UniProt functional annotation for P32396



	UniProt functional annotation for P32396

UniProt code: P32396.

Organism: Bacillus subtilis (strain 168).

Taxonomy: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.

Function: Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666). {ECO:0000269|PubMed:12761666, ECO:0000269|PubMed:1459957, ECO:0000269|PubMed:16140324, ECO:0000269|PubMed:21052751, ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396, ECO:0000269|PubMed:8119288}.

Catalytic activity: Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+); Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9; Evidence={ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49573; Evidence={ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396};

Activity regulation: Stimulated by Mg(2+) (PubMed:12761666). Inhibited by Cd(2+) (PubMed:12761666). Inhibited by N-methylmesoporphyrin (N- MeMP) and 2,4-disulfonic acid deuteroporphyrin IX (dSDP) (PubMed:10704318, PubMed:16140324, PubMed:18423489). {ECO:0000269|PubMed:10704318, ECO:0000269|PubMed:12761666, ECO:0000269|PubMed:16140324, ECO:0000269|PubMed:18423489}.

Biophysicochemical properties: Kinetic parameters: KM=7.8 uM for coproporphyrin III {ECO:0000269|PubMed:25646457}; KM=0.15 uM for Fe(2+) {ECO:0000269|PubMed:25908396}; KM=17 uM for Zn(2+) {ECO:0000269|PubMed:8119288}; KM=170 uM for Cu(2+) {ECO:0000269|PubMed:8119288}; Note=kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396). {ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:25908396}; pH dependence: Optimum pH is 7.2 with Zn(2+) and protoporphyrin IX as substrates. {ECO:0000269|PubMed:8119288};

Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:1459957, ECO:0000269|PubMed:25646457, ECO:0000269|PubMed:8119288, ECO:0000305|PubMed:25711532}.

Subunit: Monomer. {ECO:0000269|PubMed:8119288}.

Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00323, ECO:0000269|PubMed:8119288}.

Disruption phenotype: Deletion mutant requires hemin for growth. {ECO:0000269|PubMed:8119288}.

Similarity: Belongs to the ferrochelatase family. {ECO:0000255|HAMAP- Rule:MF_00323, ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus subtilis (strain 168).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.



Function:		Involved in coproporphyrin-dependent heme b biosynthesis (PubMed:25646457, PubMed:25908396). Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III (PubMed:25646457, PubMed:25908396). It can also insert iron into protoporphyrin IX (PubMed:1459957, PubMed:8119288, PubMed:21052751, PubMed:25646457). Has weaker activity with 2,4 disulfonate, deuteroporphyrin and 2,4 hydroxyethyl (PubMed:25646457, PubMed:12761666). In vitro, can also use Zn(2+) or Cu(2+) (PubMed:8119288, PubMed:16140324, PubMed:21052751, PubMed:12761666). {ECO:0000269\|PubMed:12761666, ECO:0000269\|PubMed:1459957, ECO:0000269\|PubMed:16140324, ECO:0000269\|PubMed:21052751, ECO:0000269\|PubMed:25646457, ECO:0000269\|PubMed:25908396, ECO:0000269\|PubMed:8119288}.


Catalytic activity:		Reaction=Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+); Xref=Rhea:RHEA:49572, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:68438, ChEBI:CHEBI:131725; EC=4.99.1.9; Evidence={ECO:0000255\|HAMAP-Rule:MF_00323, ECO:0000269\|PubMed:25646457, ECO:0000269\|PubMed:25908396}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49573; Evidence={ECO:0000255\|HAMAP-Rule:MF_00323, ECO:0000269\|PubMed:25646457, ECO:0000269\|PubMed:25908396};
Activity regulation:		Stimulated by Mg(2+) (PubMed:12761666). Inhibited by Cd(2+) (PubMed:12761666). Inhibited by N-methylmesoporphyrin (N- MeMP) and 2,4-disulfonic acid deuteroporphyrin IX (dSDP) (PubMed:10704318, PubMed:16140324, PubMed:18423489). {ECO:0000269\|PubMed:10704318, ECO:0000269\|PubMed:12761666, ECO:0000269\|PubMed:16140324, ECO:0000269\|PubMed:18423489}.
Biophysicochemical properties:		Kinetic parameters: KM=7.8 uM for coproporphyrin III {ECO:0000269\|PubMed:25646457}; KM=0.15 uM for Fe(2+) {ECO:0000269\|PubMed:25908396}; KM=17 uM for Zn(2+) {ECO:0000269\|PubMed:8119288}; KM=170 uM for Cu(2+) {ECO:0000269\|PubMed:8119288}; Note=kcat is 0.11 min(-1) with coproporphyrin III as substrate (PubMed:25646457). kcat is 78 min(-1) with Fe(2+) as substrate (PubMed:25908396). {ECO:0000269\|PubMed:25646457, ECO:0000269\|PubMed:25908396}; pH dependence: Optimum pH is 7.2 with Zn(2+) and protoporphyrin IX as substrates. {ECO:0000269\|PubMed:8119288};
Pathway:		Porphyrin-containing compound metabolism; protoheme biosynthesis. {ECO:0000255\|HAMAP-Rule:MF_00323, ECO:0000269\|PubMed:1459957, ECO:0000269\|PubMed:25646457, ECO:0000269\|PubMed:8119288, ECO:0000305\|PubMed:25711532}.
Subunit:		Monomer. {ECO:0000269\|PubMed:8119288}.
Subcellular location:		Cytoplasm {ECO:0000255\|HAMAP-Rule:MF_00323, ECO:0000269\|PubMed:8119288}.
Disruption phenotype:		Deletion mutant requires hemin for growth. {ECO:0000269\|PubMed:8119288}.
Similarity:		Belongs to the ferrochelatase family. {ECO:0000255\|HAMAP- Rule:MF_00323, ECO:0000305}.