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Entry version 174 (29 Sep 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Bifunctional cytochrome P450/NADPH--P450 reductase

Gene

cyp102A1

Organism
Bacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Functions as a fatty acid monooxygenase (PubMed:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028).

Catalyzes hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions (PubMed:1727637, PubMed:21875028).

Shows activity toward medium and long-chain fatty acids, with optimum chain lengths of 12, 14 and 16 carbons (lauric, myristic, and palmitic acids). Able to metabolize some of these primary metabolites to secondary and tertiary products (PubMed:1727637).

Marginal activity towards short chain lengths of 8-10 carbons (PubMed:1727637, PubMed:18619466).

Hydroxylates highly branched fatty acids, which play an essential role in membrane fluidity regulation (PubMed:16566047).

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:3106359, PubMed:1727637, PubMed:16566047, PubMed:7578081, PubMed:11695892, PubMed:14653735, PubMed:16403573, PubMed:18004886, PubMed:17077084, PubMed:17868686, PubMed:18298086, PubMed:18619466, PubMed:18721129, PubMed:19492389, PubMed:20180779, PubMed:21110374, PubMed:21875028).

Involved in inactivation of quorum sensing signals of other competing bacteria by oxidazing efficiently acyl homoserine lactones (AHLs), molecules involved in quorum sensing signaling pathways, and their lactonolysis products acyl homoserines (AHs) (PubMed:18020460).

18 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by N-(12-imidazolyl-dodecanoyl)-L-leucine.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 84.1 s(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine. kcat is 485 min(-1) for N-palmitoyl-L-glutamic acid. kcat is 1160 min(-1) for N-palmitoyl-L-leucine (PubMed:18004886). kcat is 28 s(-1) for lauric acid (PubMed:17868686). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:18721129). kcat is 77 for lauric acid (PubMed:19492389). kcat is 2770 min(-1) for laurate/dodecanoate (PubMed:20180779). kcat is 16400 min(-1) for arachidonate (PubMed:20180779). kcat is 91.4 for palmitic acid (PubMed:21110374).7 Publications
  1. KM=250 µM for lauric acid at pH 7.4 at room temperature1 Publication
  2. KM=34 µM for N-beta-oxolauroyl-DL-homoserine lactone1 Publication
  3. KM=210 µM for N-beta-oxolauroyl-DL-homoserine1 Publication
  4. KM=140 µM for N-lauroyl-DL-homoserine1 Publication
  5. KM=322 µM for lauric acid at pH 7.5 and 15 degrees Celsius1 Publication
  6. KM=265 µM for lauric acid1 Publication
  7. KM=16 mM for indole1 Publication
  8. KM=87.4 µM for laurate/dodecanoate at pH 7.0 and 25 degrees Celsius1 Publication
  9. KM=230 µM for lauric acid at pH 7.41 Publication
  10. KM=87.4 µM for laurate/dodecanoate at 25 degrees Celsius1 Publication
  11. KM=5.1 µM for arachidonate at 25 degrees Celsius1 Publication
  12. KM=42.4 µM for palmitic acid at pH 7.4 and 30 degrees Celsius1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei52PalmitoleateCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei269Important for catalytic activity2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi401Iron (heme axial ligand)Combined sources22 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi489 – 494FMNCombined sources1 Publication6
Nucleotide bindingi536 – 539FMNCombined sources1 Publication4
Nucleotide bindingi570 – 572FMNCombined sources1 Publication3
Nucleotide bindingi578 – 580FMNCombined sources1 Publication3

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionMonooxygenase, Multifunctional enzyme, Oxidoreductase
Biological processElectron transport, Transport
LigandFAD, Flavoprotein, FMN, Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17698

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.B57, 656
1.14.14.1, 656
1.6.2.4, 656

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional cytochrome P450/NADPH--P450 reductaseCurated
Alternative name(s):
Cytochrome P450(BM-3)1 Publication
Cytochrome P450BM-31 PublicationImported
Fatty acid monooxygenase1 Publication
Flavocytochrome P450 BM32 Publications
Including the following 2 domains:
Cytochrome P450 102A1 (EC:1.14.14.17 Publications)
NADPH--cytochrome P450 reductase (EC:1.6.2.47 Publications)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cyp102A1Imported
Synonyms:cyp102
ORF Names:BG04_163Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus megaterium (strain ATCC 14581 / DSM 32 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1348623 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaePriestia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000031829 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

This protein is a target of protein engineering. Its selectivity-directing and activity-enhancing mutations have been extensively studied and the designed mutations allow this enzyme to act on non-native substrates and/or in order to enhance production of synthetically desirable end-products.Curated3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi48R → Q or S: 2-3-fold decrease in binding affinity for N-myristoyl-L-methionine as substrate. 1 Publication1
Mutagenesisi75A → G: Higher activity in the hydroxylation of highly branched fatty acids; when associated with V-88 and Q-189. 1 Publication1
Mutagenesisi83A → F: 800-fold binding affinity for laurate as substrate. High coupling of NADPH consumption to laurate formation. Very much more effective in indole hydroxylation. Favors omega-2 hydroxylation. Significantly higher rates of NADPH consumption in the absence of substrate. No temperature-dependent shifts to low-spin in complex with palmitate. 1 Publication1
Mutagenesisi83A → I: No effect in binding affinity for laurate as substrate. High coupling of NADPH consumption to laurate formation. No indole hydroxylation. Favors omega-2 hydroxylation. Similarly to wild-type, shows significant shifts to low-spin in complex with palmitate as the temperature decreases. 1 Publication1
Mutagenesisi83A → W: 800-fold binding affinity for laurate as substrate. Low coupling of NADPH consumption to laurate formation. Very much more effective in indole hydroxylation. Favors omega-1 hydroxylation. Significantly higher rates of NADPH consumption in the absence of substrate. No temperature-dependent shifts to low-spin in complex with palmitate. 1 Publication1
Mutagenesisi87L → E: Ineffective covalent modification of the heme macrocycle. Extensive formation of Fe(II)CO complex in the substrate-free form. Has more positive potential in both substrate-free and arachidonate-bound forms and some high-spin content in the ferric substrate-free form of the enzyme. 1 Publication1
Mutagenesisi88F → V: Higher activity in the hydroxylation of highly branched fatty acids; when associated with G-75 and Q-189. 1 Publication1
Mutagenesisi189L → Q: Higher activity in the hydroxylation of highly branched fatty acids; when associated with G-75 and V-88. 1 Publication1
Mutagenesisi262F → E: Ineffective covalent modification of the heme macrocycle. Substantially slower FMN to heme electron transfer for the arachidonate-bound enzyme. Product distribution biased towards omega-3. 1 Publication1
Mutagenesisi265A → C: No effective fatty acid oxidation. No effect on electron transport from NADPH to FMN. Substantially lower high-spin conversion with arachidonate and palmitoleate, and negligible change is observed with palmitate, myristate and laurate/dodecanoate. 20% of omega-1, omega-2 and omega-3 laurate/dodecanoate hydroxylation products. 1 Publication1
Mutagenesisi265A → H or K: No significant stimulation of NADPH oxidation induced by addition of fatty acids and no hydroxylated products, but cytochrome c reductase activity levels are identical to wild-type enzyme. More negative reduction potential with dithionite. Unable to form Fe(2+)CO complexes on reduction with dithionite and bubbling with carbon monoxide. 1 Publication1
Mutagenesisi265A → M: No effective fatty acid oxidation. No effect on electron transport from NADPH to FMN. Slightly lower high-spin conversion with arachidonate, palmitoleate, palmitate, myristate and laurate/dodecanoate. 5% of omega-1, omega-2 and omega-3 laurate/dodecanoate hydroxylation products. 1 Publication1
Mutagenesisi265A → Q: No effective fatty acid oxidation. No effect on electron transport from NADPH to FMN. Nearly wild-type level of high-spin conversion with laurate/dodecanoate, palmitoleate and arachidonate. 5% of omega-1, omega-2 and omega-3 laurate/dodecanoate hydroxylation products. 1 Publication1
Mutagenesisi269T → A: Contrary to wild-type, significant decrease in the formation of the high-spin complex via substrate binding, and decreased substrate-induced reduction potential shift with saturating concentrations of arachidonate; when associated with H-394. Considerably lower proportion of high-spin protein and decreased substrate-induced heme reduction-potential shift on addition of saturating concentrations of arachidonate. Leads to destabilization of the oxy-ferrous complex. Exhibits slower rates of O(2) and NADPH consumption using sodium laurate as the substrate. Greater production of water and peroxide compared to wild-type indicating uncoupled electron transfer from sodium laurate hydroxylation. Only 16% yield of product after 5 min of reaction relative to the amount of NADPH used compared to 100% of wild-type. 2 Publications1
Mutagenesisi269T → N: High substrate-free turnover rate constant. Negligible substrate-induced spin-state and substrate-induced heme reduction-potential shifts on addition of saturating concentrations of arachidonate. Induces a positive shift in the substrate-free heme reduction potential. 10-fold greater rate constants for the first electron transfer in the absence of substrate; when associated with H-394. Turnover rate constants diminished. Significantly smaller degrees of coupling to product. Negligible amounts of high-spin protein on addition of saturating concentration of arachidonate. Negligible substrate-induced spin-state and substrate-induced heme reduction-potential shifts on addition of saturating concentrations of arachidonate. Induces a 60 mV positive shift in the substrate-free heme reduction potential. The apparent rate constant for heme reduction is smaller than the overall turnover rate constant. Leads to destabilization of the oxy-ferrous complex. 1 Publication1
Mutagenesisi329A → V: Substrate binding affinity increases 5-10 fold and the turnover number increases 2-8-fold for palmitate as substrate compared to the wild-type. Has a very different product distribution favoring greatly oxidation at the omega-1 position and shows almost no oxidation at the omega-3 position. 1 Publication1
Mutagenesisi331A → P: Enhanced activity with small non-natural substrates with altered product profiles compared to wild-type. 1 Publication1
Mutagenesisi394F → H: High substrate-free turnover rate constant. Negligible substrate-induced spin-state and substrate-induced heme reduction-potential shifts on addition of saturating concentrations of arachidonate. Induces a positive shift in the substrate-free heme reduction potential. 10-fold greater rate constants for the first electron transfer in the absence of substrate; when associated with N-269. Significant decrease in the formation of the high-spin complex via substrate binding, and decreased substrate-induced reduction potential shift with saturating concentrations of arachidonate; when associated with A-269. No change in product profile using myristate as substrate, but slightly higher amount of unreacted myristate indicating lower overall catalytic activity relative to wild-type. 2 Publications1
Mutagenesisi394F → W: Large decrease in the heme reduction potential in the presence and absence of substrate arachidonate. 10% reduction in efficiency to couple NADPH consumption to substrate monooxygenation. Half of the turn over rate and four times faster decay of the oxy-ferrous complex to the ferric form than that of wild-type. 1 Publication1
Mutagenesisi402I → E: Ineffective covalent modification of the heme macrocycle. 2-fold apparent limiting rate of flavin to heme electron transfer for arachidonate-bound enzyme. Substrate-free enzyme is converted rapidly and completely into its Fe(II)CO complex and has much more positive potential. 8-fold decrease in overall catalytic rate with arachidonic acid. More efficient NADPH oxidase in absence of fatty acids. Product distribution biased towards omega-1. 1 Publication1
Mutagenesisi402I → P: 10-fold increase in binding affinity for lauric acid. Catalytic activity rates accelerate across a range of hydrophobic non-natural substrates, including (+)-alpha-pinene, fluorene, 3-methylpentane and propylbenzene, while product distributions of them are broadly similar to the wild-type enzyme exept for (+)-alpha-pinene which is not metabolized by wild-type. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB08086, N-[12-(1H-imidazol-1-yl)dodecanoyl]-L-leucine
DB03440, N-hexadecanoylglycine
DB04257, Palmitoleic Acid

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000522051 – 1049Bifunctional cytochrome P450/NADPH--P450 reductaseAdd BLAST1049

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P14779

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By pentobarbital (PubMed:1544926, PubMed:3106359). Expression is negatively regulated by repressor bm3R1 at the transcriptional level (PubMed:1544926).2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

P14779
With#Exp.IntAct
itself2EBI-7701704,EBI-7701704

GO - Molecular functioni

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P14779

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11049
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P14779

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P14779

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini483 – 622Flavodoxin-likePROSITE-ProRule annotationAdd BLAST140
Domaini660 – 892FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST233

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 472Cytochrome P450Add BLAST471
Regioni473 – 1049NADPH--P450 reductaseAdd BLAST577

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_001570_7_0_9

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
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

Integrated resource of protein families, domains and functional sites

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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

Pfam protein domain database

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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

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF000209, Bifunctional_P450_P450R, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00369, FLAVODOXIN
PR00371, FPNCR

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48264, SSF48264, 1 hit
SSF52218, SSF52218, 1 hit
SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00086, CYTOCHROME_P450, 1 hit
PS51384, FAD_FR, 1 hit
PS50902, FLAVODOXIN_LIKE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P14779-1 [UniParc]FASTAAdd to basket
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MTIKEMPQPK TFGELKNLPL LNTDKPVQAL MKIADELGEI FKFEAPGRVT
60 70 80 90 100
RYLSSQRLIK EACDESRFDK NLSQALKFVR DFAGDGLFTS WTHEKNWKKA
110 120 130 140 150
HNILLPSFSQ QAMKGYHAMM VDIAVQLVQK WERLNADEHI EVPEDMTRLT
160 170 180 190 200
LDTIGLCGFN YRFNSFYRDQ PHPFITSMVR ALDEAMNKLQ RANPDDPAYD
210 220 230 240 250
ENKRQFQEDI KVMNDLVDKI IADRKASGEQ SDDLLTHMLN GKDPETGEPL
260 270 280 290 300
DDENIRYQII TFLIAGHETT SGLLSFALYF LVKNPHVLQK AAEEAARVLV
310 320 330 340 350
DPVPSYKQVK QLKYVGMVLN EALRLWPTAP AFSLYAKEDT VLGGEYPLEK
360 370 380 390 400
GDELMVLIPQ LHRDKTIWGD DVEEFRPERF ENPSAIPQHA FKPFGNGQRA
410 420 430 440 450
CIGQQFALHE ATLVLGMMLK HFDFEDHTNY ELDIKETLTL KPEGFVVKAK
460 470 480 490 500
SKKIPLGGIP SPSTEQSAKK VRKKAENAHN TPLLVLYGSN MGTAEGTARD
510 520 530 540 550
LADIAMSKGF APQVATLDSH AGNLPREGAV LIVTASYNGH PPDNAKQFVD
560 570 580 590 600
WLDQASADEV KGVRYSVFGC GDKNWATTYQ KVPAFIDETL AAKGAENIAD
610 620 630 640 650
RGEADASDDF EGTYEEWREH MWSDVAAYFN LDIENSEDNK STLSLQFVDS
660 670 680 690 700
AADMPLAKMH GAFSTNVVAS KELQQPGSAR STRHLEIELP KEASYQEGDH
710 720 730 740 750
LGVIPRNYEG IVNRVTARFG LDASQQIRLE AEEEKLAHLP LAKTVSVEEL
760 770 780 790 800
LQYVELQDPV TRTQLRAMAA KTVCPPHKVE LEALLEKQAY KEQVLAKRLT
810 820 830 840 850
MLELLEKYPA CEMKFSEFIA LLPSIRPRYY SISSSPRVDE KQASITVSVV
860 870 880 890 900
SGEAWSGYGE YKGIASNYLA ELQEGDTITC FISTPQSEFT LPKDPETPLI
910 920 930 940 950
MVGPGTGVAP FRGFVQARKQ LKEQGQSLGE AHLYFGCRSP HEDYLYQEEL
960 970 980 990 1000
ENAQSEGIIT LHTAFSRMPN QPKTYVQHVM EQDGKKLIEL LDQGAHFYIC
1010 1020 1030 1040
GDGSQMAPAV EATLMKSYAD VHQVSEADAR LWLQQLEEKG RYAKDVWAG
Length:1,049
Mass (Da):117,781
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB0BE61F8A2EE33D5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J04832 Genomic DNA Translation: AAA87602.1
CP009920 Genomic DNA Translation: AJI21949.1
S87512 Genomic DNA Translation: AAK19020.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A34286

NCBI Reference Sequences

More...
RefSeqi
WP_034650526.1, NZ_CP035094.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AJI21949; AJI21949; BG04_163

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bmeg:BG04_163

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04832 Genomic DNA Translation: AAA87602.1
CP009920 Genomic DNA Translation: AJI21949.1
S87512 Genomic DNA Translation: AAK19020.1
PIRiA34286
RefSeqiWP_034650526.1, NZ_CP035094.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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[»]
3WSPX-ray1.80A/B1-456[»]
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[»]
4RSNX-ray2.70A/B1-456[»]
4WG2X-ray2.66A/B/C2-464[»]
4ZF6X-ray2.77A1-461[»]
4ZF8X-ray2.77A1-461[»]
4ZFAX-ray2.77A1-461[»]
4ZFBX-ray2.84A1-461[»]
5B2UX-ray1.90A/B1-456[»]
5B2VX-ray2.30A/B1-456[»]
5B2WX-ray1.65A/B1-456[»]
5B2XX-ray1.90A/B1-456[»]
5B2YX-ray2.01A/B1-456[»]
5DYPX-ray2.40A/C2-471[»]
5DYZX-ray1.97A/C2-471[»]
5E78X-ray2.00A/B2-456[»]
5E7YX-ray2.00A/B2-472[»]
5E9ZX-ray2.23A/B/C/D1-468[»]
5JQ2X-ray2.00A/B2-464[»]
5JQUX-ray2.16A/B/C/D/E/F/G/H2-464[»]
5JQVX-ray2.34A/B/C/D/E/F/G/H2-464[»]
5JTDX-ray1.50A/B2-464[»]
5OG9X-ray2.09A/B2-474[»]
5UCWX-ray1.70A/B1-464[»]
5XA3X-ray2.20A/B/C/D1-456[»]
5XHJX-ray2.00A/B1-456[»]
5ZISX-ray3.10A/B/C/D2-456[»]
5ZLHX-ray3.40A/B/C/D2-456[»]
6H1OX-ray1.73A/B2-458[»]
6H1SX-ray1.95A/B2-458[»]
6HN8X-ray2.00A/B1-456[»]
6IAOX-ray2.16A/B/C/D1-473[»]
6JLVX-ray1.22A/B1-456[»]
6JMHX-ray1.46A/B1-456[»]
6JMWX-ray1.85A/B1-457[»]
6JO1X-ray2.10A/B1-456[»]
6JS8X-ray1.36A/B1-456[»]
6JVCX-ray1.75A/C1-456[»]
6JZSX-ray1.68A/C1-457[»]
6K24X-ray2.10A/B2-457[»]
6K3QX-ray2.06A/B1-456[»]
6K58X-ray1.41A/B1-456[»]
6K9SX-ray1.55A/B1-456[»]
6L1AX-ray1.84A/B1-456[»]
6L1BX-ray1.74A/B1-456[»]
6LY4X-ray1.68A3-457[»]
SMRiP14779
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiP14779
DrugBankiDB08086, N-[12-(1H-imidazol-1-yl)dodecanoyl]-L-leucine
DB03440, N-hexadecanoylglycine
DB04257, Palmitoleic Acid

Proteomic databases

PRIDEiP14779

Genome annotation databases

EnsemblBacteriaiAJI21949; AJI21949; BG04_163
KEGGibmeg:BG04_163

Phylogenomic databases

HOGENOMiCLU_001570_7_0_9

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17698
BRENDAi1.1.1.B57, 656
1.14.14.1, 656
1.6.2.4, 656

Miscellaneous databases

EvolutionaryTraceiP14779

Family and domain databases

Gene3Di1.10.630.10, 1 hit
1.20.990.10, 1 hit
3.40.50.360, 1 hit
3.40.50.80, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00667, FAD_binding_1, 1 hit
PF00258, Flavodoxin_1, 1 hit
PF00175, NAD_binding_1, 1 hit
PF00067, p450, 1 hit
PIRSFiPIRSF000209, Bifunctional_P450_P450R, 1 hit
PRINTSiPR00369, FLAVODOXIN
PR00371, FPNCR
SUPFAMiSSF48264, SSF48264, 1 hit
SSF52218, SSF52218, 1 hit
SSF52343, SSF52343, 1 hit
SSF63380, SSF63380, 1 hit
PROSITEiView protein in PROSITE
PS00086, CYTOCHROME_P450, 1 hit
PS51384, FAD_FR, 1 hit
PS50902, FLAVODOXIN_LIKE, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCPXB_BACMB
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P14779
Secondary accession number(s): A0A0B6AQ66, Q9AE23
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 174 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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