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UniProtKB - O08336 (CYPB_BACSU)
Protein
Bifunctional cytochrome P450/NADPH--P450 reductase 2
Gene
cypB
Organism
Bacillus subtilis (strain 168)
Status
Functioni
Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of medium to long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 and omega-3 positions, in approximately equal proportions. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain.
2 PublicationsCatalytic activityi
- an organic molecule + O2 + reduced [NADPH—hemoprotein reductase] = an alcohol + H+ + H2O + oxidized [NADPH—hemoprotein reductase]2 PublicationsEC:1.14.14.12 Publications
- EC:1.6.2.42 Publications
Cofactori
Protein has several cofactor binding sites:Kineticsi
kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytanic acid hydroxylation. kcat is 3845 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 1690 min(-1) for arachidonic acid hydroxylation. kcat is 3520 min(-1) for the reduction of cytochrome c. kcat is 37050 min(-1) for the reduction of ferricyanide.1 Publication
- KM=165 µM for lauric acid1 Publication
- KM=542 µM for myristic acid1 Publication
- KM=337 µM for palmitic acid1 Publication
- KM=68.5 µM for stearic acid1 Publication
- KM=28.7 µM for phytanic acid1 Publication
- KM=68.3 µM for 15-methylpalmitic acid1 Publication
- KM=79 µM for arachidonic acid1 Publication
- KM=5.1 µM for NADPH1 Publication
- KM=2.43 mM for NADH1 Publication
- KM=10.9 µM for cytochrome c (in the reductase assay)1 Publication
- KM=285 µM for ferricyanide (in the reductase assay)1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 271 | Important for catalytic activityBy similarity | 1 | |
Metal bindingi | 403 | Iron (heme axial ligand)By similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 492 – 497 | FMNBy similarity | 6 | |
Nucleotide bindingi | 539 – 542 | FMNBy similarity | 4 | |
Nucleotide bindingi | 573 – 575 | FMNBy similarity | 3 | |
Nucleotide bindingi | 581 – 583 | FMNBy similarity | 3 |
GO - Molecular functioni
- aromatase activity Source: UniProtKB-EC
- fatty acid binding Source: UniProtKB
- flavin adenine dinucleotide binding Source: UniProtKB
- FMN binding Source: UniProtKB
- heme binding Source: UniProtKB
- iron ion binding Source: UniProtKB
- NADPH-hemoprotein reductase activity Source: UniProtKB
- oxidoreductase activity Source: GO_Central
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen Source: UniProtKB
GO - Biological processi
- fatty acid oxidation Source: UniProtKB
Keywordsi
Molecular function | Monooxygenase, Multifunctional enzyme, Oxidoreductase |
Biological process | Electron transport, Transport |
Ligand | FAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP |
Enzyme and pathway databases
BioCyci | BSUB:BSU27160-MONOMER |
SABIO-RKi | O08336 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional cytochrome P450/NADPH--P450 reductase 2CuratedAlternative name(s): CYP102A31 Publication Fatty acid hydroxylase CypBCurated Flavocytochrome P450 102A3Curated Including the following 2 domains: |
Gene namesi | Name:cypBImported Synonyms:cyp102A32 Publications, yrhJ2 Publications Ordered Locus Names:BSU27160 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Cytosol
- cytosol Source: GO_Central
Keywords - Cellular componenti
CytoplasmPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 89 | F → V: Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with Q-190. 1 Publication | 1 | |
Mutagenesisi | 190 | S → Q: Hydroxylates shorter substrates with higher conversion rates than wild-type, and in contrast to wild-type, is also able to convert medium-chain alkanes and aromatic compounds; when associated with V-89. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052207 | 1 – 1054 | Bifunctional cytochrome P450/NADPH--P450 reductase 2Add BLAST | 1054 |
Proteomic databases
PaxDbi | O08336 |
Expressioni
Inductioni
Negatively regulated by the transcriptional repressor FatR (PubMed:11574077, PubMed:11734890). Is induced by fatty acids such as oleate, linoleate and phytanate, that bind and displace the FatR repressor (PubMed:11734890). Is also induced by palmitate, likely via another mechanism (PubMed:11574077). Transcribed under partial control of SigM ECF sigma factor (PubMed:17434969).3 Publications
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 486 – 625 | Flavodoxin-likePROSITE-ProRule annotationAdd BLAST | 140 | |
Domaini | 663 – 896 | FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST | 234 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 475 | Cytochrome P4501 PublicationAdd BLAST | 475 | |
Regioni | 462 – 482 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 476 – 1053 | NADPH--P450 reductase1 PublicationAdd BLAST | 578 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 462 – 481 | Basic and acidic residuesSequence analysisAdd BLAST | 20 |
Sequence similaritiesi
In the N-terminal section; belongs to the cytochrome P450 family.Curated
Phylogenomic databases
eggNOGi | COG0369, Bacteria COG2124, Bacteria |
InParanoidi | O08336 |
OMAi | EDYPACE |
PhylomeDBi | O08336 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit 1.20.990.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR023206, Bifunctional_P450_P450_red IPR003097, CysJ-like_FAD-binding IPR001128, Cyt_P450 IPR017972, Cyt_P450_CS IPR036396, Cyt_P450_sf IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR001433, OxRdtase_FAD/NAD-bd IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF00667, FAD_binding_1, 1 hit PF00258, Flavodoxin_1, 1 hit PF00175, NAD_binding_1, 1 hit PF00067, p450, 1 hit |
PIRSFi | PIRSF000209, Bifunctional_P450_P450R, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SUPFAMi | SSF48264, SSF48264, 1 hit SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
O08336-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKQASAIPQP KTYGPLKNLP HLEKEQLSQS LWRIADELGP IFRFDFPGVS
60 70 80 90 100
SVFVSGHNLV AEVCDEKRFD KNLGKGLQKV REFGGDGLFT SWTHEPNWQK
110 120 130 140 150
AHRILLPSFS QKAMKGYHSM MLDIATQLIQ KWSRLNPNEE IDVADDMTRL
160 170 180 190 200
TLDTIGLCGF NYRFNSFYRD SQHPFITSML RALKEAMNQS KRLGLQDKMM
210 220 230 240 250
VKTKLQFQKD IEVMNSLVDR MIAERKANPD ENIKDLLSLM LYAKDPVTGE
260 270 280 290 300
TLDDENIRYQ IITFLIAGHE TTSGLLSFAI YCLLTHPEKL KKAQEEADRV
310 320 330 340 350
LTDDTPEYKQ IQQLKYIRMV LNETLRLYPT APAFSLYAKE DTVLGGEYPI
360 370 380 390 400
SKGQPVTVLI PKLHRDQNAW GPDAEDFRPE RFEDPSSIPH HAYKPFGNGQ
410 420 430 440 450
RACIGMQFAL QEATMVLGLV LKHFELINHT GYELKIKEAL TIKPDDFKIT
460 470 480 490 500
VKPRKTAAIN VQRKEQADIK AETKPKETKP KHGTPLLVLF GSNLGTAEGI
510 520 530 540 550
AGELAAQGRQ MGFTAETAPL DDYIGKLPEE GAVVIVTASY NGAPPDNAAG
560 570 580 590 600
FVEWLKELEE GQLKGVSYAV FGCGNRSWAS TYQRIPRLID DMMKAKGASR
610 620 630 640 650
LTAIGEGDAA DDFESHRESW ENRFWKETMD AFDINEIAQK EDRPSLSITF
660 670 680 690 700
LSEATETPVA KAYGAFEGIV LENRELQTAA STRSTRHIEL EIPAGKTYKE
710 720 730 740 750
GDHIGILPKN SRELVQRVLS RFGLQSNHVI KVSGSAHMAH LPMDRPIKVV
760 770 780 790 800
DLLSSYVELQ EPASRLQLRE LASYTVCPPH QKELEQLVSD DGIYKEQVLA
810 820 830 840 850
KRLTMLDFLE DYPACEMPFE RFLALLPSLK PRYYSISSSP KVHANIVSMT
860 870 880 890 900
VGVVKASAWS GRGEYRGVAS NYLAELNTGD AAACFIRTPQ SGFQMPNDPE
910 920 930 940 950
TPMIMVGPGT GIAPFRGFIQ ARSVLKKEGS TLGEALLYFG CRRPDHDDLY
960 970 980 990 1000
REELDQAEQD GLVTIRRCYS RVENEPKGYV QHLLKQDTQK LMTLIEKGAH
1010 1020 1030 1040 1050
IYVCGDGSQM APDVERTLRL AYEAEKAASQ EESAVWLQKL QDQRRYVKDV
WTGM
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U93874 Genomic DNA Translation: AAB80867.1 AL009126 Genomic DNA Translation: CAB14658.1 |
PIRi | A69975 |
RefSeqi | NP_390594.1, NC_000964.3 WP_003246174.1, NZ_JNCM01000036.1 |
Genome annotation databases
EnsemblBacteriai | CAB14658; CAB14658; BSU_27160 |
GeneIDi | 937585 |
KEGGi | bsu:BSU27160 |
PATRICi | fig|224308.179.peg.2949 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U93874 Genomic DNA Translation: AAB80867.1 AL009126 Genomic DNA Translation: CAB14658.1 |
PIRi | A69975 |
RefSeqi | NP_390594.1, NC_000964.3 WP_003246174.1, NZ_JNCM01000036.1 |
3D structure databases
SMRi | O08336 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU27160 |
Proteomic databases
PaxDbi | O08336 |
Protocols and materials databases
DNASUi | 937585 |
Genome annotation databases
EnsemblBacteriai | CAB14658; CAB14658; BSU_27160 |
GeneIDi | 937585 |
KEGGi | bsu:BSU27160 |
PATRICi | fig|224308.179.peg.2949 |
Phylogenomic databases
eggNOGi | COG0369, Bacteria COG2124, Bacteria |
InParanoidi | O08336 |
OMAi | EDYPACE |
PhylomeDBi | O08336 |
Enzyme and pathway databases
BioCyci | BSUB:BSU27160-MONOMER |
SABIO-RKi | O08336 |
Family and domain databases
Gene3Di | 1.10.630.10, 1 hit 1.20.990.10, 1 hit 3.40.50.360, 1 hit 3.40.50.80, 1 hit |
InterProi | View protein in InterPro IPR023206, Bifunctional_P450_P450_red IPR003097, CysJ-like_FAD-binding IPR001128, Cyt_P450 IPR017972, Cyt_P450_CS IPR036396, Cyt_P450_sf IPR017927, FAD-bd_FR_type IPR001094, Flavdoxin-like IPR008254, Flavodoxin/NO_synth IPR001709, Flavoprot_Pyr_Nucl_cyt_Rdtase IPR029039, Flavoprotein-like_sf IPR039261, FNR_nucleotide-bd IPR023173, NADPH_Cyt_P450_Rdtase_alpha IPR001433, OxRdtase_FAD/NAD-bd IPR017938, Riboflavin_synthase-like_b-brl |
Pfami | View protein in Pfam PF00667, FAD_binding_1, 1 hit PF00258, Flavodoxin_1, 1 hit PF00175, NAD_binding_1, 1 hit PF00067, p450, 1 hit |
PIRSFi | PIRSF000209, Bifunctional_P450_P450R, 1 hit |
PRINTSi | PR00369, FLAVODOXIN PR00371, FPNCR |
SUPFAMi | SSF48264, SSF48264, 1 hit SSF52218, SSF52218, 1 hit SSF52343, SSF52343, 1 hit SSF63380, SSF63380, 1 hit |
PROSITEi | View protein in PROSITE PS00086, CYTOCHROME_P450, 1 hit PS51384, FAD_FR, 1 hit PS50902, FLAVODOXIN_LIKE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CYPB_BACSU | |
Accessioni | O08336Primary (citable) accession number: O08336 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | July 1, 1997 | |
Last modified: | February 23, 2022 | |
This is version 160 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families