[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2544578 [NCBI, ExPASy, EBI, Israel, Japan] Ruettinger R.T., Wen L.-P., Fulco A.J.; "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."; J. Biol. Chem. 264:10987-10995(1989).
[2]	CHARACTERIZATION. DOI=10.1016/0003-9861(92)90045-X; PubMed=1727637 [NCBI, ExPASy, EBI, Israel, Japan] Boddupalli S.S., Pramanik B.C., Slaughter C.A., Estabrook R.W., Peterson J.A.; "Fatty acid monooxygenation by P450BM-3: product identification and proposed mechanisms for the sequential hydroxylation reactions."; Arch. Biochem. Biophys. 292:20-28(1992).
[3]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-472. PubMed=8342039 [NCBI, ExPASy, EBI, Israel, Japan] Ravichandran K.G., Boddupalli S.S., Hasemann C.A., Peterson J.A., Deisenhofer J.; "Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's."; Science 261:731-736(1993).
[4]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-472. DOI=10.1038/nsb0297-140; PubMed=9033595 [NCBI, ExPASy, EBI, Israel, Japan] Li H.Y., Poulos T.L.; "The structure of the cytochrome p450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid."; Nat. Struct. Biol. 4:140-146(1997).
[5]	X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 1-650. DOI=10.1073/pnas.96.5.1863; PubMed=10051560 [NCBI, ExPASy, EBI, Israel, Japan] Sevrioukova I.F., Li H., Zhang H., Peterson J.A., Poulos T.L.; "Structure of a cytochrome P450-redox partner electron-transfer complex."; Proc. Natl. Acad. Sci. U.S.A. 96:1863-1868(1999).
[6]	X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471. DOI=10.1021/bi011197q; PubMed=11695892 [NCBI, ExPASy, EBI, Israel, Japan] Haines D.C., Tomchick D.R., Machius M., Peterson J.A.; "Pivotal role of water in the mechanism of P450BM-3."; Biochemistry 40:13456-13465(2001).

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.
CATALYTIC ACTIVITY: RH + reduced flavoprotein + O₂ = ROH + oxidized flavoprotein + H₂O.
COFACTOR: FAD.
COFACTOR: FMN.
COFACTOR: Heme group.
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: In the N-terminal section; belongs to the cytochrome P450 family.
SIMILARITY: Contains 1 FAD-binding FR-type domain.
SIMILARITY: Contains 1 flavodoxin-like domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J04832; AAA87602.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A34286; A34286.

3D structure databases

PDB

1BU7; X-ray; 1.65 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1BVY; X-ray; 2.03 A; A/B=1-459, F=460-650.	[ExPASy / RCSB / EBI]
1FAG; X-ray; 2.70 A; A/B/C/D=1-472.	[ExPASy / RCSB / EBI]
1FAH; X-ray; 2.30 A; A/B=1-472.	[ExPASy / RCSB / EBI]
1JME; X-ray; 2.00 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1JPZ; X-ray; 1.65 A; A/B=1-471.	[ExPASy / RCSB / EBI]
1P0V; X-ray; 2.05 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1P0W; X-ray; 2.00 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1P0X; X-ray; 2.00 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1SMI; X-ray; 2.00 A; A/B=1-472.	[ExPASy / RCSB / EBI]
1SMJ; X-ray; 2.75 A; A/B/C/D=1-472.	[ExPASy / RCSB / EBI]
1YQO; X-ray; 1.90 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1YQP; X-ray; 1.80 A; A/B=1-456.	[ExPASy / RCSB / EBI]
1ZO4; X-ray; 1.46 A; A/B=1-471.	[ExPASy / RCSB / EBI]
1ZO9; X-ray; 1.70 A; A/B=1-471.	[ExPASy / RCSB / EBI]
1ZOA; X-ray; 1.74 A; A/B=1-471.	[ExPASy / RCSB / EBI]
2BMH; X-ray; 2.00 A; A/B=1-456.	[ExPASy / RCSB / EBI]
2HPD; X-ray; 2.00 A; A/B=1-472.	[ExPASy / RCSB / EBI]
2IJ2; X-ray; 1.20 A; A/B=1-471.	[ExPASy / RCSB / EBI]
2IJ3; X-ray; 1.90 A; A/B=1-471.	[ExPASy / RCSB / EBI]
2IJ4; X-ray; 2.40 A; A/B=1-471.	[ExPASy / RCSB / EBI]
2J1M; X-ray; 1.70 A; A/B=2-456.	[ExPASy / RCSB / EBI]
2J4S; X-ray; 2.10 A; A/B=2-456.	[ExPASy / RCSB / EBI]
2NNB; X-ray; 1.90 A; A/B=2-472.	[ExPASy / RCSB / EBI]
2UWH; X-ray; 2.80 A; A/B/C/D/E/F=2-459.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

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; -.

ModBase

P14779.

Family and domain databases

InterPro

IPR001128; Cyt_P450.
IPR002401; Cyt_P450_E_grp-I.
IPR003097; FAD-binding_1.
IPR001094; Flavdoxin_like.
IPR008254; Flavodoxin/NO_synth.
IPR001709; FPN_cyt_redctse.
IPR015702; NADPH_Cyt_Red.
IPR001433; OxRdtase_FAD/NAD_bd.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.630.10; Cyt_P450; 1.

PANTHER

PTHR19384:SF17; NADPH_Cyt_Red; 1.

Pfam

PF00667; FAD_binding_1; 1.
PF00258; Flavodoxin_1; 1.
PF00175; NAD_binding_1; 1.
PF00067; p450; 1.
Pfam graphical view of domain structure.

PRINTS

PR00463; EP450I.
PR00369; FLAVODOXIN.
PR00371; FPNCR.
PR00385; P450.

PROSITE

PS00086; CYTOCHROME_P450; 1.
PS51384; FAD_FR; 1.
PS50902; FLAVODOXIN_LIKE; 1.
PROSITE graphical view of domain structure (profiles).

Other

P14779; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cytoplasm; Electron transport; FAD; Flavoprotein; FMN; Heme; Iron; Metal-binding; Monooxygenase; Multifunctional enzyme; NADP; Oxidoreductase; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 1049`	`1048`	`Bifunctional P-450/NADPH-P450 reductase.`	`PRO_0000052205`
`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.`
`METAL`	`401 401`		`Iron (heme axial ligand).`
`HELIX`	`13 15`	`3`
`HELIX`	`18 21`	`4`
`HELIX`	`26 37`	`12`
`STRAND`	`39 45`	`7`
`STRAND`	`48 53`	`6`
`HELIX`	`56 62`	`7`
`TURN`	`65 67`	`3`
`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`
`STRAND`	`301 303`	`3`
`HELIX`	`306 311`	`6`
`HELIX`	`313 325`	`13`
`STRAND`	`331 338`	`8`
`STRAND`	`340 342`	`3`
`TURN`	`343 345`	`3`
`STRAND`	`346 348`	`3`
`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`
`STRAND`	`422 425`	`4`
`STRAND`	`434 442`	`9`
`STRAND`	`446 451`	`6`
`STRAND`	`483 488`	`6`
`STRAND`	`490 492`	`3`
`HELIX`	`493 506`	`14`
`TURN`	`507 509`	`3`
`STRAND`	`513 516`	`4`
`HELIX`	`517 519`	`3`
`STRAND`	`526 534`	`9`
`TURN`	`543 545`	`3`
`HELIX`	`546 553`	`8`
`STRAND`	`565 571`	`7`
`HELIX`	`576 578`	`3`
`HELIX`	`581 591`	`11`
`TURN`	`592 594`	`3`
`STRAND`	`599 605`	`7`
`HELIX`	`610 628`	`19`

Sequence information

Length: 1049 AA [This is the length of the unprocessed precursor]

Molecular weight: 117781 Da [This is the MW of the unprocessed precursor]

CRC64: B0BE61F8A2EE33D5 [This is a checksum on the sequence]

        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

P14779 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools