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A1VN15 (HEM6_POLNA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 36. 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:Pnap_1730
OrganismPolaromonas naphthalenivorans (strain CJ2) [Complete proteome] [HAMAP]
Taxonomic identifier365044 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length307 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 – 307307Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019474

Regions

Region53 – 6210Important for dimerization By similarity
Region113 – 1153Substrate binding By similarity
Region247 – 28236Important for dimerization By similarity
Region265 – 2706Substrate binding By similarity

Sites

Active site1111Proton donor By similarity
Binding site971Substrate By similarity
Site1821Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
A1VN15 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 686D38EF6C3B5C06

FASTA30735,246
        10         20         30         40         50         60 
MSSIDLSTVR TFLLGLQERI THAIAEVDGQ PFMTDHWQKE PGETLQGNGI TKILEQGRVF 

        70         80         90        100        110        120 
ERAGCGFSHV RGPRLPPSAT QHRPELAGAA FEAMGVSLVF HPRNPYVPTV HMNVRMLAAT 

       130        140        150        160        170        180 
PVGENCEPVC WFGGGMDLTP FYGFDEDAVH FHQVCKDSLK PFGDDKYPRF KQWCDEYFYL 

       190        200        210        220        230        240 
KHRQEQRGIG GVFFDDFQEL GLAQSFAMMQ SVGDSFLQAY LPIVERRKDS LFGERERDFQ 

       250        260        270        280        290        300 
LYRRGRYVEF NLVWDRGTHF GLQSGGRTES ILMSMPPLAS WSYQRPNEAG SPEERLYKEF 


LVRRDWV 

« Hide

References

[1]"Complete sequence of chromosome 1 of Polaromonas naphthalenivorans CJ2."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D.R., Brettin T., Bruce D., Han C., Tapia R., Brainard J., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Madsen E.L., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CJ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000529 Genomic DNA. Translation: ABM37043.1.
RefSeqYP_981964.1. NC_008781.1.

3D structure databases

ProteinModelPortalA1VN15.
SMRA1VN15. Positions 2-307.
ModBaseSearch...

Protein-protein interaction databases

STRINGA1VN15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4687031.
GenomeReviewsGene locus Pnap_1730 in contig CP000529_GR.
KEGGpna:Pnap_1730.
PATRIC22948088. VBIPolNap76733_2591.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVKAYLLD.
PhylomeDBA1VN15.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycPNAP365044:PNAP_1730-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_POLNA
AccessionPrimary (citable) accession number: A1VN15
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 6, 2007
Last modified: December 14, 2011
This is version 36 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