Reviewed, UniProtKB/Swiss-Prot P14779 (CPXB_BACME)

Names and origin

Protein names

Recommended name:
    Bifunctional P-450/NADPH-P450 reductase
Alternative name(s):
    Cytochrome P450(BM-3)
      Short name=P450BM-3
Including the following 2 domains:
    1- Recommended name:
            Cytochrome P450 102
              EC=1.14.14.1
    2- Recommended name:
            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 › 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 transport 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
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

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

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1049

Helix Strand Turn

Details...

Helix

13 – 15

3

Helix

18 – 21

4

Helix

26 – 37

12

Beta strand

39 – 45

7

Beta strand

48 – 53

6

Helix

56 – 62

7

Turn

65 – 67

3

Beta strand

68 – 70

3

Helix

74 – 83

10

Helix

95 – 104

10

Helix

105 – 108

4

Turn

110 – 112

3

Helix

113 – 132

20

Helix

142 – 159

18

Helix

165 – 167

3

Helix

173 – 187

15

Helix

188 – 190

3

Helix

197 – 199

3

Helix

200 – 227

28

Helix

234 – 240

7

Turn

244 – 246

3

Helix

252 – 283

32

Helix

285 – 298

14

Beta strand

301 – 303

3

Helix

306 – 311

6

Helix

313 – 325

13

Beta strand

331 – 338

8

Beta strand

340 – 342

3

Turn

343 – 345

3

Beta strand

346 – 348

3

Beta strand

353 – 357

5

Helix

358 – 361

4

Helix

365 – 368

4

Helix

377 – 380

4

Helix

383 – 385

3

Helix

397 – 399

3

Helix

404 – 421

18

Beta strand

422 – 425

4

Beta strand

434 – 442

9

Beta strand

446 – 451

6

Beta strand

483 – 488

6

Beta strand

490 – 492

3

Helix

493 – 506

14

Turn

507 – 509

3

Beta strand

513 – 516

4

Helix

517 – 519

3

Beta strand

526 – 534

9

Turn

543 – 545

3

Helix

546 – 553

8

Beta strand

565 – 571

7

Helix

576 – 578

3

Helix

581 – 591

11

Turn

592 – 594

3

Beta strand

599 – 605

7

Helix

610 – 628

19

Sequences

	Sequence		Length	Mass (Da)
	P14779-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: B0BE61F8A2EE33D5	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

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: 2544578] [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: 1727637] [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: 8342039] [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: 9033595] [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: 10051560] [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: 11695892] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J04832 Genomic DNA. Translation: AAA87602.1.

PIR

A34286.

3D structure databases

PDBPDBe

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	[»]
3BEN	X-ray	1.65	A/B	1-470	[»]
3CBD	X-ray	2.65	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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.14.14.1. 325.
1.6.2.4. 325.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR003097. FAD-binding_1.
IPR017927. Fd_Rdtase_FAD-bd.
IPR001094. Flavdoxin-like.
IPR008254. Flavodoxin/NO_synth.
IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase.
IPR015702. NADPH_Cyt_P450_Rdtase.
IPR001433. OxRdtase_FAD/NAD_bd.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19384:SF17. NADPH_Cyt_Red. 1 hit.

Pfam

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

PRINTS

PR00369. FLAVODOXIN.
PR00371. FPNCR.

PROSITE

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

ProtoNet

Search...

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:	June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)