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A4ST50 (HEM6_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 33. 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:ASA_4133
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAeromonadalesAeromonadaceaeAeromonas

Protein attributes

Sequence length302 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 – 302302Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019456

Regions

Region50 – 5910Important for dimerization By similarity
Region110 – 1123Substrate binding By similarity
Region242 – 27736Important for dimerization By similarity
Region260 – 2656Substrate binding By similarity

Sites

Active site1081Proton donor By similarity
Binding site941Substrate By similarity
Site1771Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
A4ST50 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: 54EF7632B55F89C1

FASTA30234,914
        10         20         30         40         50         60 
MSKPDVAQVK AFLLQLQDEI CRSLEQADGV GRFVEDAWAR EGGGGGRTRV MRHGDMIEQG 

        70         80         90        100        110        120 
GVNFSHVYGD AMPASATAHR PELAGRKFEA MGVSLVIHPH NPYVPTSHAN VRFFIAEKEG 

       130        140        150        160        170        180 
EEPIWWFGGG FDLTPFYPFA EDVQHWHRVS RDLCQPFGED IYPEFKSWCD RYFFLKHRNE 

       190        200        210        220        230        240 
TRGVGGLFFD DLNRWPFADC FAFMQAVGRG YLDAYLPIIE RRKAQPYGER EREFQLYRRG 

       250        260        270        280        290        300 
RYVEFNLVYD RGTLFGLQTG GRTESILMSM PPLARWEYDW QPEAGSPEAL LYTDYLAPRE 


WL 

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed: 18801193] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000644 Genomic DNA. Translation: ABO92072.1.
RefSeqYP_001143820.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4ST50.
SMRA4ST50. Positions 6-302.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4ST50.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4997266.
GenomeReviewsGene locus ASA_4133 in contig CP000644_GR.
KEGGasa:ASA_4133.
PATRIC20794714. VBIAerSal2987_4102.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVKAYLLD.
PhylomeDBA4ST50.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycASAL382245:ASA_4133-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_AERS4
AccessionPrimary (citable) accession number: A4ST50
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: December 14, 2011
This is version 33 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