UniProt functional annotation for P14779



	UniProt functional annotation for P14779

UniProt code: P14779.

Organism: Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512).

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

Function: Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460). {ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081}.

Catalytic activity: Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA- COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};

Catalytic activity: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269|PubMed:11695889, ECO:0000269|PubMed:11695892, ECO:0000269|PubMed:14653735, ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:16566047, ECO:0000269|PubMed:17077084, ECO:0000269|PubMed:1727637, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18020460, ECO:0000269|PubMed:18298086, ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374, ECO:0000269|PubMed:21875028, ECO:0000269|PubMed:3106359, ECO:0000269|PubMed:7578081};

Cofactor: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:7578081};

Cofactor: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:10051560};

Cofactor: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374};

Activity regulation: Inhibited by N-(12-imidazolyl-dodecanoyl)-L- leucine. {ECO:0000269|PubMed:18298086}.

Biophysicochemical properties: Kinetic parameters: KM=250 uM for lauric acid at pH 7.4 at room temperature {ECO:0000269|PubMed:18020460}; KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone {ECO:0000269|PubMed:18020460}; KM=210 uM for N-beta-oxolauroyl-DL-homoserine {ECO:0000269|PubMed:18020460}; KM=140 uM for N-lauroyl-DL-homoserine {ECO:0000269|PubMed:18020460}; KM=322 uM for lauric acid at pH 7.5 and 15 degrees Celsius {ECO:0000269|PubMed:16403573}; KM=265 uM for lauric acid {ECO:0000269|PubMed:17868686}; KM=16 mM for indole {ECO:0000269|PubMed:17868686}; KM=87.4 uM for laurate/dodecanoate at pH 7.0 and 25 degrees Celsius {ECO:0000269|PubMed:18721129}; KM=230 uM for lauric acid at pH 7.4 {ECO:0000269|PubMed:19492389}; KM=87.4 uM for laurate/dodecanoate at 25 degrees Celsius {ECO:0000269|PubMed:20180779}; KM=5.1 uM for arachidonate at 25 degrees Celsius {ECO:0000269|PubMed:20180779}; KM=42.4 uM for palmitic acid at pH 7.4 and 30 degrees Celsius {ECO:0000269|PubMed:21110374}; Note=kcat is 84.1 s(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N- palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine. kcat is 485 min(-1) for N-palmitoyl-L-glutamic acid. kcat is 1160 min(-1) for N- palmitoyl-L-leucine (PubMed:18004886). kcat is 28 s(-1) for lauric acid (PubMed:17868686). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:18721129). kcat is 77 for lauric acid (PubMed:19492389). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:20180779). kcat is 16400 min(-1) for arachidonate (PubMed:20180779). kcat is 91.4 for palmitic acid (PubMed:21110374). {ECO:0000269|PubMed:16403573, ECO:0000269|PubMed:17868686, ECO:0000269|PubMed:18004886, ECO:0000269|PubMed:18721129, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:20180779, ECO:0000269|PubMed:21110374};

Subcellular location: Cytoplasm {ECO:0000250}.

Induction: By pentobarbital (PubMed:1544926, PubMed:3106359). Expression is negatively regulated by repressor bm3R1 at the transcriptional level (PubMed:1544926). {ECO:0000269|PubMed:1544926, ECO:0000269|PubMed:3106359}.

Biotechnology: This protein is a target of protein engineering. Its selectivity-directing and activity-enhancing mutations have been extensively studied and the designed mutations allow this enzyme to act on non-native substrates and/or in order to enhance production of synthetically desirable end-products. {ECO:0000269|PubMed:18619466, ECO:0000269|PubMed:19492389, ECO:0000269|PubMed:21110374, ECO:0000305}.

Similarity: In the N-terminal section; belongs to the cytochrome P450 family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512).
Taxonomy:		Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Priestia.



Function:		Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028). Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637). Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466). Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047). Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028). Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460). {ECO:0000269\|PubMed:11695892, ECO:0000269\|PubMed:14653735, ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:16566047, ECO:0000269\|PubMed:17077084, ECO:0000269\|PubMed:1727637, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18020460, ECO:0000269\|PubMed:18298086, ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:21110374, ECO:0000269\|PubMed:21875028, ECO:0000269\|PubMed:3106359, ECO:0000269\|PubMed:7578081}.


Catalytic activity:		Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA- COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378, ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60344; EC=1.6.2.4; Evidence={ECO:0000269\|PubMed:11695889, ECO:0000269\|PubMed:11695892, ECO:0000269\|PubMed:14653735, ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:16566047, ECO:0000269\|PubMed:17077084, ECO:0000269\|PubMed:1727637, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18020460, ECO:0000269\|PubMed:18298086, ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:21110374, ECO:0000269\|PubMed:21875028, ECO:0000269\|PubMed:3106359, ECO:0000269\|PubMed:7578081};
Catalytic activity:		Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA- COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:142491; EC=1.14.14.1; Evidence={ECO:0000269\|PubMed:11695889, ECO:0000269\|PubMed:11695892, ECO:0000269\|PubMed:14653735, ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:16566047, ECO:0000269\|PubMed:17077084, ECO:0000269\|PubMed:1727637, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18020460, ECO:0000269\|PubMed:18298086, ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:21110374, ECO:0000269\|PubMed:21875028, ECO:0000269\|PubMed:3106359, ECO:0000269\|PubMed:7578081};
Cofactor:		Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269\|PubMed:7578081};
Cofactor:		Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269\|PubMed:10051560};
Cofactor:		Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:21110374};
Activity regulation:		Inhibited by N-(12-imidazolyl-dodecanoyl)-L- leucine. {ECO:0000269\|PubMed:18298086}.
Biophysicochemical properties:		Kinetic parameters: KM=250 uM for lauric acid at pH 7.4 at room temperature {ECO:0000269\|PubMed:18020460}; KM=34 uM for N-beta-oxolauroyl-DL-homoserine lactone {ECO:0000269\|PubMed:18020460}; KM=210 uM for N-beta-oxolauroyl-DL-homoserine {ECO:0000269\|PubMed:18020460}; KM=140 uM for N-lauroyl-DL-homoserine {ECO:0000269\|PubMed:18020460}; KM=322 uM for lauric acid at pH 7.5 and 15 degrees Celsius {ECO:0000269\|PubMed:16403573}; KM=265 uM for lauric acid {ECO:0000269\|PubMed:17868686}; KM=16 mM for indole {ECO:0000269\|PubMed:17868686}; KM=87.4 uM for laurate/dodecanoate at pH 7.0 and 25 degrees Celsius {ECO:0000269\|PubMed:18721129}; KM=230 uM for lauric acid at pH 7.4 {ECO:0000269\|PubMed:19492389}; KM=87.4 uM for laurate/dodecanoate at 25 degrees Celsius {ECO:0000269\|PubMed:20180779}; KM=5.1 uM for arachidonate at 25 degrees Celsius {ECO:0000269\|PubMed:20180779}; KM=42.4 uM for palmitic acid at pH 7.4 and 30 degrees Celsius {ECO:0000269\|PubMed:21110374}; Note=kcat is 84.1 s(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N- palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine. kcat is 485 min(-1) for N-palmitoyl-L-glutamic acid. kcat is 1160 min(-1) for N- palmitoyl-L-leucine (PubMed:18004886). kcat is 28 s(-1) for lauric acid (PubMed:17868686). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:18721129). kcat is 77 for lauric acid (PubMed:19492389). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:20180779). kcat is 16400 min(-1) for arachidonate (PubMed:20180779). kcat is 91.4 for palmitic acid (PubMed:21110374). {ECO:0000269\|PubMed:16403573, ECO:0000269\|PubMed:17868686, ECO:0000269\|PubMed:18004886, ECO:0000269\|PubMed:18721129, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:20180779, ECO:0000269\|PubMed:21110374};
Subcellular location:		Cytoplasm {ECO:0000250}.
Induction:		By pentobarbital (PubMed:1544926, PubMed:3106359). Expression is negatively regulated by repressor bm3R1 at the transcriptional level (PubMed:1544926). {ECO:0000269\|PubMed:1544926, ECO:0000269\|PubMed:3106359}.
Biotechnology:		This protein is a target of protein engineering. Its selectivity-directing and activity-enhancing mutations have been extensively studied and the designed mutations allow this enzyme to act on non-native substrates and/or in order to enhance production of synthetically desirable end-products. {ECO:0000269\|PubMed:18619466, ECO:0000269\|PubMed:19492389, ECO:0000269\|PubMed:21110374, ECO:0000305}.
Similarity:		In the N-terminal section; belongs to the cytochrome P450 family. {ECO:0000305}.