AC   MF_00333;
DC   Protein; auto
TR   HAMAP; MF_00333; -; 1; level=0
XX
Names: Coprogen_oxidas
XX
ID   HEM6
DE   RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase;
DE            Short=CPO;
DE            Short=Coprogen oxidase;
DE            Short=Coproporphyrinogenase;
DE            EC=1.3.3.3;
GN   Name=hemF;
XX
case <OC:Cyanobacteriota>
CC   -!- FUNCTION: Involved in the heme and chlorophyll biosynthesis. Catalyzes
CC       the aerobic oxidative decarboxylation of propionate groups of rings A
CC       and B of coproporphyrinogen-III to yield the vinyl groups in
CC       protoporphyrinogen-IX.
else
CC   -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic
CC       oxidative decarboxylation of propionate groups of rings A and B of
CC       coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-
CC       IX.
end case
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=coproporphyrinogen III + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC         protoporphyrinogen IX; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3;
case <OC:Escherichia>
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
else
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
end case
CC   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2
CC       route): step 1/1.
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family.
XX
DR   Pfam; PF01218; Coprogen_oxidas; 1; trigger=no
DR   PRINTS; PR00073; COPRGNOXDASE; 1; trigger=no
DR   PROSITE; PS01021; COPROGEN_OXIDASE; 1; trigger=no
XX
case <OC:Cyanobacteriota>
KW   Chlorophyll biosynthesis
end case
KW   Cytoplasm
KW   Heme biosynthesis
case <OC:Escherichia>
KW   Manganese
end case
KW   Metal-binding
KW   Oxidoreductase
KW   Porphyrin biosynthesis
XX
GO   GO:0004109; F:coproporphyrinogen oxidase activity
case <OC:Escherichia>
GO   GO:0030145; F:manganese ion binding
end case
GO   GO:0042803; F:protein homodimerization activity
GO   GO:0006779; P:porphyrin-containing compound biosynthetic process
GO   GO:0006783; P:heme biosynthetic process
case <OC:Cyanobacteriota>
GO   GO:0015995; P:chlorophyll biosynthetic process
end case
GO   GO:0005737; C:cytoplasm
XX
FT   From: HEM6_ECOLI (P36553)
FT   BINDING         108..110
FT                   /ligand="substrate"
FT   Condition: N-x-R
FT   REGION          240..275
FT                   /note="Important for dimerization"
FT   BINDING         258..260
FT                   /ligand="substrate"
FT   Condition: G-x-[NR]
FT   ACT_SITE        106
FT                   /note="Proton donor"
FT   Condition: H
case <OC:Escherichia>
FT   BINDING         96
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         106
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         145
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
FT   BINDING         175
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT   Condition: H
else
FT   BINDING         96
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         106
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         145
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
FT   BINDING         175
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT   Condition: H
end case
FT   BINDING         92
FT                   /ligand="substrate"
FT   Condition: S
FT   SITE            175
FT                   /note="Important for dimerization"
FT   Condition: H
XX
Size: 279-363;
Related: None;
Template: P36553; P72848;
Scope:
 Bacteria
Fusion:
 Nter: None
 Cter: None
Duplicate: in NOSS1
Plasmid: None
Comments: None
XX
# Revision 1.45 2023/02/17
//