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Entry version 2 (11 Dec 2019)
Sequence version 1 (13 Nov 2019)
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Protein

A type blood N-acetyl-alpha-D-galactosamine deacetylase

Gene
N/A
Organism
Flavonifractor plautii (Fusobacterium plautii)
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

One of an enzyme pair that work together to convert the A antigen to the H antigen of the O blood type, which together release galactosamine. Catalyzes the first step in the conversion, generating the substrate for the subsequent enzyme (FpGalNase, AC P0DTR5). Works on many different A antigen subtypes. Glu-90 probably activates a nucleophilic water molecule to start the deacetylation reaction.1 Publication

Miscellaneous

DNA was isolated from a male human fecal sample of AB+ blood type, the sequence was given to UniProtKB by the submitters.1 Publication

<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

a divalent metal cation1 Publication

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

Inhibited by EDTA.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=340 µM for A antigen type 1 penta-MU1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei87SubstrateCombined sources1 Publication1
    Binding sitei123SubstrateCombined sources1 Publication1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi126Divalent metal cationCombined sources1 Publication1
    Binding sitei236SubstrateCombined sources1 Publication1
    Metal bindingi278Divalent metal cationCombined sources1 Publication1

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

    GO - Biological processi

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

    Molecular functionGlycosidase, Hydrolase
    LigandMetal-binding

    <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:
    A type blood N-acetyl-alpha-D-galactosamine deacetylase1 Publication (EC:3.5.1.-1 Publication)
    Alternative name(s):
    CBM321 Publication
    FpGalNAc deacetylase
    Short name:
    FpGalNAcDeAc1 Publication
    <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>OrganismiFlavonifractor plautii (Fusobacterium plautii)
    <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 identifieri292800 [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 lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeFlavonifractor

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

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

    5 µg/ml of this enzyme pair converts A blood type to O blood type in an hour, and can be removed by centrifugation, showing the pair can be used for production of universal type donor blood.1 Publication

    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>Mutagenesisi90E → A or L: Loss of deacetylase activity. 1 Publication1
    Mutagenesisi125C → A or S: 5-fold reduction in deacetylase rate. 1 Publication1
    Mutagenesisi126D → N: Dramatic reduction in deacetylase rate. 1 Publication1
    Mutagenesisi278H → A or F: Very dramatic reduction in deacetylase rate. 1 Publication1
    Mutagenesisi341Y → F: 3000-fold reduction in deacetylase rate. 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 – 27Sequence analysisAdd BLAST27
    <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_000044857128 – 772A type blood N-acetyl-alpha-D-galactosamine deacetylaseAdd BLAST745

    <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

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    SWISS-MODEL Interactive Workspace

    More...
    SWISS-MODEL-Workspacei
    Submit a new modelling project...

    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_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>Domaini494 – 605F5/8 type CPROSITE-ProRule annotationAdd BLAST112

    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>Regioni180 – 402Deacetylase activity1 PublicationAdd BLAST223
    Regioni502 – 765CBM32 carbohydrate-binding domain1 PublicationAdd BLAST264
    Regioni515 – 772Not required for activity on soluble substrates1 PublicationAdd BLAST258

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The deacetylase domain is in the N-terminus, while the C-terminus has a CBM32-type carbohydrate-binding domain that is not required for activity on soluble substrates. The CBM32 domain binds preferentially to repeating N-acetyl lactosamine structures.1 Publication

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.115.10.20, 1 hit
    2.60.120.260, 2 hits

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR003343 Big_2
    IPR000421 FA58C
    IPR008979 Galactose-bd-like_sf
    IPR023296 Glyco_hydro_beta-prop_sf
    IPR008964 Invasin/intimin_cell_adhesion
    IPR036278 Sialidase_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02368 Big_2, 1 hit
    PF00754 F5_F8_type_C, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00635 BID_2, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF49373 SSF49373, 1 hit
    SSF49785 SSF49785, 1 hit
    SSF50939 SSF50939, 1 hit
    SSF75005 SSF75005, 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

    <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 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.

    P0DTR4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MRNRRKAVSL LTGLLVTAQL FPTAALAADS SESALNKAPG YQDFPAYYSD
    60 70 80 90 100
    SAHADDQVTH PDVVVLEEPW NGYRYWAVYT PNVMRISIYE NPSIVASSDG
    110 120 130 140 150
    VHWVEPEGLS NPIEPQPPST RYHNCDADMV YNAEYDAMMA YWNWADDQGG
    160 170 180 190 200
    GVGAEVRLRI SYDGVHWGVP VTYDEMTRVW SKPTSDAERQ VADGEDDFIT
    210 220 230 240 250
    AIASPDRYDM LSPTIVYDDF RDVFILWANN TGDVGYQNGQ ANFVEMRYSD
    260 270 280 290 300
    DGITWGEPVR VNGFLGLDEN GQQLAPWHQD VQYVPDLKEF VCISQCFAGR
    310 320 330 340 350
    NPDGSVLHLT TSKDGVNWEQ VGTKPLLSPG PDGSWDDFQI YRSSFYYEPG
    360 370 380 390 400
    SSAGDGTMRV WYSALQKDTN NKMVADSSGN LTIQAKSEDD RIWRIGYAEN
    410 420 430 440 450
    SFVEMMRVLL DDPGYTTPAL VSGNSLMLSA ETTSLPTGDV MKLETSFAPV
    460 470 480 490 500
    DTSDQVVKYT SSDPDVATVD EFGTITGVSV GSARIMAETR EGLSDDLEIA
    510 520 530 540 550
    VVENPYTLIP QSNMTATATS VYGGTTEGPA SNVLDGNVRT IWHTNYAPKD
    560 570 580 590 600
    ELPQSITVSF DQPYTVGRFV YTPRQNGTNG IISEYELYAI HQDGSKDLVA
    610 620 630 640 650
    SGSDWALDAK DKTVSFAPVE AVGLELKAIA GAGGFGTAAE LNVYAYGPIE
    660 670 680 690 700
    PAPVYVPVDD RDASLVFTGA WNSDSNGSFY EGTARYTNEI GASVEFTFVG
    710 720 730 740 750
    TAIRWYGQND VNFGAAEVYV DGVLAGEVNV YGPAAAQQLL FEADGLAYGK
    760 770
    HTIRIVCVSP VVDFDYFSYV GE
    Length:772
    Mass (Da):84,441
    Last modified:November 13, 2019 - 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:i55C1AD3F8018D0D7
    GO

    Sequence databases

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_009260926.1, NZ_SPHS01000039.1

    <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

    Sequence databases

    RefSeqiWP_009260926.1, NZ_SPHS01000039.1

    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
    6N1AX-ray1.60A28-509[»]
    6N1BX-ray1.30A28-509[»]
    ModBaseiSearch...
    SWISS-MODEL-WorkspaceiSubmit a new modelling project...
    PDBe-KBiSearch...

    Family and domain databases

    Gene3Di2.115.10.20, 1 hit
    2.60.120.260, 2 hits
    InterProiView protein in InterPro
    IPR003343 Big_2
    IPR000421 FA58C
    IPR008979 Galactose-bd-like_sf
    IPR023296 Glyco_hydro_beta-prop_sf
    IPR008964 Invasin/intimin_cell_adhesion
    IPR036278 Sialidase_sf
    PfamiView protein in Pfam
    PF02368 Big_2, 1 hit
    PF00754 F5_F8_type_C, 1 hit
    SMARTiView protein in SMART
    SM00635 BID_2, 1 hit
    SUPFAMiSSF49373 SSF49373, 1 hit
    SSF49785 SSF49785, 1 hit
    SSF50939 SSF50939, 1 hit
    SSF75005 SSF75005, 1 hit
    PROSITEiView protein in PROSITE
    PS50022 FA58C_3, 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 nameiADAC_FLAPL
    <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: P0DTR4
    <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: November 13, 2019
    Last sequence update: November 13, 2019
    Last modified: December 11, 2019
    This is version 2 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

    3D-structure

    Documents

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