UniProtKB - O08394 (CYPD_BACSU)
Bifunctional cytochrome P450/NADPH--P450 reductase 1
cypD
Functioni
Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of 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 position. 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 (PubMed:15375636, PubMed:15122913).
Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS) (PubMed:21048857).
3 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
- KM=38.8 µM for stearic acid1 Publication
- KM=150 µM for phytanic acid1 Publication
- KM=56.8 µM for 15-methylpalmitic acid1 Publication
- KM=3.6 µM for NADPH1 Publication
- KM=17.9 mM for NADH1 Publication
- KM=6.9 µM for cytochrome c (in the reductase assay)1 Publication
- KM=153.4 µM for ferricyanide (in the reductase assay)1 Publication
- KM=17.36 µM for oleic acid1 Publication
pH dependencei
Temperature dependencei
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 | 499 – 504 | FMNBy similarity | 6 | |
Nucleotide bindingi | 546 – 549 | FMNBy similarity | 4 | |
Nucleotide bindingi | 580 – 582 | FMNBy similarity | 3 | |
Nucleotide bindingi | 588 – 590 | 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:BSU07250-MONOMER |
SABIO-RKi | O08394 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional cytochrome P450/NADPH--P450 reductase 1CuratedAlternative name(s): CYP102A21 Publication Fatty acid hydroxylase CypDCurated Flavocytochrome P450 102A2Curated Including the following 2 domains: |
Gene namesi | Name:cypDImported Synonyms:cyp102A22 Publications, yetO1 Publication, yfnJ Ordered Locus Names:BSU07250 |
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 | 15 | P → S: Exhibits modified substrate specificity. Shows approximately 6- to 9-fold increased activity with SDS, lauric acid and 1,4-naphthoquinone, and enhanced activity for other substrates such as ethacrynic acid and epsilon-amino-n-caproic acid. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000052206 | 1 – 1061 | Bifunctional cytochrome P450/NADPH--P450 reductase 1Add BLAST | 1061 |
Proteomic databases
PaxDbi | O08394 |
PRIDEi | O08394 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 493 – 632 | Flavodoxin-likePROSITE-ProRule annotationAdd BLAST | 140 | |
Domaini | 671 – 904 | 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 | 476 – 1061 | NADPH--P450 reductase1 PublicationAdd BLAST | 586 |
Sequence similaritiesi
Phylogenomic databases
eggNOGi | COG0369, Bacteria COG2124, Bacteria |
InParanoidi | O08394 |
OMAi | WKKAHNI |
PhylomeDBi | O08394 |
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.
10 20 30 40 50
MKETSPIPQP KTFGPLGNLP LIDKDKPTLS LIKLAEEQGP IFQIHTPAGT
60 70 80 90 100
TIVVSGHELV KEVCDEERFD KSIEGALEKV RAFSGDGLFT SWTHEPNWRK
110 120 130 140 150
AHNILMPTFS QRAMKDYHEK MVDIAVQLIQ KWARLNPNEA VDVPGDMTRL
160 170 180 190 200
TLDTIGLCGF NYRFNSYYRE TPHPFINSMV RALDEAMHQM QRLDVQDKLM
210 220 230 240 250
VRTKRQFRYD IQTMFSLVDS IIAERRANGD QDEKDLLARM LNVEDPETGE
260 270 280 290 300
KLDDENIRFQ IITFLIAGHE TTSGLLSFAT YFLLKHPDKL KKAYEEVDRV
310 320 330 340 350
LTDAAPTYKQ VLELTYIRMI LNESLRLWPT APAFSLYPKE DTVIGGKFPI
360 370 380 390 400
TTNDRISVLI PQLHRDRDAW GKDAEEFRPE RFEHQDQVPH HAYKPFGNGQ
410 420 430 440 450
RACIGMQFAL HEATLVLGMI LKYFTLIDHE NYELDIKQTL TLKPGDFHIS
460 470 480 490 500
VQSRHQEAIH ADVQAAEKAA PDEQKEKTEA KGASVIGLNN RPLLVLYGSD
510 520 530 540 550
TGTAEGVARE LADTASLHGV RTKTAPLNDR IGKLPKEGAV VIVTSSYNGK
560 570 580 590 600
PPSNAGQFVQ WLQEIKPGEL EGVHYAVFGC GDHNWASTYQ YVPRFIDEQL
610 620 630 640 650
AEKGATRFSA RGEGDVSGDF EGQLDEWKKS MWADAIKAFG LELNENADKE
660 670 680 690 700
RSTLSLQFVR GLGESPLARS YEASHASIAE NRELQSADSD RSTRHIEIAL
710 720 730 740 750
PPDVEYQEGD HLGVLPKNSQ TNVSRILHRF GLKGTDQVTL SASGRSAGHL
760 770 780 790 800
PLGRPVSLHD LLSYSVEVQE AATRAQIREL ASFTVCPPHR RELEELSAEG
810 820 830 840 850
VYQEQILKKR ISMLDLLEKY EACDMPFERF LELLRPLKPR YYSISSSPRV
860 870 880 890 900
NPRQASITVG VVRGPAWSGR GEYRGVASND LAERQAGDDV VMFIRTPESR
910 920 930 940 950
FQLPKDPETP IIMVGPGTGV APFRGFLQAR DVLKREGKTL GEAHLYFGCR
960 970 980 990 1000
NDRDFIYRDE LERFEKDGIV TVHTAFSRKE GMPKTYVQHL MADQADTLIS
1010 1020 1030 1040 1050
ILDRGGRLYV CGDGSKMAPD VEAALQKAYQ AVHGTGEQEA QNWLRHLQDT
1060
GMYAKDVWAG I
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D87979 Genomic DNA Translation: BAA20123.1 AL009126 Genomic DNA Translation: CAB12544.1 |
PIRi | D69799 |
RefSeqi | NP_388606.1, NC_000964.3 WP_003242884.1, NZ_JNCM01000032.1 |
Genome annotation databases
EnsemblBacteriai | CAB12544; CAB12544; BSU_07250 |
GeneIDi | 938784 |
KEGGi | bsu:BSU07250 |
PATRICi | fig|224308.179.peg.786 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | D87979 Genomic DNA Translation: BAA20123.1 AL009126 Genomic DNA Translation: CAB12544.1 |
PIRi | D69799 |
RefSeqi | NP_388606.1, NC_000964.3 WP_003242884.1, NZ_JNCM01000032.1 |
3D structure databases
SMRi | O08394 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU07250 |
Proteomic databases
PaxDbi | O08394 |
PRIDEi | O08394 |
Genome annotation databases
EnsemblBacteriai | CAB12544; CAB12544; BSU_07250 |
GeneIDi | 938784 |
KEGGi | bsu:BSU07250 |
PATRICi | fig|224308.179.peg.786 |
Phylogenomic databases
eggNOGi | COG0369, Bacteria COG2124, Bacteria |
InParanoidi | O08394 |
OMAi | WKKAHNI |
PhylomeDBi | O08394 |
Enzyme and pathway databases
BioCyci | BSUB:BSU07250-MONOMER |
SABIO-RKi | O08394 |
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 | CYPD_BACSU | |
Accessioni | O08394Primary (citable) accession number: O08394 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | July 1, 1997 | |
Last modified: | February 23, 2022 | |
This is version 156 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