGRTES ILMSMPPVAN WRYNWQPEPG SPEARLSEFL 


VPRDWV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Burkholderia cepacia AMMD."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000440 Genomic DNA. Translation: ABI87890.1.
RefSeqYP_774224.1. NC_008390.1.

3D structure databases

ProteinModelPortalQ0BD83.
SMRQ0BD83. Positions 5-306.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ0BD83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4309131.
GenomeReviewsGene locus Bamb_2334 in contig CP000440_GR.
KEGGbam:Bamb_2334.
NMPDRfig|339670.3.peg.5630.
PATRIC19020344. VBIBurAmb61564_2439.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVKAYLLD.
PhylomeDBQ0BD83.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycBAMB339670:BAMB_2334-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_BURCM
AccessionPrimary (citable) accession number: Q0BD83
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: January 25, 2012
This is version 39 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