Bifunctional P-450/NADPH-P450 reductase

Preferred order of sections

Names and origin

Protein names

Recommended name:
Bifunctional P-450/NADPH-P450 reductase

Alternative name(s):
Cytochrome P450(BM-3)
Short name=Cytochrome P450BM-3

Including the following 2 domains:

Cytochrome P450 102
EC=1.14.14.1
NADPH--cytochrome P450 reductase
EC=1.6.2.4

Gene names

Name:	cyp102A1
Synonyms:	cyp102

Organism

Bacillus megaterium

Taxonomic identifier

1404 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	1049 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.
Catalytic activity	NADPH + n oxidized hemoprotein = NADP⁺ + n reduced hemoprotein. RH + reduced flavoprotein + O₂ = ROH + oxidized flavoprotein + H₂O.
Cofactor	FAD. FMN. Heme group.
Subcellular location	Cytoplasm By similarity.
Sequence similarities	In the N-terminal section; belongs to the cytochrome P450 family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Ligand	FAD FMN Flavoprotein Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	FMN binding Inferred from electronic annotation. Source: InterPro NADPH-hemoprotein reductase activity Inferred from electronic annotation. Source: EC aromatase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed

Chain

2 – 1049

1048

Bifunctional P-450/NADPH-P450 reductase

PRO_0000052205

Regions

Domain

483 – 622

140

Flavodoxin-like

Domain

660 – 892

233

FAD-binding FR-type

Region

2 – 472

471

Cytochrome P450

Region

473 – 1049

577

NADPH-P-450 reductase

Sites

Metal binding

401

1

Iron (heme axial ligand)

Secondary structure

1

.

1049

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14779 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: B0BE61F8A2EE33D5
Show »

FASTA

1,049

117,781

        10         20         30         40         50         60 
MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT RYLSSQRLIK 

        70         80         90        100        110        120 
EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA HNILLPSFSQ QAMKGYHAMM 

       130        140        150        160        170        180 
VDIAVQLVQK WERLNADEHI EVPEDMTRLT LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR 

       190        200        210        220        230        240 
ALDEAMNKLQ RANPDDPAYD ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN 

       250        260        270        280        290        300 
GKDPETGEPL DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV 

       310        320        330        340        350        360 
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK GDELMVLIPQ 

       370        380        390        400        410        420 
LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA CIGQQFALHE ATLVLGMMLK 

       430        440        450        460        470        480 
HFDFEDHTNY ELDIKETLTL KPEGFVVKAK SKKIPLGGIP SPSTEQSAKK VRKKAENAHN 

       490        500        510        520        530        540 
TPLLVLYGSN MGTAEGTARD LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH 

       550        560        570        580        590        600 
PPDNAKQFVD WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD 

       610        620        630        640        650        660 
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS AADMPLAKMH 

       670        680        690        700        710        720 
GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH LGVIPRNYEG IVNRVTARFG 

       730        740        750        760        770        780 
LDASQQIRLE AEEEKLAHLP LAKTVSVEEL LQYVELQDPV TRTQLRAMAA KTVCPPHKVE 

       790        800        810        820        830        840 
LEALLEKQAY KEQVLAKRLT MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE 

       850        860        870        880        890        900 
KQASITVSVV SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI 

       910        920        930        940        950        960 
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL ENAQSEGIIT 

       970        980        990       1000       1010       1020 
LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC GDGSQMAPAV EATLMKSYAD 

      1030       1040 
VHQVSEADAR LWLQQLEEKG RYAKDVWAG

« Hide

References

[1]	"Coding nucleotide, 5' regulatory, and deduced amino acid sequences of P-450BM-3, a single peptide cytochrome P-450:NADPH-P-450 reductase from Bacillus megaterium." Ruettinger R.T., Wen L.-P., Fulco A.J. J. Biol. Chem. 264:10987-10995(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions." Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W., Peterson J.A. Arch. Biochem. Biophys. 292:20-28(1992) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.
[3]	"Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's." Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A., Deisenhofer J. Science 261:731-736(1993) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-472.
[4]	"The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid." Li H.Y., Poulos T.L. Nat. Struct. Biol. 4:140-146(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-472.
[5]	"Structure of a cytochrome P450-redox partner electron-transfer complex." Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L. Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-650.
[6]	"Pivotal role of water in the mechanism of P450BM-3." Haines D.C., Tomchick D.R., Machius M., Peterson J.A. Biochemistry 40:13456-13465(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04832 Genomic DNA. Translation: AAA87602.1.

PIR

A34286.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BU7	X-ray	1.65	A/B	2-456	[»]
1BVY	X-ray	2.03	A/B	2-459	[»]
			F	460-650	[»]
1FAG	X-ray	2.70	A/B/C/D	2-472	[»]
1FAH	X-ray	2.30	A/B	2-471	[»]
1JME	X-ray	2.00	A/B	2-455	[»]
1JPZ	X-ray	1.65	A/B	1-471	[»]
1P0V	X-ray	2.05	A/B	2-455	[»]
1P0W	X-ray	2.00	A/B	2-455	[»]
1P0X	X-ray	2.00	A/B	2-455	[»]
1SMI	X-ray	2.00	A/B	2-471	[»]
1SMJ	X-ray	2.75	A/B/C/D	2-471	[»]
1YQO	X-ray	1.90	A/B	2-455	[»]
1YQP	X-ray	1.80	A/B	2-455	[»]
1ZO4	X-ray	1.46	A/B	2-470	[»]
1ZO9	X-ray	1.70	A/B	2-470	[»]
1ZOA	X-ray	1.74	A/B	2-470	[»]
2BMH	X-ray	2.00	A/B	2-455	[»]
2HPD	X-ray	2.00	A/B	2-472	[»]
2IJ2	X-ray	1.20	A/B	2-470	[»]
2IJ3	X-ray	1.90	A/B	2-470	[»]
2IJ4	X-ray	2.40	A/B	2-470	[»]
2J1M	X-ray	1.70	A/B	2-455	[»]
2J4S	X-ray	2.10	A/B	2-455	[»]
2NNB	X-ray	1.90	A/B	2-471	[»]
2UWH	X-ray	2.80	A/B/C/D/E/F	2-458	[»]
2X7Y	X-ray	2.10	A/B	2-456	[»]
2X80	X-ray	2.30	A/B	2-456	[»]
3BEN	X-ray	1.65	A/B	1-470	[»]
3CBD	X-ray	2.65	A/B	2-456	[»]
3DGI	X-ray	1.95	A/B	2-456	[»]
3EKB	X-ray	2.30	A/B	2-471	[»]
3EKD	X-ray	2.50	A/B	2-471	[»]
3EKF	X-ray	2.10	A/B	2-471	[»]
3HF2	X-ray	2.20	A/B	1-482	[»]
3KX3	X-ray	1.80	A/B	2-471	[»]
3KX4	X-ray	1.95	A/B	2-471	[»]
3KX5	X-ray	1.69	A/B	2-471	[»]
3M4V	X-ray	1.90	A/B	1-482	[»]
3NPL	X-ray	2.40	A/B	1-464	[»]
3PSX	X-ray	1.90	A/B	1-482	[»]
4DQK	X-ray	2.40	A/B	659-1049	[»]
4DQL	X-ray	2.15	A/B	657-1049	[»]
4DTW	X-ray	1.80	A/B	2-464	[»]
4DTY	X-ray	1.45	A/B	2-464	[»]
4DTZ	X-ray	1.55	A/B	2-464	[»]
4DU2	X-ray	1.90	A/B	1-464	[»]
4DUA	X-ray	2.00	A/B	2-464	[»]
4DUB	X-ray	1.70	A/B	1-464	[»]
4DUC	X-ray	1.92	A/B	1-464	[»]
4DUD	X-ray	1.85	A/B	2-464	[»]
4DUE	X-ray	1.70	A/B	2-464	[»]
4DUF	X-ray	1.80	A/B/C/D	2-464	[»]

ProteinModelPortal

P14779.

SMR

P14779. Positions 2-459, 480-631.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-17698.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.
1.20.990.10. 1 hit.

InterPro

IPR023206. Bifunctional_P450_P450_red.
IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]

Pfam

PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view]

PIRSF

PIRSF000209. Bifunctional_P450_P450R. 1 hit.

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.
SSF63380. Riboflavin_synthase_like_b-brl. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P14779.

Entry information

Entry name

CPXB_BACME

Accession

Primary (citable) accession number: P14779

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families