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UniProtKB - O08336 (CYPB_BACSU)

Entry version 148 (10 Apr 2019)
Sequence version 1 (01 Jul 1997)
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Protein

Bifunctional cytochrome P450/NADPH--P450 reductase 2

Gene

cypB

Organism
Bacillus subtilis (strain 168)
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. 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 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 ‘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 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
  1. KM=165 µM for lauric acid1 Publication
  2. KM=542 µM for myristic acid1 Publication
  3. KM=337 µM for palmitic acid1 Publication
  4. KM=68.5 µM for stearic acid1 Publication
  5. KM=28.7 µM for phytanic acid1 Publication
  6. KM=68.3 µM for 15-methylpalmitic acid1 Publication
  7. KM=79 µM for arachidonic acid1 Publication
  8. KM=5.1 µM for NADPH1 Publication
  9. KM=2.43 mM for NADH1 Publication
  10. KM=10.9 µM for cytochrome c (in the reductase assay)1 Publication
  11. KM=285 µM for ferricyanide (in the reductase assay)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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>Sitei271Important for catalytic activityBy similarity1
    <p>This subsection of the ‘Function’ 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 bindingi403Iron (heme axial ligand)By similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ 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 bindingi492 – 497FMNBy similarity6
    Nucleotide bindingi539 – 542FMNBy similarity4
    Nucleotide bindingi573 – 575FMNBy similarity3
    Nucleotide bindingi581 – 583FMNBy similarity3

    <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

    View the complete GO annotation on QuickGO ...

    GO - Biological processi

    View the complete GO annotation on QuickGO ...

    <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    		BSUB:BSU27160-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		O08336

    <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 reductase 2Curated
    Alternative name(s):
    CYP102A31 Publication
    Fatty acid hydroxylase CypBCurated
    Flavocytochrome P450 102A3Curated
    Including the following 2 domains:
    Cytochrome P450 102A3Curated (EC:1.14.14.12 Publications)
    NADPH--cytochrome P450 reductase (EC:1.6.2.42 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:cypBImported
    Synonyms:cyp102A32 Publications, yrhJ2 Publications
    Ordered Locus Names:BSU27160
    <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 subtilis (strain 168)
    <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 identifieri224308 [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 lineageiBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›
    <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
    • UP000001570 <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

    GO - Cellular componenti

    View the complete GO annotation on QuickGO ...

    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

    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>Mutagenesisi89F → 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 Publication1
    Mutagenesisi190S → 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 Publication1

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000522071 – 1054Bifunctional cytochrome P450/NADPH--P450 reductase 2Add BLAST1054

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...    PaxDbi    		O08336

    PRoteomics IDEntifications database

    More...    PRIDEi    		O08336

    <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

    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

    <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

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...    STRINGi    		224308.BSU27160

    <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

    3D structure databases

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...    ProteinModelPortali    		O08336

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

    More...    SMRi    		O08336

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		Search...

    <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>Domaini486 – 625Flavodoxin-likePROSITE-ProRule annotationAdd BLAST140
    Domaini663 – 896FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST234

    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>Regioni1 – 475Cytochrome P4501 PublicationAdd BLAST475
    Regioni476 – 1053NADPH--P450 reductase1 PublicationAdd BLAST578

    <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

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4107EER Bacteria
    COG0369 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000093545

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		O08336

    KEGG Orthology (KO)

    More...    KOi    		K14338

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		EDYPACE

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		O08336

    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

    More...    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

    More...    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

    More...    PIRSFi    		PIRSF000209 Bifunctional_P450_P450R, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...    PRINTSi    		PR00369 FLAVODOXIN
    PR00371 FPNCR

    Superfamily database of structural and functional annotation

    More...    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>.<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.

    O08336-1 [UniParc]FASTAAdd to basket
    « Hide
            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
    Length:1,054
    Mass (Da):118,676
    Last modified:July 1, 1997 - v1
    <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:i705F8E27866CA110
    GO

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...    EMBLi

    GenBank nucleotide sequence database

    More...    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...    DDBJi
    Links Updated
    		U93874 Genomic DNA Translation: AAB80867.1
    AL009126 Genomic DNA Translation: CAB14658.1

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A69975

    NCBI Reference Sequences

    More...    RefSeqi    		NP_390594.1, NC_000964.3
    WP_003246174.1, NZ_JNCM01000036.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...    EnsemblBacteriai    		CAB14658; CAB14658; BSU27160

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		937585

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		bsu:BSU27160

    Pathosystems Resource Integration Center (PATRIC)

    More...    PATRICi    		fig|224308.179.peg.2949

    <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
    		U93874 Genomic DNA Translation: AAB80867.1
    AL009126 Genomic DNA Translation: CAB14658.1
    PIRiA69975
    RefSeqiNP_390594.1, NC_000964.3
    WP_003246174.1, NZ_JNCM01000036.1

    3D structure databases

    ProteinModelPortaliO08336
    SMRiO08336
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224308.BSU27160

    Proteomic databases

    PaxDbiO08336
    PRIDEiO08336

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiCAB14658; CAB14658; BSU27160
    GeneIDi937585
    KEGGibsu:BSU27160
    PATRICifig|224308.179.peg.2949

    Phylogenomic databases

    eggNOGiENOG4107EER Bacteria
    COG0369 LUCA
    HOGENOMiHOG000093545
    InParanoidiO08336
    KOiK14338
    OMAiEDYPACE
    PhylomeDBiO08336

    Enzyme and pathway databases

    BioCyciBSUB:BSU27160-MONOMER
    SABIO-RKiO08336

    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...    ProtoNeti    		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 nameiCYPB_BACSU
    <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: O08336
    <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: December 1, 2000
    Last sequence update: July 1, 1997
    Last modified: April 10, 2019
    This is version 148 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
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