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P14779 (CPXB_BACME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional P-450/NADPH-P450 reductase
Alternative name(s):
Cytochrome P450(BM-3)
Short name=Cytochrome P450BM-3

Including the following 2 domains:

  1. Cytochrome P450 102
    EC=1.14.14.1
  2. NADPH--cytochrome P450 reductase
    EC=1.6.2.4
Gene names
Name:cyp102A1
Synonyms:cyp102
OrganismBacillus megaterium
Taxonomic identifier1404 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length1049 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-7701704,EBI-7701704

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 10491048Bifunctional P-450/NADPH-P450 reductase
PRO_0000052205

Regions

Domain483 – 622140Flavodoxin-like
Domain660 – 892233FAD-binding FR-type
Region2 – 472471Cytochrome P450
Region473 – 1049577NADPH-P-450 reductase

Sites

Metal binding4011Iron (heme axial ligand)

Secondary structure

........................................................................................................................................................................ 1049
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14779 [UniParc].

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

FASTA1,049117,781
        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.
PIRA34286.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BU7X-ray1.65A/B2-456[»]
1BVYX-ray2.03A/B2-459[»]
F460-650[»]
1FAGX-ray2.70A/B/C/D2-472[»]
1FAHX-ray2.30A/B2-471[»]
1JMEX-ray2.00A/B2-455[»]
1JPZX-ray1.65A/B1-471[»]
1P0VX-ray2.05A/B2-455[»]
1P0WX-ray2.00A/B2-455[»]
1P0XX-ray2.00A/B2-455[»]
1SMIX-ray2.00A/B2-471[»]
1SMJX-ray2.75A/B/C/D2-471[»]
1YQOX-ray1.90A/B2-455[»]
1YQPX-ray1.80A/B2-455[»]
1ZO4X-ray1.46A/B2-470[»]
1ZO9X-ray1.70A/B2-470[»]
1ZOAX-ray1.74A/B2-470[»]
2BMHX-ray2.00A/B2-455[»]
2HPDX-ray2.00A/B2-472[»]
2IJ2X-ray1.20A/B2-470[»]
2IJ3X-ray1.90A/B2-470[»]
2IJ4X-ray2.40A/B2-470[»]
2J1MX-ray1.70A/B2-455[»]
2J4SX-ray2.10A/B2-455[»]
2NNBX-ray1.90A/B2-471[»]
2UWHX-ray2.80A/B/C/D/E/F2-458[»]
2X7YX-ray2.10A/B2-456[»]
2X80X-ray2.30A/B2-456[»]
3BENX-ray1.65A/B1-470[»]
3CBDX-ray2.65A/B2-456[»]
3DGIX-ray1.95A/B2-456[»]
3EKBX-ray2.30A/B2-471[»]
3EKDX-ray2.50A/B2-471[»]
3EKFX-ray2.10A/B2-471[»]
3HF2X-ray2.20A/B1-482[»]
3KX3X-ray1.80A/B2-471[»]
3KX4X-ray1.95A/B2-471[»]
3KX5X-ray1.69A/B2-471[»]
3M4VX-ray1.90A/B1-482[»]
3NPLX-ray2.40A/B1-464[»]
3PSXX-ray1.90A/B1-482[»]
4DQKX-ray2.40A/B659-1049[»]
4DQLX-ray2.15A/B657-1049[»]
4DTWX-ray1.80A/B2-464[»]
4DTYX-ray1.45A/B2-464[»]
4DTZX-ray1.55A/B2-464[»]
4DU2X-ray1.90A/B1-464[»]
4DUAX-ray2.00A/B2-464[»]
4DUBX-ray1.70A/B1-464[»]
4DUCX-ray1.92A/B1-464[»]
4DUDX-ray1.85A/B2-464[»]
4DUEX-ray1.70A/B2-464[»]
4DUFX-ray1.80A/B/C/D2-464[»]
4H23X-ray3.30A/B1-464[»]
4H24X-ray2.50A/B/C/D1-464[»]
4HGFX-ray1.70A/B2-456[»]
4HGGX-ray1.70A/B2-456[»]
4HGHX-ray1.40A/B2-456[»]
4HGIX-ray1.50A/B2-456[»]
4HGJX-ray1.90A/B2-456[»]
4KEWX-ray1.89A/B2-456[»]
4KEYX-ray2.05A/B2-456[»]
4KF0X-ray1.45A/B2-458[»]
4KF2X-ray1.82A/B2-458[»]
4KPAX-ray2.00A1-471[»]
4KPBX-ray2.10A/B1-471[»]
4O4PX-ray1.83A/B2-456[»]
ProteinModelPortalP14779.
SMRP14779. Positions 2-459, 480-631.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-8313368.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17698.

Family and domain databases

Gene3D1.10.630.10. 1 hit.
1.20.990.10. 1 hit.
InterProIPR023206. 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]
PfamPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view]
PIRSFPIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTSPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMSSF48264. SSF48264. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP14779.

Entry information

Entry nameCPXB_BACME
AccessionPrimary (citable) accession number: P14779
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references