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P14779

- CPXB_BACME

UniProt

P14779 - CPXB_BACME

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Protein

Bifunctional P-450/NADPH-P450 reductase

Gene
cyp102A1, cyp102
Organism
Bacillus megaterium
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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 activityi

NADPH + n oxidized hemoprotein = NADP+ + n reduced hemoprotein.
RH + reduced flavoprotein + O2 = ROH + oxidized flavoprotein + H2O.

Cofactori

FAD.
FMN.
Heme group.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi401 – 4011Iron (heme axial ligand)

GO - Molecular functioni

  1. aromatase activity Source: UniProtKB-EC
  2. FMN binding Source: InterPro
  3. heme binding Source: InterPro
  4. identical protein binding Source: IntAct
  5. iron ion binding Source: InterPro
  6. NADPH-hemoprotein reductase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17698.

Names & Taxonomyi

Protein namesi
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 namesi
Name:cyp102A1
Synonyms:cyp102
OrganismiBacillus megaterium
Taxonomic identifieri1404 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 10491048Bifunctional P-450/NADPH-P450 reductasePRO_0000052205Add
BLAST

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-7701704,EBI-7701704

Protein-protein interaction databases

MINTiMINT-8313368.

Structurei

Secondary structure

1
1049
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 153
Helixi18 – 214
Helixi26 – 3712
Beta strandi39 – 457
Beta strandi48 – 536
Helixi56 – 627
Turni65 – 673
Beta strandi68 – 703
Helixi74 – 8310
Helixi87 – 893
Beta strandi92 – 943
Helixi95 – 10410
Helixi105 – 1084
Turni110 – 1123
Helixi113 – 13220
Helixi142 – 15918
Helixi165 – 1673
Helixi173 – 18715
Helixi188 – 1903
Helixi197 – 1993
Helixi200 – 22728
Helixi234 – 2407
Turni244 – 2463
Helixi252 – 28332
Helixi285 – 29814
Beta strandi301 – 3033
Helixi306 – 3105
Helixi313 – 32513
Beta strandi331 – 3388
Beta strandi340 – 3423
Turni343 – 3453
Beta strandi346 – 3483
Beta strandi353 – 3575
Helixi358 – 3614
Helixi365 – 3684
Turni370 – 3734
Helixi377 – 3804
Helixi383 – 3853
Helixi397 – 3993
Helixi404 – 42118
Beta strandi422 – 4254
Beta strandi434 – 4429
Beta strandi446 – 4516
Beta strandi483 – 4886
Beta strandi490 – 4923
Helixi493 – 50614
Turni507 – 5093
Beta strandi513 – 5164
Helixi517 – 5193
Beta strandi526 – 5349
Turni543 – 5453
Helixi546 – 5538
Beta strandi565 – 5717
Helixi576 – 5783
Helixi581 – 59111
Turni592 – 5943
Beta strandi599 – 6057
Helixi610 – 62819
Beta strandi663 – 67210
Beta strandi682 – 6887
Beta strandi700 – 7034
Helixi709 – 71911
Beta strandi726 – 7294
Beta strandi741 – 7466
Helixi747 – 7504
Helixi751 – 7533
Beta strandi756 – 7594
Helixi762 – 7709
Helixi775 – 7839
Helixi787 – 7937
Turni794 – 7985
Helixi801 – 8077
Helixi815 – 8206
Beta strandi828 – 8314
Turni836 – 8383
Beta strandi842 – 8487
Beta strandi851 – 8533
Beta strandi857 – 8626
Helixi864 – 8718
Beta strandi877 – 8837
Beta strandi899 – 9024
Helixi905 – 9084
Helixi909 – 92315
Beta strandi931 – 9388
Turni940 – 9423
Helixi947 – 9559
Beta strandi960 – 9678
Helixi976 – 9827
Helixi984 – 9929
Beta strandi996 – 10027
Turni1003 – 10053
Helixi1006 – 102217
Helixi1026 – 103813
Beta strandi1042 – 10476

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/B2-472[»]
1JMEX-ray2.00A/B2-456[»]
1JPZX-ray1.65A/B2-471[»]
1P0VX-ray2.05A/B2-456[»]
1P0WX-ray2.00A/B2-456[»]
1P0XX-ray2.00A/B2-456[»]
1SMIX-ray2.00A/B2-472[»]
1SMJX-ray2.75A/B/C/D2-472[»]
1YQOX-ray1.90A/B2-456[»]
1YQPX-ray1.80A/B2-456[»]
1ZO4X-ray1.46A/B2-471[»]
1ZO9X-ray1.70A/B2-471[»]
1ZOAX-ray1.74A/B2-471[»]
2BMHX-ray2.00A/B2-456[»]
2HPDX-ray2.00A/B2-472[»]
2IJ2X-ray1.20A/B2-471[»]
2IJ3X-ray1.90A/B2-471[»]
2IJ4X-ray2.40A/B2-471[»]
2J1MX-ray1.70A/B2-456[»]
2J4SX-ray2.10A/B2-456[»]
2NNBX-ray1.90A/B2-472[»]
2UWHX-ray2.80A/B/C/D/E/F2-459[»]
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[»]
ProteinModelPortaliP14779.
SMRiP14779. Positions 2-459, 480-631.

Miscellaneous databases

EvolutionaryTraceiP14779.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini483 – 622140Flavodoxin-likeAdd
BLAST
Domaini660 – 892233FAD-binding FR-typeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 472471Cytochrome P450Add
BLAST
Regioni473 – 1049577NADPH-P-450 reductaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the cytochrome P450 family.

Family and domain databases

Gene3Di1.10.630.10. 1 hit.
1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProiIPR023206. 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.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PfamiPF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view]
PIRSFiPIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTSiPR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMiSSF48264. SSF48264. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEiPS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P14779-1 [UniParc]FASTAAdd to Basket

« Hide

MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT     50
RYLSSQRLIK EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA 100
HNILLPSFSQ QAMKGYHAMM VDIAVQLVQK WERLNADEHI EVPEDMTRLT 150
LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR ALDEAMNKLQ RANPDDPAYD 200
ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN GKDPETGEPL 250
DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV 300
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK 350
GDELMVLIPQ LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA 400
CIGQQFALHE ATLVLGMMLK HFDFEDHTNY ELDIKETLTL KPEGFVVKAK 450
SKKIPLGGIP SPSTEQSAKK VRKKAENAHN TPLLVLYGSN MGTAEGTARD 500
LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH PPDNAKQFVD 550
WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD 600
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS 650
AADMPLAKMH GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH 700
LGVIPRNYEG IVNRVTARFG LDASQQIRLE AEEEKLAHLP LAKTVSVEEL 750
LQYVELQDPV TRTQLRAMAA KTVCPPHKVE LEALLEKQAY KEQVLAKRLT 800
MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE KQASITVSVV 850
SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI 900
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL 950
ENAQSEGIIT LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC 1000
GDGSQMAPAV EATLMKSYAD VHQVSEADAR LWLQQLEEKG RYAKDVWAG 1049
Length:1,049
Mass (Da):117,781
Last modified:January 23, 2007 - v2
Checksum:iB0BE61F8A2EE33D5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04832 Genomic DNA. Translation: AAA87602.1.
PIRiA34286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J04832 Genomic DNA. Translation: AAA87602.1 .
PIRi A34286.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 2-472 [» ]
1JME X-ray 2.00 A/B 2-456 [» ]
1JPZ X-ray 1.65 A/B 2-471 [» ]
1P0V X-ray 2.05 A/B 2-456 [» ]
1P0W X-ray 2.00 A/B 2-456 [» ]
1P0X X-ray 2.00 A/B 2-456 [» ]
1SMI X-ray 2.00 A/B 2-472 [» ]
1SMJ X-ray 2.75 A/B/C/D 2-472 [» ]
1YQO X-ray 1.90 A/B 2-456 [» ]
1YQP X-ray 1.80 A/B 2-456 [» ]
1ZO4 X-ray 1.46 A/B 2-471 [» ]
1ZO9 X-ray 1.70 A/B 2-471 [» ]
1ZOA X-ray 1.74 A/B 2-471 [» ]
2BMH X-ray 2.00 A/B 2-456 [» ]
2HPD X-ray 2.00 A/B 2-472 [» ]
2IJ2 X-ray 1.20 A/B 2-471 [» ]
2IJ3 X-ray 1.90 A/B 2-471 [» ]
2IJ4 X-ray 2.40 A/B 2-471 [» ]
2J1M X-ray 1.70 A/B 2-456 [» ]
2J4S X-ray 2.10 A/B 2-456 [» ]
2NNB X-ray 1.90 A/B 2-472 [» ]
2UWH X-ray 2.80 A/B/C/D/E/F 2-459 [» ]
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 [» ]
4H23 X-ray 3.30 A/B 1-464 [» ]
4H24 X-ray 2.50 A/B/C/D 1-464 [» ]
4HGF X-ray 1.70 A/B 2-456 [» ]
4HGG X-ray 1.70 A/B 2-456 [» ]
4HGH X-ray 1.40 A/B 2-456 [» ]
4HGI X-ray 1.50 A/B 2-456 [» ]
4HGJ X-ray 1.90 A/B 2-456 [» ]
4KEW X-ray 1.89 A/B 2-456 [» ]
4KEY X-ray 2.05 A/B 2-456 [» ]
4KF0 X-ray 1.45 A/B 2-458 [» ]
4KF2 X-ray 1.82 A/B 2-458 [» ]
4KPA X-ray 2.00 A 1-471 [» ]
4KPB X-ray 2.10 A/B 1-471 [» ]
4O4P X-ray 1.83 A/B 2-456 [» ]
ProteinModelPortali P14779.
SMRi P14779. Positions 2-459, 480-631.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-8313368.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-17698.

Miscellaneous databases

EvolutionaryTracei P14779.

Family and domain databases

Gene3Di 1.10.630.10. 1 hit.
1.20.990.10. 1 hit.
3.40.50.360. 1 hit.
InterProi 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.
IPR029039. Flavoprotein-like.
IPR023173. NADPH_Cyt_P450_Rdtase_dom3.
IPR001433. OxRdtase_FAD/NAD-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
Pfami PF00667. FAD_binding_1. 1 hit.
PF00258. Flavodoxin_1. 1 hit.
PF00175. NAD_binding_1. 1 hit.
PF00067. p450. 1 hit.
[Graphical view ]
PIRSFi PIRSF000209. Bifunctional_P450_P450R. 1 hit.
PRINTSi PR00369. FLAVODOXIN.
PR00371. FPNCR.
SUPFAMi SSF48264. SSF48264. 1 hit.
SSF52218. SSF52218. 1 hit.
SSF63380. SSF63380. 1 hit.
PROSITEi PS00086. CYTOCHROME_P450. 1 hit.
PS51384. FAD_FR. 1 hit.
PS50902. FLAVODOXIN_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-471.

Entry informationi

Entry nameiCPXB_BACME
AccessioniPrimary (citable) accession number: P14779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi