Skip Header

Contribute Send feedback
Read comments (?) or add your own

A5VWK4 (HEM6_PSEP1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 34. 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:Pput_0089
OrganismPseudomonas putida (strain F1 / ATCC 700007) [Complete proteome] [HAMAP]
Taxonomic identifier351746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length303 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 – 303303Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019488

Regions

Region49 – 5810Important for dimerization By similarity
Region109 – 1113Substrate binding By similarity
Region241 – 27636Important for dimerization By similarity
Region259 – 2646Substrate binding By similarity

Sites

Active site1071Proton donor By similarity
Binding site931Substrate By similarity
Site1761Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
A5VWK4 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 0A81CBC240C6DE4E

FASTA30334,419
        10         20         30         40         50         60 
MTSRTEAVKA YLLDLQDRIC SALETEDGGA RFVEDAWVRE AGGGGRTRVI GDGKVIEKGG 

        70         80         90        100        110        120 
VNFSHVFGAG LPPSASAHRP ELAGRGFEAL GVSLVIHPYN PHVPTSHANV RFFIAEKEGE 

       130        140        150        160        170        180 
EAVWWFGGGF DLTPYYGNEE DCVHWHRVAE QACAPFGADV YPRYKAWCDR YFHLKHRGEP 

       190        200        210        220        230        240 
RGIGGLFFDD LNEWDFDTCF AFIRAIGDAY INAYLPIVQR RKDTPYTPQQ REFQEYRRGR 

       250        260        270        280        290        300 
YVEFNLVYDR GTLFGLQSGG RTESILMSLP PQVRWGYDWK AAPGSEEARL TEYFLQDRDW 


LGQ 

« Hide

References

[1]"Complete sequence of Pseudomonas putida F1."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F1 / ATCC 700007.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000712 Genomic DNA. Translation: ABQ76264.1.
RefSeqYP_001265448.1. NC_009512.1.

3D structure databases

ProteinModelPortalA5VWK4.
SMRA5VWK4. Positions 1-301.
ModBaseSearch...

Protein-protein interaction databases

STRINGA5VWK4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5193295.
GenomeReviewsGene locus Pput_0089 in contig CP000712_GR.
KEGGppf:Pput_0089.
PATRIC19916127. VBIPsePut56420_0093.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVKAYLLD.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycPPUT351746:PPUT_0089-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_PSEP1
AccessionPrimary (citable) accession number: A5VWK4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 10, 2007
Last modified: December 14, 2011
This is version 34 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