BACMB:CPXB

Species (Taxon ID)	Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC15308 / NCIMB 9376 / NCTC 10342 / VKM B-512). (1348623)
Gene Name(s)	cyp102A1 (ECO:0000312 with EMBL:AJI21949.1) (synonyms: cyp102)
Protein Name(s)	Bifunctional cytochrome P450/NADPH--P450 reductase (ECO:0000305) Cytochrome P450(BM-3) (ECO:0000303 with PMID:15299332^[1]) Cytochrome P450BM-3 (ECO:0000303 with PMID:8342039^[2], ECO:0000312 with EMBL:AAK19020.1) Fatty acid monooxygenase (ECO:0000303 with PMID:3106359^[3]) Flavocytochrome P450 BM3 (ECO:0000303 with PMID:11695889^[4], ECO:0000303 with PMID:14653735^[5]) Cytochrome P450 102A1 NADPH--cytochrome P450 reductase
External Links
UniProt	P14779
EMBL	J04832 CP009920 S87512
PIR	A34286
RefSeq	WP_034650526.1
PDB	1BU7 1BVY 1FAG 1FAH 1JME 1JPZ 1P0V 1P0W 1P0X 1SMI 1SMJ 1YQO 1YQP 1ZO4 1ZO9 1ZOA 2BMH 2HPD 2IJ2 2IJ3 2IJ4 2J1M 2J4S 2NNB 2UWH 2X7Y 2X80 3BEN 3CBD 3DGI 3EKB 3EKD 3EKF 3HF2 3KX3 3KX4 3KX5 3M4V 3NPL 3PSX 3WSP 4DQK 4DQL 4DTW 4DTY 4DTZ 4DU2 4DUA 4DUB 4DUC 4DUD 4DUE 4DUF 4H23 4H24 4HGF 4HGG 4HGH 4HGI 4HGJ 4KEW 4KEY 4KF0 4KF2 4KPA 4KPB 4O4P 4RSN 4WG2 5DYP 5DYZ 5E9Z
PDBsum	1BU7 1BVY 1FAG 1FAH 1JME 1JPZ 1P0V 1P0W 1P0X 1SMI 1SMJ 1YQO 1YQP 1ZO4 1ZO9 1ZOA 2BMH 2HPD 2IJ2 2IJ3 2IJ4 2J1M 2J4S 2NNB 2UWH 2X7Y 2X80 3BEN 3CBD 3DGI 3EKB 3EKD 3EKF 3HF2 3KX3 3KX4 3KX5 3M4V 3NPL 3PSX 3WSP 4DQK 4DQL 4DTW 4DTY 4DTZ 4DU2 4DUA 4DUB 4DUC 4DUD 4DUE 4DUF 4H23 4H24 4HGF 4HGG 4HGH 4HGI 4HGJ 4KEW 4KEY 4KF0 4KF2 4KPA 4KPB 4O4P 4RSN 4WG2 5DYP 5DYZ 5E9Z
ProteinModelPortal	P14779
SMR	P14779
MINT	MINT-8313368
STRING	545693.BMQ_3237
EnsemblBacteria	AJI21949
eggNOG	ENOG4107EER COG0369
BioCyc	MetaCyc:MONOMER-17698
BRENDA	1.14.14.1 1.6.2.4
EvolutionaryTrace	P14779
Proteomes	UP000031829
GO	GO:0005737 GO:0070330 GO:0010181 GO:0020037 GO:0042802 GO:0005506 GO:0003958
Gene3D	1.10.630.10 1.20.990.10 3.40.50.360
InterPro	IPR023206 IPR001128 IPR017972 IPR003097 IPR017927 IPR001094 IPR008254 IPR001709 IPR029039 IPR023173 IPR001433 IPR017938
Pfam	PF00667 PF00258 PF00175 PF00067
PIRSF	PIRSF000209
PRINTS	PR00369 PR00371
SUPFAM	SSF48264 SSF52218 SSF63380
PROSITE	PS00086 PS51384 PS50902

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:0009055	electron carrier activity	other:GO_REF:0000100	ECO:0000247		PMID:2334437^[6]	F	The transfer annotation HHpred hits had an E-value of 5.5E-28, a similarity of 100%, and a query coverage of 87.35% which serves as the evidence.	complete CACAO 12048
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:11695889^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:11695889^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:11695892^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:16566047^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:1727637^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:18020460^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	PMID:3106359^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:7578081^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:7578081^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:7578081^[11]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:3106359^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:3106359^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:18020460^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:18020460^[10]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:1727637^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:1727637^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:16566047^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:16566047^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:11695892^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:11695892^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	PMID:11695889^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0016712	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen	PMID:11695889^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	PMID:17077084^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22356131^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14779	F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023206	F	Seeded From UniProt	complete
enables	GO:0005506	iron ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR036396	F	Seeded From UniProt	complete
enables	GO:0010181	FMN binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001094 InterPro:IPR008254	F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001433 InterPro:IPR001709 InterPro:IPR003097 InterPro:IPR017927 InterPro:IPR023173	F	Seeded From UniProt	complete
enables	GO:0016705	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR017972 InterPro:IPR036396	F	Seeded From UniProt	complete
enables	GO:0020037	heme binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001128 InterPro:IPR036396	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001094 InterPro:IPR001128 InterPro:IPR001433 InterPro:IPR001709 InterPro:IPR003097 InterPro:IPR017927 InterPro:IPR017972 InterPro:IPR023173 InterPro:IPR023206 InterPro:IPR036396	P	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR023206	F	Seeded From UniProt	complete
enables	GO:0003958	NADPH-hemoprotein reductase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.6.2.4	F	Seeded From UniProt	complete
enables	GO:0070330	aromatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:1.14.14.1	F	Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0560	F	Seeded From UniProt	complete
enables	GO:0004497	monooxygenase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0503	F	Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0249 UniProtKB-KW:KW-0560	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Li, H & Poulos, TL (1995) Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3). Acta Crystallogr. D Biol. Crystallogr. 51 21-32 PubMed GONUTS page
↑ Ravichandran, KG et al. (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261 731-6 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Wen, LP & Fulco, AJ (1987) Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts. J. Biol. Chem. 262 6676-82 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Ost, TW et al. (2001) Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Biochemistry 40 13430-8 PubMed GONUTS page
↑ Ost, TW et al. (2003) Oxygen activation and electron transfer in flavocytochrome P450 BM3. J. Am. Chem. Soc. 125 15010-20 PubMed GONUTS page
↑ Helms, LR et al. (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168 809-17 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Haines, DC et al. (2001) Pivotal role of water in the mechanism of P450BM-3. Biochemistry 40 13456-65 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Budde, M et al. (2006) Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. Chembiochem 7 789-94 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Boddupalli, SS et al. (1992) Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions. Arch. Biochem. Biophys. 292 20-8 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 Chowdhary, PK et al. (2007) Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones and acyl homoserines. Biochemistry 46 14429-37 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 Yeom, H et al. (1995) The role of Thr268 in oxygen activation of cytochrome P450BM-3. Biochemistry 34 14733-40 PubMed GONUTS page
↑ Girvan, HM et al. (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. J. Biol. Chem. 282 564-72 PubMed GONUTS page
↑ Joyce, MG et al. (2012) The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. FEBS J. 279 1694-706 PubMed GONUTS page

[PMID:15299332-1] Li, H & Poulos, TL (1995) Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3). Acta Crystallogr. D Biol. Crystallogr. 51 21-32 PubMed GONUTS page

[PMID:8342039-2] Ravichandran, KG et al. (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's. Science 261 731-6 PubMed GONUTS page

[PMID:3106359-3] 3.0 ^3.1 ^3.2 ^3.3 Wen, LP & Fulco, AJ (1987) Cloning of the gene encoding a catalytically self-sufficient cytochrome P-450 fatty acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts. J. Biol. Chem. 262 6676-82 PubMed GONUTS page

[PMID:11695889-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Ost, TW et al. (2001) Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3. Biochemistry 40 13430-8 PubMed GONUTS page

[PMID:14653735-5] Ost, TW et al. (2003) Oxygen activation and electron transfer in flavocytochrome P450 BM3. J. Am. Chem. Soc. 125 15010-20 PubMed GONUTS page

[PMID:2334437-6] Helms, LR et al. (1990) Identification, sequence determination, and expression of the flavodoxin gene from Desulfovibrio salexigens. Biochem. Biophys. Res. Commun. 168 809-17 PubMed GONUTS page

[PMID:11695892-7] 7.0 ^7.1 ^7.2 Haines, DC et al. (2001) Pivotal role of water in the mechanism of P450BM-3. Biochemistry 40 13456-65 PubMed GONUTS page

[PMID:16566047-8] 8.0 ^8.1 ^8.2 Budde, M et al. (2006) Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. Chembiochem 7 789-94 PubMed GONUTS page

[PMID:1727637-9] 9.0 ^9.1 ^9.2 Boddupalli, SS et al. (1992) Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions. Arch. Biochem. Biophys. 292 20-8 PubMed GONUTS page

[PMID:18020460-10] 10.0 ^10.1 ^10.2 Chowdhary, PK et al. (2007) Bacillus megaterium CYP102A1 oxidation of acyl homoserine lactones and acyl homoserines. Biochemistry 46 14429-37 PubMed GONUTS page

[PMID:7578081-11] 11.0 ^11.1 ^11.2 Yeom, H et al. (1995) The role of Thr268 in oxygen activation of cytochrome P450BM-3. Biochemistry 34 14733-40 PubMed GONUTS page

[PMID:17077084-12] Girvan, HM et al. (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets. New heme ligation states influence conformational equilibria in P450 BM3. J. Biol. Chem. 282 564-72 PubMed GONUTS page

[PMID:22356131-13] Joyce, MG et al. (2012) The crystal structure of the FAD/NADPH-binding domain of flavocytochrome P450 BM3. FEBS J. 279 1694-706 PubMed GONUTS page

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BACMB:CPXB

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