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UniProtKB - Q8GTB6 (THCAS_CANSA)

Entry version 77 (23 Feb 2022)
Sequence version 1 (01 Mar 2003)
Previous versions | rss
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Protein

Tetrahydrocannabinolic acid synthase

Gene

THCAS

Organism
Cannabis sativa (Hemp) (Marijuana)
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

Oxidoreductase involved in the biosynthesis of cannabinoids-related terpenophenolic natural products, which have pharmacological activity (PubMed:15190053, PubMed:17669365, Ref. 4).

Catalyzes the oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA), producing delta9-tetrahydrocannabinolate (THCA), the major cannabioid in drug-type Cannabis plants (PubMed:15190053, PubMed:17669365, Ref. 4).

Can also use cannabinerolic acid as substrate, but not cannabigerol or cannabinerol (PubMed:15190053, PubMed:17669365, Ref. 4).

3 Publications

Miscellaneous

THCA synthase might contribute to the self-defense of Cannabis plants by producing both THCA and hydrogen peroxide, but since these reaction products are toxic to the plant itself, THCA synthase must be secreted from secretory cells into the storage cavity to avoid cellular damage.

<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

FAD1 PublicationNote: Binds 1 FAD per subunit in a bicovalent manner.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 Hg2+.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 0.30 sec(-1) for cannabigerolate.
  1. KM=134 µM for cannabigerolic acid2 Publications
  2. KM=254 µM for cannabinerolic acid2 Publications
  1. Vmax=2.68 nmol/sec/mg enzyme with cannabigerolic acid as substrate2 Publications
  2. Vmax=0.37 nmol/sec/mg enzyme with cannabinerolic acid as substrate2 Publications

pH dependencei

Optimum pH is 5.5-6.0.2 Publications

<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: terpenoid biosynthesis

This protein is involved in the pathway terpenoid biosynthesis, which is part of Secondary metabolite biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway terpenoid biosynthesis and in Secondary metabolite biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei120FADCombined sources1 Publication1
Binding sitei176FADCombined sources1 Publication1
Binding sitei190FAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei236FADCombined sources1 Publication1
Binding sitei241FAD; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei292Cannabigerolate1 Publication1
Binding sitei417Cannabigerolate1 Publication1
Binding sitei442CannabigerolateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei484Proton acceptor1 Publication1

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 bindingi109 – 115FADCombined sources1 Publication7
Nucleotide bindingi180 – 184FADCombined sources1 Publication5
Nucleotide bindingi481 – 483FADCombined 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

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 functionOxidoreductase
LigandFAD, Flavoprotein

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.21.3.7, 1159

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...UniPathwayi		UPA00213

<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:
Tetrahydrocannabinolic acid synthase1 Publication (EC:1.21.3.73 Publications)
Short name:
THCA synthase1 Publication
Alternative name(s):
Delta(1)-tetrahydrocannabinolic acid synthase1 Publication
<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:THCAS1 Publication
<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>OrganismiCannabis sativa (Hemp) (Marijuana)
<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 identifieri3483 [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 › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › rosids › fabids › Rosales › Cannabaceae › Cannabis

<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

Apoplast, Secreted

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi92H → A: No effect. 1 Publication1
Mutagenesisi108R → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi110R → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi114H → A: Loss of FAD binding and loss of catalytic activity. 2 Publications1
Mutagenesisi208H → A: No effect. 1 Publication1
Mutagenesisi292H → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi417Y → F: Reduced catalytic activity. 1 Publication1
Mutagenesisi442E → Q: Slightly reduced catalytic activity. 1 Publication1
Mutagenesisi484Y → F: Loss of catalytic activity. 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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 282 PublicationsAdd BLAST28
<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_000042114229 – 545Tetrahydrocannabinolic acid synthaseAdd BLAST517

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi37 ↔ 99Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi65N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Glycosylationi89N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki114 ↔ 1766-(S-cysteinyl)-8alpha-(pros-histidyl)-FAD (His-Cys)1 Publication
Glycosylationi168N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Glycosylationi297N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi305N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi329N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Glycosylationi467N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1
Glycosylationi499N-linked (GlcNAc...) asparaginePROSITE-ProRule annotationCombined sources1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Glycosylated when produced in a heterologous system. The deglycosylated THCA synthase has more catalytic activity than the glycosylated form.2 Publications
The FAD cofactor is bound via a bicovalent 6-S-cysteinyl, 8alpha-N1-histidyl FAD linkage.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in the secretory cells of glandular trichomes.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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

2 Publications

<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

1545
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

More...SMRi		Q8GTB6

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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>Domaini77 – 251FAD-binding PCMH-typePROSITE-ProRule annotationAdd BLAST175

<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

Belongs to the oxygen-dependent FAD-linked oxidoreductase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.43.10, 1 hit
3.30.465.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012951, BBE
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
IPR006094, Oxid_FAD_bind_N

Pfam protein domain database

More...Pfami		View protein in Pfam
PF08031, BBE, 1 hit
PF01565, FAD_binding_4, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF56176, SSF56176, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51387, FAD_PCMH, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GTB6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNCSAFSFWF VCKIIFFFLS FHIQISIANP RENFLKCFSK HIPNNVANPK 
        60         70         80         90        100
LVYTQHDQLY MSILNSTIQN LRFISDTTPK PLVIVTPSNN SHIQATILCS 
       110        120        130        140        150
KKVGLQIRTR SGGHDAEGMS YISQVPFVVV DLRNMHSIKI DVHSQTAWVE 
       160        170        180        190        200
AGATLGEVYY WINEKNENLS FPGGYCPTVG VGGHFSGGGY GALMRNYGLA 
       210        220        230        240        250
ADNIIDAHLV NVDGKVLDRK SMGEDLFWAI RGGGGENFGI IAAWKIKLVA 
       260        270        280        290        300
VPSKSTIFSV KKNMEIHGLV KLFNKWQNIA YKYDKDLVLM THFITKNITD 
       310        320        330        340        350
NHGKNKTTVH GYFSSIFHGG VDSLVDLMNK SFPELGIKKT DCKEFSWIDT 
       360        370        380        390        400
TIFYSGVVNF NTANFKKEIL LDRSAGKKTA FSIKLDYVKK PIPETAMVKI 
       410        420        430        440        450
LEKLYEEDVG AGMYVLYPYG GIMEEISESA IPFPHRAGIM YELWYTASWE 
       460        470        480        490        500
KQEDNEKHIN WVRSVYNFTT PYVSQNPRLA YLNYRDLDLG KTNHASPNNY 
       510        520        530        540 
TQARIWGEKY FGKNFNRLVK VKTKVDPNNF FRNEQSIPPL PPHHH
Length:545
Mass (Da):61,927
Last modified:March 1, 2003 - 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:i6C24D805208E7421
GO

<p>This subsection of the 'Sequence' section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement%5Fin%5Fdisease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Several isoforms of the active tetrahydrocannabinolic acid synthase found in the 'drug-type' cannabis plants exist due to polymorphism.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti63I → L in strain: 001. 1 Publication1

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
AB057805 mRNA Translation: BAC41356.1
AB212829 Genomic DNA Translation: BAE48241.1
AB212832 Genomic DNA Translation: BAE48244.1
AB212834 Genomic DNA Translation: BAE48246.1
AB212835 Genomic DNA Translation: BAE48247.1
AB212837 Genomic DNA Translation: BAE48249.1
AB212838 Genomic DNA Translation: BAE48250.1
AB183698 Genomic DNA Translation: BAD82947.1
AB183699 Genomic DNA Translation: BAD82948.1
AB183700 Genomic DNA Translation: BAD82949.1
AB183701 Genomic DNA Translation: BAD82950.1
AB183702 Genomic DNA Translation: BAD82951.1
AB183703 Genomic DNA Translation: BAD82952.1
AB183704 Genomic DNA Translation: BAD82953.1
AB183705 Genomic DNA Translation: BAD82954.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:BAC41356

<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
AB057805 mRNA Translation: BAC41356.1
AB212829 Genomic DNA Translation: BAE48241.1
AB212832 Genomic DNA Translation: BAE48244.1
AB212834 Genomic DNA Translation: BAE48246.1
AB212835 Genomic DNA Translation: BAE48247.1
AB212837 Genomic DNA Translation: BAE48249.1
AB212838 Genomic DNA Translation: BAE48250.1
AB183698 Genomic DNA Translation: BAD82947.1
AB183699 Genomic DNA Translation: BAD82948.1
AB183700 Genomic DNA Translation: BAD82949.1
AB183701 Genomic DNA Translation: BAD82950.1
AB183702 Genomic DNA Translation: BAD82951.1
AB183703 Genomic DNA Translation: BAD82952.1
AB183704 Genomic DNA Translation: BAD82953.1
AB183705 Genomic DNA Translation: BAD82954.1

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
3VTEX-ray2.75A28-545[»]
SMRiQ8GTB6
ModBaseiSearch...
PDBe-KBiSearch...

Genome annotation databases

KEGGiag:BAC41356

Enzyme and pathway databases

UniPathwayiUPA00213
BRENDAi1.21.3.7, 1159

Family and domain databases

Gene3Di3.30.43.10, 1 hit
3.30.465.10, 1 hit
InterProiView protein in InterPro
IPR012951, BBE
IPR016166, FAD-bd_PCMH
IPR036318, FAD-bd_PCMH-like_sf
IPR016167, FAD-bd_PCMH_sub1
IPR016169, FAD-bd_PCMH_sub2
IPR006094, Oxid_FAD_bind_N
PfamiView protein in Pfam
PF08031, BBE, 1 hit
PF01565, FAD_binding_4, 1 hit
SUPFAMiSSF56176, SSF56176, 1 hit
PROSITEiView protein in PROSITE
PS51387, FAD_PCMH, 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 nameiTHCAS_CANSA
<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: Q8GTB6
Secondary accession number(s): Q33DQ4, Q5NTX8
<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: February 6, 2013
Last sequence update: March 1, 2003
Last modified: February 23, 2022
This is version 77 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 programPlant 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, Direct protein sequencing

Documents

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