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A2BYW5 (HEM6_PROM5) 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
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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:P9515_17691
OrganismProchlorococcus marinus (strain MIT 9515) [Complete proteome] [HAMAP]
Taxonomic identifier167542 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchlorophytesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length342 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 – 342342Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_1000019478

Regions

Region54 – 6310Important for dimerization By similarity
Region114 – 1163Substrate binding By similarity
Region266 – 30136Important for dimerization By similarity
Region284 – 2896Substrate binding By similarity

Sites

Active site1121Proton donor By similarity
Binding site981Substrate By similarity
Site1761Important for dimerization By similarity

Sequences

Sequence LengthMass (Da)Tools
A2BYW5 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: A4FF00395B216F33

FASTA34239,764
        10         20         30         40         50         60 
MSKEPPNNSR EKTKNLLLKL QDNICKNLEN IDGKAKFTEE SWLREEGGGG RSRVLKNGSI 

        70         80         90        100        110        120 
FEQAGVNFSE VYGKELPQSI ISQRPEAKGH EWFATGTSMV LHPKNPFIPT VHLNYRYFEA 

       130        140        150        160        170        180 
GPVWWFGGGA DLTPYYPYLS DVRHFHKEHS NACEKVNKKL HLVFKPWCDE YFFLKHRNES 

       190        200        210        220        230        240 
RGIGGIFYDY QDGSGNIYKG SNKDGNAYKE SNNIGELNLN WNNLFALAEN CGEAFLSSYQ 

       250        260        270        280        290        300 
PIIEKRVSQN YTKEEREFQL YRRGRYVEFN LVWDRGTIFG LQTNGRTESI LMSLPPLARW 

       310        320        330        340 
EYGYKAKQGS REDLLTKIFT RPQDWQNDKV LEEFCLENNI FD 

« Hide

References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed: 18159947] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MIT 9515.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000552 Genomic DNA. Translation: ABM72976.1.
RefSeqYP_001012083.1. NC_008817.1.

3D structure databases

ProteinModelPortalA2BYW5.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2BYW5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4719892.
GenomeReviewsGene locus P9515_17691 in contig CP000552_GR.
KEGGpmc:P9515_17691.
PATRIC23017220. VBIProMar113831_1819.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVFKPWCD.
PhylomeDBA2BYW5.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycPMAR167542:P9515ORF_1845-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_PROM5
AccessionPrimary (citable) accession number: A2BYW5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 20, 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