Enzyme

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     1. Oxidoreductases
        1.3 Acting on the CH-CH group of donors
            1.3.3 With oxygen as acceptor
ID:1.3.3.15
Description:Coproporphyrinogen III oxidase (coproporphyrin-forming).

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.3.3.15
BRENDA Enzyme Link: BRENDA 1.3.3.15
KEGG Enzyme Link: KEGG1.3.3.15
BioCyc Enzyme Link: BioCyc 1.3.3.15
ExPASy Enzyme Link: ExPASy1.3.3.15
EC2PDB Enzyme Link: EC2PDB 1.3.3.15
ExplorEnz Enzyme Link: ExplorEnz 1.3.3.15
PRIAM enzyme-specific profiles Link: PRIAM 1.3.3.15
IntEnz Enzyme Link: IntEnz 1.3.3.15
MEDLINE Enzyme Link: MEDLINE 1.3.3.15
MSA:

1.3.3.15;

Phylogenetic Tree:

1.3.3.15;

Uniprot:
M-CSA:
RHEA:43436 coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
RULE(radius=1) ([*:1]-[CH2;+0:2]-[*:3]:[nH;+0:4]:[*:5]-[CH2;+0:6]-[*:7].[*:8]-[CH2;+0:9]-[*:10]:[nH;+0:11]:[*:12]-[CH2;+0:13]-[*:14]).[O;H0;+0:15]=[O;H0;+0:16].[O;H0;+0:17]=[O;H0;+0:18].[O;H0;+0:19]=[O;H0;+0:20]>>([*:1]:[cH;+0:2]:[*:3]:[n;H0;+0:4]:[*:5]:[cH;+0:6]:[*:7].[*:8]:[cH;+0:9]:[*:10]:[n;H0;+0:11]:[*:12]:[cH;+0:13]:[*:14]).[OH;+0:15]-[OH;+0:16].[OH;+0:17]-[OH;+0:18].[OH;+0:19]-[OH;+0:20]
Reaction
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References

TitleAuthorsDatePubMed ID
Purification of and kinetic studies on a cloned protoporphyrinogen oxidase from the aerobic bacterium Bacillus subtilis.Corrigall AV, Siziba KB, Maneli MH, Shephard EG, Ziman M, Dailey TA, Dailey HA, Kirsch RE, Meissner PN1998 Oct 159784236
Bacillus subtilis HemY is a peripheral membrane protein essential for protoheme IX synthesis which can oxidize coproporphyrinogen III and protoporphyrinogen IX.Hansson M, Hederstedt L1994 Oct7928957
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin.Dailey HA, Gerdes S, Dailey TA, Burch JS, Phillips JD2015 Feb 1725646457
Structural insight into unique properties of protoporphyrinogen oxidase from Bacillus subtilis.Qin X, Sun L, Wen X, Yang X, Tan Y, Jin H, Cao Q, Zhou W, Xi Z, Shen Y2010 Apr19944166