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UniProtKB - Q9HGE0 (FUM6_GIBM7)

Entry version 111 (07 Apr 2021)
Sequence version 1 (01 Mar 2001)
Previous versions | rss
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Protein

Bifunctional cytochrome P450/NADPH--P450 reductase

Gene

FUM6

Organism
Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
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 transcript 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

Bifunctional cytochrome P450/NADPH--P450 reductase; part of the gene cluster that mediates the biosynthesis of fumonisins B1 (FB1), B2 (FB2), B3 (FB3), and B4 (FB4), which are carcinogenic mycotoxins (PubMed:11728154, PubMed:15137825). On the basis of the chemical structures of fumonisins and precursor feeding studies, fumonisin biosynthesis is predicted to include at least five groups of biochemical reactions: synthesis of a linear polyketide with a single terminal carbonyl function and methyl groups at C-10 and C-14; condensation of the polyketide with alanine; reduction of the polyketide carbonyl to a hydroxyl; hydroxylation of 2-4 polyketide carbons; and esterification of six-carbon tricarboxylic acids to two of the hydroxyls (PubMed:12620260). The biosynthesis starts with the polyketide synthase FUM1-catalyzed carbon chain assembly from one molecule of acetyl CoA, eight molecules of malonyl CoA, and two molecules of methionine (PubMed:10413619). The C-18 polyketide chain is released from the enzyme by a nucleophilic attack of a carbanion, which is derived from R-carbon of alanine by decarboxylation, on the carbonyl carbon of polyketide acyl chain (PubMed:15137825, PubMed:12720383). This step is catalyzed by a pyridoxal 5'-phosphate-dependent aminoacyl transferase FUM8 (PubMed:15137825, PubMed:12720383). The resultant 3-keto intermediate 2-amino-3-oxo-12,16-dimethylicosane is then stereospecifically reduced to the 3-hydroxyl product 2-amino-3-hydroxy-12,16-dimethylicosane by reductase FUM13 (PubMed:12720383, PubMed:15137825). Subsequent oxidations at C-5, C-10, C-14 and C-15 followed by tricarballylic esterification of the hydroxyl groups on C-14 and C-15 furnish the biosynthesis of fumonisins (PubMed:15066782, PubMed:15137825, PubMed:16489749). The C-10 hydroxylation is performed by the cytochrome P450 monooxygenase FUM2 and occurs early in the biosynthesis (PubMed:16536629). The C-5 hydroxylation is performed by the dioxygenase FUM3 and occurs late in the biosynthesis (PubMed:20237561, PubMed:15066782, PubMed:15137825, PubMed:16536629). Cytochrome P450 monooxygenases FUM6 and FUM15 may be responsible for the two remaining hydroxylations at positions C-14 and C-15 (PubMed:12620260). The FUM11 tricarboxylate transporter makes a tricarboxylic acid precursor available for fumonisin biosynthesis via its export from the mitochondria (PubMed:12620260). If the precursor is citrate, the FUM7 dehydrogenase could remove the C-3 hydroxyl of citrate to form tricarballylic acid either before or after the CoA activation by the FUM10 acyl-CoA synthetase and FUM14 catalyzed esterification of CoA-activated tricarballylic acid to the C-14 and C-15 hydroxyls of the fumonisin backbone (PubMed:16489749, PubMed:17147424). Alternatively, if the precursor is cis-aconitate, FUM7 may function to reduce the double bond (PubMed:17147424). In this alternate proposal, feeding studies with tetradehydro-fumonisin B1 suggests that FUM7 cannot function on the tricarballylic ester and must therefore act before the FUM14-mediated esterification (PubMed:17147424).10 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: Mycotoxin biosynthesis

This protein is involved in Mycotoxin biosynthesis.2 Publications
View all proteins of this organism that are known to be involved in Mycotoxin biosynthesis.

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>Sitei288Important for catalytic activityBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi422Iron (heme axial ligand)By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei618FMNBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi528 – 533FMNBy similarity6
Nucleotide bindingi528 – 532FMNPROSITE-ProRule annotation5
Nucleotide bindingi576 – 579FMNBy similarity4
Nucleotide bindingi607 – 639FMNPROSITE-ProRule annotationAdd BLAST33

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

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

<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%5Fand%5Ftaxonomy%5Fsection">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 reductase1 Publication
Alternative name(s):
Fumonisin biosynthesis cluster protein 61 Publication
Including the following 2 domains:
Cytochrome P450 monooxygenaseBy similarity (EC:1.14.14.1By similarity)
NADPH--cytochrome P450 reductaseBy similarity (EC:1.6.2.4By similarity)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:FUM61 Publication
ORF Names:FVEG_00317
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiGibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot fungus) (Fusarium verticillioides)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri334819 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Fusarium › Fusarium fujikuroi species complex ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000009096 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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> Componentsi: Chromosome 1, Unassembled WGS sequence

<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 in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs the production of fumonisins (PubMed:11728154, PubMed:15137825).2 Publications

<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_00004411441 – 1115Bifunctional cytochrome P450/NADPH--P450 reductaseAdd BLAST1115

<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

Expression correlates with fuminisins production (PubMed:11728154).1 Publication

<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		117187.FVEG_00317T0

<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

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

More...SMRi		Q9HGE0

Database of comparative protein structure models

More...ModBasei		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%5Fand%5Fdomains%5Fsection">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>Domaini522 – 664Flavodoxin-likePROSITE-ProRule annotationAdd BLAST143
Domaini703 – 952FAD-binding FR-typePROSITE-ProRule annotationAdd BLAST250

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>Regioni16 – 494Cytochrome P450By similarityAdd BLAST479
Regioni495 – 1115NADPH-P-450 reductaseBy similarityAdd BLAST621

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili219 – 246Sequence analysisAdd BLAST28

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0157, Eukaryota
KOG1158, Eukaryota

Identification of Orthologs from Complete Genome Data

More...OMAi		ASYNGEP

Database of Orthologous Groups

More...OrthoDBi		174046at2759

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
IPR002401, Cyt_P450_E_grp-I
IPR036396, Cyt_P450_sf
IPR017927, FAD-bd_FR_type
IPR008254, Flavodoxin/NO_synth
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		PR00463, EP450I
PR00385, P450

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q9HGE0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSATALFTRR SVSTSNPELR PIPGPKPLPL LGNLFDFDFD NLTKSLGELG 
        60         70         80         90        100
KIHGPIYSIT FGASTEIMVT SREIAQELCD ETRFCKLPGG ALDVMKAVVG 
       110        120        130        140        150
DGLFTAETSN PKWAIAHRII TPLFGAMRIR GMFDDMKDIC EQMCLRWARF 
       160        170        180        190        200
GPDEPLNVCD NMTKLTLDTI ALCTIDYRFN SFYRENGAAH PFAEAVVDVM 
       210        220        230        240        250
TESFDQSNLP DFVNNYVRFR AMAKFKRQAA ELRRQTEELI AARRQNPVDR 
       260        270        280        290        300
DDLLNAMLSA KDPKTGEGLS PESIVDNLLT FLIAGHETTS SLLSFCFYYL 
       310        320        330        340        350
LENPHVLRRV QQEVDTVVGS DTITVDHLSS MPYLEAVLRE TLRLRDPGPG 
       360        370        380        390        400
FYVKPLKDEV VAGKYAVNKD QPLFIVFDSV HRDQSTYGAD ADEFRPERML 
       410        420        430        440        450
KDGFDKLPPC AWKPFGNGVR ACVGRPFAMQ QAILAVAMVL HKFDLVKDES 
       460        470        480        490        500
YTLKYHVTMT VRPVGFTMKV RLRQGQRATD LAMGLHRGHS QEASAAASPS 
       510        520        530        540        550
RASLKRLSSD VNGDDTDHKS QIAVLYASNS GSCEALAYRL AAEATERGFG 
       560        570        580        590        600
IRAVDVVNNA IDRIPVGSPV ILITASYNGE PADDAQEFVP WLKSLESGRL 
       610        620        630        640        650
NGVKFAVFGN GHRDWANTLF AVPRLIDSEL ARCGAERVSL MGVSDTCDSS 
       660        670        680        690        700
DPFSDFERWI DEKLFPELET PHGPGGVKNG DRAVPRQELQ VSLGQPPRIT 
       710        720        730        740        750
MRKGYVRAIV TEARSLSSPG VPEKRHLELL LPKDFNYKAG DHVYILPRNS 
       760        770        780        790        800
PRDVVRALSY FGLGEDTLIT IRNTARKLSL GLPLDTPITA TDLLGAYVEL 
       810        820        830        840        850
GRTASLKNLW TLVDAAGHGS RAALLSLTEP ERFRAEVQDR HVSILDLLER 
       860        870        880        890        900
FPDIDLSLSC FLPMLAQIRP RAYSFSSAPD WKPGHATLTY TVVDFATPAT 
       910        920        930        940        950
QGINGSSKSK AVGDGTAVVQ RQGLASSYLS SLGPGTSLYV SLHRASPYFC 
       960        970        980        990       1000
LQKSTSLPVI MVGAGTGLAP FRAFLQERRM AAEGAKQRFG PALLFFGCRG 
      1010       1020       1030       1040       1050
PRLDSLYSVE LEAYETIGLV QVRRAYSRDP SAQDAQGCKY VTDRLGKCRD 
      1060       1070       1080       1090       1100
EVARLWMDGA QVLVCGGKKM ANDVLEVLGP MLLEIDQKRG ETTAKTVVEW 
      1110 
RARLDKSRYV EEVYV
Length:1,115
Mass (Da):123,277
Last modified:March 1, 2001 - 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:i5C6D2B947AE86C25
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence EWG36196 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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
AF155773 Genomic DNA Translation: AAG27132.1
DS022242 Genomic DNA Translation: EWG36196.1 Sequence problems.

NCBI Reference Sequences

More...RefSeqi		XP_018742387.1, XM_018886755.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		30058695

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		fvr:FVEG_00317

<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
AF155773 Genomic DNA Translation: AAG27132.1
DS022242 Genomic DNA Translation: EWG36196.1 Sequence problems.
RefSeqiXP_018742387.1, XM_018886755.1

3D structure databases

SMRiQ9HGE0
ModBaseiSearch...

Protein-protein interaction databases

STRINGi117187.FVEG_00317T0

Genome annotation databases

GeneIDi30058695
KEGGifvr:FVEG_00317

Phylogenomic databases

eggNOGiKOG0157, Eukaryota
KOG1158, Eukaryota
OMAiASYNGEP
OrthoDBi174046at2759

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
IPR002401, Cyt_P450_E_grp-I
IPR036396, Cyt_P450_sf
IPR017927, FAD-bd_FR_type
IPR008254, Flavodoxin/NO_synth
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
PRINTSiPR00463, EP450I
PR00385, P450
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...

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 nameiFUM6_GIBM7
<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: Q9HGE0
Secondary accession number(s): W7LC82
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 30, 2017
Last sequence update: March 1, 2001
Last modified: April 7, 2021
This is version 111 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 programFungal 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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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