Identification
Name:Oxygen-independent coproporphyrinogen-III oxidase
Synonyms:
  • Coprogen oxidase
  • Coproporphyrinogenase
Gene Name:hemN
Enzyme Class:
Biological Properties
General Function:Involved in coproporphyrinogen oxidase activity
Specific Function:Anaerobic transformation of coproporphyrinogen-III into protoporphyrinogen-IX
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Porphyrin and chlorophyll metabolism ec00860
KEGG Reactions:
2.0Thumb+1.0Thumb2.0Thumb+2.0Thumb+2.0Thumb+1.0Thumb
SMPDB Reactions:
1.0S-adenosyl-L-methionine+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB211745'-DeoxyadenosineMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB00570Coproporphyrin IIIMetaboCard
ECMDB01261Coproporphyrinogen IIIMetaboCard
ECMDB00696L-MethionineMetaboCard
ECMDB01097Protoporphyrinogen IXMetaboCard
ECMDB01185S-AdenosylmethionineMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
coproporphyrinogen oxidase activity
iron-sulfur cluster binding
metal cluster binding
oxidoreductase activity
oxidoreductase activity, acting on the CH-CH group of donors
oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
Process
metabolic process
nitrogen compound metabolic process
oxidation reduction
porphyrin biosynthetic process
porphyrin metabolic process
tetrapyrrole metabolic process
Gene Properties
Blattner:b3867
Gene OrientationClockwise
Centisome Percentage:87.29
Left Sequence End4050068
Right Sequence End4051441
Gene Sequence:
>1374 bp
ATGGAAAGTAAGAACAAGCTAAAGCGTGGGCTAAGTACCCGCCACATACGCTTTATGGCA
CTGGGTTCAGCAATTGGCACCGGGCTGTTTTACGGTTCGGCAGACGCCATCAAAATGGCC
GGTCCGAGCGTGTTGTTGGCCTATATTATCGGTGGTATCGCGGCGTATATCATTATGCGT
GCGCTGGGGGAAATGTCGGTACATAACCCGGCCGCCAGCTCTTTCTCGCGTTATGCGCAG
GAAAACCTCGGCCCGCTGGCAGGTTACATTACCGGCTGGACCTACTGCTTTGAAATCCTT
ATTGTCGCCATCGCCGATGTGACCGCTTTTGGTATCTATATGGGTGTCTGGTTCCCGACG
GTGCCGCACTGGATTTGGGTACTGAGCGTGGTGCTGATCATTTGCGCCGTAAACCTGATG
AGCGTGAAGGTATTCGGTGAGCTGGAATTCTGGTTCTCGTTCTTTAAAGTCGCCACCATC
ATCATCATGATTGTCGCCGGTTTCGGCATCATCATCTGGGGGATTGGCAACGGCGGGCAA
CCGACCGGTATTCATAACCTGTGGAGCAACGGCGGCTTCTTCAGTAACGGCTGGCTTGGC
ATGGTAATGTCGTTGCAAATGGTGATGTTTGCTTACGGTGGGATCGAAATTATCGGGATT
ACCGCCGGTGAAGCGAAAGATCCTGAGAAATCGATACCGCGTGCGATTAACTCCGTGCCG
ATGCGTATTCTGGTGTTCTACGTCGGTACGCTGTTCGTCATTATGTCTATCTACCCGTGG
AATCAGGTTGGCACTGCCGGTAGCCCGTTCGTGCTGACGTTCCAGCATATGGGCATTACC
TTTGCCGCCAGCATTCTTAACTTTGTTGTGCTGACTGCTTCGCTGTCGGCAATTAACAGT
GATGTATTTGGCGTAGGCCGTATGCTCCACGGTATGGCAGAGCAGGGCAGCGCGCCGAAA
ATTTTCAGCAAAACGTCGCGTCGCGGTATTCCGTGGGTTACGGTGCTGGTGATGACTACC
GCGCTGCTGTTTGCGGTGTATCTGAACTACATCATGCCGGAAAACGTCTTCCTGGTGATC
GCTTCGCTGGCAACCTTCGCCACGGTGTGGGTGTGGATTATGATCCTGCTGTCGCAAATT
GCCTTCCGTCGCCGTTTGCCGCCAGAAGAAGTTAAGGCGCTGAAATTTAAAGTGCCGGGT
GGGGTAGCAACGACCATCGGCGGGCTGATTTTCCTGCTCTTTATTATCGGGTTGATTGGT
TATCACCCGGATACGCGTATCTCGCTGTATGTCGGTTTCGCGTGGATTGTTGTGCTGTTG
ATTGGCTGGATGTTTAAACGCCGCCACGATCGTCAGCTGGCTGAAAACCAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:457
Protein Molecular Weight:52729
Protein Theoretical pI:6
PDB File:1OLT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Oxygen-independent coproporphyrinogen-III oxidase
MSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIP
FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYLNK
AQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQR
LVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAELNPDRLSVF
NYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVA
QREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRG
IALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDVDE
KGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI
References
External Links:
ResourceLink
Uniprot ID:P32131
Uniprot Name:HEMN_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674542
PDB ID:1OLT
Ecogene ID:EG11836
Ecocyc:EG11836
ColiBase:b3867
Kegg Gene:b3867
EchoBASE ID:EB1782
CCDB:HEMN_ECOLI
BacMap:90111657
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Layer, G., Grage, K., Teschner, T., Schunemann, V., Breckau, D., Masoumi, A., Jahn, M., Heathcote, P., Trautwein, A. X., Jahn, D. (2005). "Radical S-adenosylmethionine enzyme coproporphyrinogen III oxidase HemN: functional features of the [4Fe-4S] cluster and the two bound S-adenosyl-L-methionines." J Biol Chem 280:29038-29046. Pubmed: 15967800
  • Layer, G., Moser, J., Heinz, D. W., Jahn, D., Schubert, W. D. (2003). "Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes." EMBO J 22:6214-6224. Pubmed: 14633981
  • Layer, G., Verfurth, K., Mahlitz, E., Jahn, D. (2002). "Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli." J Biol Chem 277:34136-34142. Pubmed: 12114526
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Troup, B., Hungerer, C., Jahn, D. (1995). "Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase." J Bacteriol 177:3326-3331. Pubmed: 7768836