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Q5QXJ4 (HEM6_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 49. 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:IL0023
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesIdiomarinaceaeIdiomarina

Protein attributes

Sequence length304 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 – 304304Coproporphyrinogen-III oxidase, aerobic HAMAP MF_00333
PRO_0000109899

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
Q5QXJ4 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: DB7F81B4B9B414AF

FASTA30435,113
        10         20         30         40         50         60 
MHNDYLKQVK SYLMSLQDAI CQQLAQADGE QSFQEDSWDR PGGGGGRSRI MKNGAVFEQG 

        70         80         90        100        110        120 
GVGFSHVYGE KMPASATAHR PELEGRDFNA CGVSLVMHPE NPMVPTVHMN VRFFIAQKEG 

       130        140        150        160        170        180 
EEPVWWFGGG FDLTPFYPFD QDIIEWHQQA KNALDSVDEK LYPEYKAWCD DYFFLKHRDE 

       190        200        210        220        230        240 
ARGVGGIFFD DLNDRSFDEC FSVIKAVGDA FTKAYLPIVE RRKNLAYTQQ QRDFQLYRRG 

       250        260        270        280        290        300 
RYVEFNLVWD RGTLFGLQTG GRTESILMSM PPLARWEYNW QAEPGSAEEQ LTEYYLKPRD 


WLSV 

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References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017340 Genomic DNA. Translation: AAV80867.1.
RefSeqYP_154416.1. NC_006512.1.

3D structure databases

ProteinModelPortalQ5QXJ4.
SMRQ5QXJ4. Positions 6-302.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3173121.
GenomeReviewsGene locus IL0023 in contig AE017340_GR.
KEGGilo:IL0023.
NMPDRfig|283942.3.peg.73.
PATRIC22138051. VBIIdiLoi21852_0023.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG631180.
OMAVKAYLLD.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycILOI283942:IL0023-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_IDILO
AccessionPrimary (citable) accession number: Q5QXJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 49 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