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Q7UZS3 (HEM6_PROMP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 57. 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:PMM1582
OrganismProchlorococcus marinus subsp. pastoris (strain CCMP1986 / MED4) [Complete proteome] [HAMAP]
Taxonomic identifier59919 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Prochlorophytes › Prochlorococcaceae › Prochlorococcus

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_0000109909

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
Q7UZS3 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: F9D874BAA3B7FB7F

FASTA34239,848
        10         20         30         40         50         60 
MSKEPPKNSR EKTKNLLLKL QDNICKGLEN IDGKAKFTEE SWLREEGGGG KSRVLKNGSI 

        70         80         90        100        110        120 
FEQAGVNFSE VHGKELPQSI ISQRPEAKGH KWFATGTSMV LHPKNPFIPT VHLNYRYFEA 

       130        140        150        160        170        180 
GPVWWFGGGA DLTPYYPYLT DVRNFHKEHC NACEKVNKNL HKVFKPWCDE YFFLKHRNES 

       190        200        210        220        230        240 
RGIGGIFYDY QDGSGRIYKG NNKESKAYKE SINIGELNLN WNNLFSLAEN CGGAFLDSYQ 

       250        260        270        280        290        300 
PIIEKRVNQN YTKEQREFQL YRRGRYVEFN LVWDRGTIFG LQTNGRTESI LMSLPPLARW 

       310        320        330        340 
EYGYKAKKGS REDYLTKIFT KPQDWQNDKI LEKFCKENNI FD

« Hide

References

[1]"Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche differentiation."
Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A., Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L., Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C. expand/collapse author list , Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R., Chisholm S.W.
Nature 424:1042-1047(2003) [PubMed: 12917642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CCMP1986 / MED4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX548174 Genomic DNA. Translation: CAE20041.1.
RefSeqNP_893699.1. NC_005072.1.

3D structure databases

ProteinModelPortalQ7UZS3.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ7UZS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1726476.
GenomeReviewsGene locus PMM1582 in contig BX548174_GR.
KEGGpmm:PMM1582.
NMPDRfig|59919.1.peg.1578.
PATRIC23034350. VBIProMar68066_1825.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHBG631180.
OMAVFKPWCD.
PhylomeDBQ7UZS3.
ProtClustDBPRK05330.

Enzyme and pathway databases

BioCycPMAR167540:PMM1582-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_PROMP
AccessionPrimary (citable) accession number: Q7UZS3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: October 1, 2003
Last modified: January 25, 2012
This is version 57 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

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