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Entry version 35 (12 Aug 2020)
Sequence version 1 (11 Jul 2012)
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Protein

Galactose oxidase

Gene

GAOA

Organism
Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum)
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

Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.2 Publications

Caution

Was originally thought to originate from Polyporus circinatus then later from Dactylium dendroides and is now known to be originating from Gibberella (Fusarium).Curated

<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

Cu2+Note: Binds 1 Cu2+ ion per subunit.

<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 diethyldithiocarbamate.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

  1. KM=56 mM for 1-methyl-alpha-D-galactopyranoside5 Publications
  2. KM=57 mM for 2-methylene-1,3-propanediol5 Publications
  3. KM=68 mM for D-galactose5 Publications
  4. KM=2.5 M for D-fructose5 Publications

    pH dependencei

    Optimum pH is 7. Active from pH 5.7 to 9.4.5 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 bindingi313Copper1
    <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 sitei536Proton acceptor1 Publication1
    Metal bindingi536Copper1
    Metal bindingi537Copper1
    Metal bindingi622Copper1

    <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

    <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
    LigandCopper, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:MONOMER-15357

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P0CS93

    Protein family/group databases

    Carbohydrate-Active enZymes

    More...
    CAZyi
    AA5, Auxiliary Activities 5
    CBM32, Carbohydrate-Binding Module Family 32

    <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:
    Galactose oxidase (EC:1.1.3.9)
    Short name:
    GAO
    Short name:
    GO
    Short name:
    GOase
    <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:GAOA
    <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 zeae (Wheat head blight fungus) (Fusarium graminearum)
    <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 identifieri5518 [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 lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesNectriaceaeFusarium

    <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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    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>Mutagenesisi269C → G: Reduces catalytic activity more than 10000-fold. 1
    Mutagenesisi331W → F: Reduces catalytic efficiency 50-fold and substrate affinity 36-fold. 1
    Mutagenesisi331W → G: Reduces substrate affinity 20-fold and catalytic activity more than 6000-fold. 1
    Mutagenesisi331W → H: Reduces catalytic efficiency 1000-fold. 1
    Mutagenesisi371R → A: Reduces catalytic efficiency 250-fold and substrate affinity 22-fold for D-galactose, but improves catalytic efficiency 1.8-fold towards D-fructose. 1 Publication1
    Mutagenesisi371R → K: Reduces catalytic efficiency 45-fold and substrate affinity 8.7-fold for D-galactose, but improves catalytic efficiency 8-fold towards D-fructose. 1 Publication1
    Mutagenesisi424C → A: Reduces catalytic efficiency 1.5- to 2-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside. 1 Publication1
    Mutagenesisi424C → S: Improves catalytic efficiency 3- to 4-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside, mainly by increasing the affinity for the substrates. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with H-477. Improves catalytic efficiency 4.9-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with A-535. Improves catalytic activity 4.7-fold towards D-galactose, but only 1.8-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with A-477. 1 Publication1
    Mutagenesisi477Y → A: No effect. Improves catalytic efficiency 2- to 3-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside; when associated with A-535. Improves catalytic activity 4.7-fold towards D-galactose, but only 1.8-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with S-424. 1 Publication1
    Mutagenesisi477Y → H: No effect. Improves catalytic efficiency 5.3-fold towards D-galactose; when associated with S-424. 1 Publication1
    Mutagenesisi505F → A: Reduces catalytic efficiency 166-fold and substrate affinity 9-fold. 1 Publication1
    Mutagenesisi535V → A: Improves catalytic efficiency 1.3- to 1.8-fold. Improves catalytic efficiency 2- to 3-fold towards D-galactose and 1-methyl-alpha-D-galactopyranoside; when associated with A-477. Improves catalytic efficiency 4.9-fold towards 1-methyl-alpha-D-galactopyranoside; when associated with S-424. 1 Publication1
    Mutagenesisi536Y → F: Reduces catalytic efficiency 1000-fold, but does not reduce substrate affinity. 1

    <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 – 241 PublicationAdd BLAST24
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000028540725 – 412 PublicationsAdd BLAST17
    <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_000001661042 – 680Galactose oxidaseAdd BLAST639

    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 bondi59 ↔ 68
    <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-linki269 ↔ 3133'-(S-cysteinyl)-tyrosine (Cys-Tyr)
    Disulfide bondi556 ↔ 559

    <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

    Galactose oxidase contains a protein-derived free radical cofactor. In the active state, Tyr-313, which is cross-linked to Cys-269 via a thioether bond, is oxidized to a radical and acts with Cu2+ as a two-electron acceptor in the oxidation reaction. The cross-link is believed to modulate the redox potential of the tyrosyl radical, which is further stabilized by a stacking interaction with Trp-331 in the active site. The post-translational formation of the cross-link is closely linked to the propeptide cleavage event, and both are copper-dependent, autocatalytic processes. The propeptide may act as an intramolecular chaperone, facilitating thioester bond formation and copper binding by positioning of active-site residues, including copper ligands.

    Keywords - PTMi

    Disulfide bond, Thioether bond

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P0CS93

    <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.

    6 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

    1680
    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
    P0CS93

    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>Domaini42 – 189F5/8 type CPROSITE-ProRule annotationAdd BLAST148
    <p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati223 – 268Kelch 1Add BLAST46
    Repeati279 – 321Kelch 2Add BLAST43
    Repeati323 – 372Kelch 3Add BLAST50
    Repeati436 – 490Kelch 4Add BLAST55
    Repeati492 – 544Kelch 5Add BLAST53

    Keywords - Domaini

    Kelch repeat, Repeat, Signal

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd02851, E_set_GO_C, 1 hit
    cd00057, FA58C, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.130.10.80, 1 hit
    2.60.120.260, 1 hit
    2.60.40.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000421, FA58C
    IPR011043, Gal_Oxase/kelch_b-propeller
    IPR037293, Gal_Oxidase_central_sf
    IPR008979, Galactose-bd-like_sf
    IPR015202, GO-like_E_set
    IPR013783, Ig-like_fold
    IPR014756, Ig_E-set
    IPR006652, Kelch_1

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF09118, DUF1929, 1 hit
    PF00754, F5_F8_type_C, 1 hit
    PF01344, Kelch_1, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00231, FA58C, 1 hit
    SM00612, Kelch, 3 hits

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF49785, SSF49785, 1 hit
    SSF50965, SSF50965, 1 hit
    SSF81296, SSF81296, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50022, FA58C_3, 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.

    P0CS93-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKHLLTLALC FSSINAVAVT VPHKAVGTGI PEGSLQFLSL RASAPIGSAI
    60 70 80 90 100
    SRNNWAVTCD SAQSGNECNK AIDGNKDTFW HTFYGANGDP KPPHTYTIDM
    110 120 130 140 150
    KTTQNVNGLS MLPRQDGNQN GWIGRHEVYL SSDGTNWGSP VASGSWFADS
    160 170 180 190 200
    TTKYSNFETR PARYVRLVAI TEANGQPWTS IAEINVFQAS SYTAPQPGLG
    210 220 230 240 250
    RWGPTIDLPI VPAAAAIEPT SGRVLMWSSY RNDAFGGSPG GITLTSSWDP
    260 270 280 290 300
    STGIVSDRTV TVTKHDMFCP GISMDGNGQI VVTGGNDAKK TSLYDSSSDS
    310 320 330 340 350
    WIPGPDMQVA RGYQSSATMS DGRVFTIGGS WSGGVFEKNG EVYSPSSKTW
    360 370 380 390 400
    TSLPNAKVNP MLTADKQGLY RSDNHAWLFG WKKGSVFQAG PSTAMNWYYT
    410 420 430 440 450
    SGSGDVKSAG KRQSNRGVAP DAMCGNAVMY DAVKGKILTF GGSPDYQDSD
    460 470 480 490 500
    ATTNAHIITL GEPGTSPNTV FASNGLYFAR TFHTSVVLPD GSTFITGGQR
    510 520 530 540 550
    RGIPFEDSTP VFTPEIYVPE QDTFYKQNPN SIVRVYHSIS LLLPDGRVFN
    560 570 580 590 600
    GGGGLCGDCT TNHFDAQIFT PNYLYNSNGN LATRPKITRT STQSVKVGGR
    610 620 630 640 650
    ITISTDSSIS KASLIRYGTA THTVNTDQRR IPLTLTNNGG NSYSFQVPSD
    660 670 680
    SGVALPGYWM LFVMNSAGVP SVASTIRVTQ
    Length:680
    Mass (Da):72,823
    Last modified:July 11, 2012 - 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:i2F97C561B63E46E9
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti111M → I in AAB94635 (Ref. 4) Curated1

    <p>This subsection of the 'Sequence' section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

    Molecular mass is 68520 Da. Determined by ESI. 1 Publication

    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
    M86819 Unassigned DNA Translation: AAA16228.1
    AH005781 Genomic DNA Translation: AAB94635.1

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Worthington enzyme manual

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M86819 Unassigned DNA Translation: AAA16228.1
    AH005781 Genomic DNA Translation: AAB94635.1

    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
    1GOFX-ray1.70A42-680[»]
    1GOGX-ray1.90A42-680[»]
    1GOHX-ray2.20A42-680[»]
    1K3IX-ray1.40A25-680[»]
    1T2XX-ray2.30A42-680[»]
    2EIBX-ray2.10A42-680[»]
    2EICX-ray2.80A42-680[»]
    2EIDX-ray2.20A42-680[»]
    2EIEX-ray1.80A42-680[»]
    2JKXX-ray1.84A42-680[»]
    2VZ1X-ray1.91A42-680[»]
    2VZ3X-ray1.90A42-680[»]
    2WQ8X-ray2.19A42-680[»]
    SMRiP0CS93
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein family/group databases

    CAZyiAA5, Auxiliary Activities 5
    CBM32, Carbohydrate-Binding Module Family 32

    Proteomic databases

    PRIDEiP0CS93

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-15357
    SABIO-RKiP0CS93

    Family and domain databases

    CDDicd02851, E_set_GO_C, 1 hit
    cd00057, FA58C, 1 hit
    Gene3Di2.130.10.80, 1 hit
    2.60.120.260, 1 hit
    2.60.40.10, 1 hit
    InterProiView protein in InterPro
    IPR000421, FA58C
    IPR011043, Gal_Oxase/kelch_b-propeller
    IPR037293, Gal_Oxidase_central_sf
    IPR008979, Galactose-bd-like_sf
    IPR015202, GO-like_E_set
    IPR013783, Ig-like_fold
    IPR014756, Ig_E-set
    IPR006652, Kelch_1
    PfamiView protein in Pfam
    PF09118, DUF1929, 1 hit
    PF00754, F5_F8_type_C, 1 hit
    PF01344, Kelch_1, 1 hit
    SMARTiView protein in SMART
    SM00231, FA58C, 1 hit
    SM00612, Kelch, 3 hits
    SUPFAMiSSF49785, SSF49785, 1 hit
    SSF50965, SSF50965, 1 hit
    SSF81296, SSF81296, 1 hit
    PROSITEiView protein in PROSITE
    PS50022, FA58C_3, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiGAOA_GIBZA
    <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: P0CS93
    Secondary accession number(s): O43098, Q01745, Q4HVH6
    <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: July 11, 2012
    Last sequence update: July 11, 2012
    Last modified: August 12, 2020
    This is version 35 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

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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