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Reviewed, UniProtKB/Swiss-Prot P36553 (HEM6_ECOLI)

Last modified June 16, 2009. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Coproporphyrinogen-III oxidase, aerobic
      Short name=Coproporphyrinogenase
      Short name=Coprogen oxidase
    EC=1.3.3.3
Gene names
Name: hemF
Ordered Locus Names: b2436, JW2429
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O. HAMAP MF_00333

Cofactor

Manganese. 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. HAMAP MF_00333

Subcellular location

Cytoplasm. HAMAP MF_00333

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   Cellular componentCytoplasm
   LigandManganese
Metal-binding
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

porphyrin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncoproporphyrinogen oxidase activity

Inferred from electronic annotation. Source: HAMAP

manganese ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Coproporphyrinogen-III oxidase, aerobic
PRO_0000109894

Sites

Metal binding961Manganese HAMAP MF_00333
Metal binding1061Manganese HAMAP MF_00333
Metal binding1451Manganese HAMAP MF_00333
Metal binding1751Manganese HAMAP MF_00333

Sequences

Sequence LengthMass (Da)Tools
P36553-1 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 53667E5C7B6D0198

FASTA29934,323
        10         20         30         40         50         60 
MKPDAHQVKQ FLLNLQDTIC QQLTAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV 

        70         80         90        100        110        120 
NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAD 

       130        140        150        160        170        180 
PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR 

       190        200        210        220        230        240 
GIGGLFFDDL NTPDFDRCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY 

       250        260        270        280        290 
VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant."
Troup B., Jahn M., Hungerer C., Jahn D.
J. Bacteriol. 176:673-680(1994) [PubMed: 8300522] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. expand/collapse author list , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation."
Breckau D., Mahlitz E., Sauerwald A., Layer G., Jahn D.
FEMS Microbiol. Lett. 226:31-37(2003) [PubMed: 13129604] [Abstract]
Cited for: CHARACTERIZATION, CRYSTALLIZATION.
[6]"Oxygen-dependent coproporphyrinogen III oxidase (HemF) from Escherichia coli is stimulated by manganese."
Breckau D., Mahlitz E., Sauerwald A., Layer G., Jahn D.
J. Biol. Chem. 278:46625-46631(2003) [PubMed: 12975365] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS OF TRP-36; HIS-96; HIS-106; TRP-123; TYR-135; HIS-145; TYR-160; TRP-166; CYS-167; TYR-170; HIS-175; TYR-213; TYR-240; TYR-276 AND TRP-298.

Cross-references

Sequence databases

X75413 Genomic DNA. Translation: CAA53167.1.
U00096 Genomic DNA. Translation: AAC75489.1.
AP009048 Genomic DNA. Translation: BAA16319.1.
PIRB36964.
RefSeqAP_003030.1.
NP_416931.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP36553. 3 interactions.

Genome annotation databases

GeneID946908.
GenomeReviewsGene locus JW2429 in contig AP009048_GR.
Gene locus b2436 in contig U00096_GR.
KEGGecj:JW2429.
eco:b2436.

Organism-specific databases

EchoBASEEB2106.
EcoGeneEG12189. hemF.
CMRSearch...

Phylogenomic databases

HOGENOMP36553.
OMAP36553. VKAYLLD.

Enzyme and pathway databases

BioCycEcoCyc:COPROGENOXI-MON.
MetaCyc:COPROGENOXI-MON.
BRENDA1.3.3.3. 246.

Family and domain databases

HAMAPMF_00333.
[Tree]
InterProIPR001260. Coprogen_oxidas.
IPR018375. Coproporphyrinogen-3_ox_CS.
[Graphical view]
Gene3DG3DSA:3.40.1500.10. Coprogen_oxidas. 1 hit.
PANTHERPTHR10755. Coprogen_oxidas. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PIRSFPIRSF000166. Coproporphyri_ox. 1 hit.
PRINTSPR00073. COPRGNOXDASE.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM6_ECOLI
AccessionPrimary (citable) accession number: P36553
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: June 16, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents