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Entry version 71 (02 Jun 2021)
Sequence version 1 (14 Dec 2011)
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Protein

Alpha-galactosidase

Gene

galA

Organism
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
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

Hydrolyzes the short-chain alpha-galactosaccharides raffinose, melibiose and stachyose.

2 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 <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 hydrolyzation product alpha-galactopyranose and to a lesser extent by beta-galactopyranose, its mutarotational product (PubMed:26005928). Inhibited by synthetic cyclopropyl carbasugars (PubMed:27783466).2 Publications

<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 176 s1 for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius). kcat is 109 s1 for raffinose (at pH 5.0 and 75 degrees Celsius) (PubMed:9741105). kcat is 8 s1 for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius) (PubMed:24237145). kcat is 2.33 s1 for melibiose (at pH 5.0 and 37 degrees Celsius). kcat is 5.0 s1 for raffinose (at pH 5.0 and 37 degrees Celsius). kcat is 0.53 s1 for stachyose (at pH 5.0 and 37 degrees Celsius) (PubMed:25486100).3 Publications
  1. KM=0.075 mM for p-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius)1 Publication
  2. KM=2.100 mM for raffinose (at pH 5.0 and 75 degrees Celsius)1 Publication
  3. KM=0.110 mM for p-nitrophenyl-alpha-D-galactopyranoside (at pH 5.0 and 37 degrees Celsius)1 Publication
  4. KM=1.170 mM for melibiose (at pH 5.0 and 37 degrees Celsius)1 Publication
  5. KM=10.040 mM for raffinose (at pH 5.0 and 37 degrees Celsius)1 Publication
  6. KM=2.840 mM for stachyose (at pH 5.0 and 37 degrees Celsius)1 Publication
  1. Vmax=166 µmol/min/mg enzyme for 4-nitrophenol-alpha-galactoside (at pH 5.0 and 75 degrees Celsius)1 Publication
  2. Vmax=103 µmol/min/mg enzyme for raffinose (at pH 5.0 and 75 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 5.0-5.5 when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside.1 Publication

Temperature dependencei

Optimum temperature is 90-95 degrees Celsius when using synthetic substrate p-nitrophenyl-alpha-D-galactopyranoside. The half-life of thermoinactivation is 6.5 h at 85 degrees Celsius.1 Publication

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 sitei65SubstrateCombined sources1 Publication1
Binding sitei191SubstrateCombined sources1 Publication1
<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 sitei327Nucleophile1 Publication1
Binding sitei368SubstrateCombined sources1 Publication1
Binding sitei383SubstrateCombined sources1 Publication1
Active sitei387Proton donor/acceptor1 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
Biological processCarbohydrate metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
TMAR243274:G1H0Q-1680-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.22, 6331

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH36, Glycoside Hydrolase Family 36

<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:
Alpha-galactosidase1 PublicationImported (EC:3.2.1.226 Publications)
Alternative name(s):
MelibiaseCurated
<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:galA1 PublicationImported
Ordered Locus Names:TM_1192Imported
ORF Names:Tmari_1199Imported
<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>OrganismiThermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)Imported
<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 identifieri243274 [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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
<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
  • UP000013901 <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> Componenti: Chromosome
  • UP000008183 Componenti: Chromosome

<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>Mutagenesisi220D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi220D → G: Reduced activity compared to the wild-type enzyme. 1 Publication1
Mutagenesisi327D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi327D → G: Between 200 and 800-fold lower catalytic rate and between 300 and 1700-fold lower catalytic efficiency than the wild-type enzyme with aryl-alpha-galactosides as substrates. 1 Publication1
Mutagenesisi328F → A: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. Able to produce 16 times more of a regio-isomer with the (alpha1,2)-bond than wild-type enzyme. 1 Publication1
Mutagenesisi385G → L: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. 1 Publication1
Mutagenesisi387D → A: Less than 1% of the wild-type enzyme activity with p-nitrophenyl-alpha-D-galactopyranoside as substrate at 80 degrees Celsius. 1 Publication1
Mutagenesisi387D → G: 1500-fold lower catalytic rate and 1000-fold lower catalytic efficiency than the wild-type enzyme with p-nitrophenyl-alpha-D-galactopyranoside as substrate. 1 Publication1
Mutagenesisi402P → D: Increased transglycosylating activity at high concentrations of p-nitrophenyl-alpha-D-galactopyranoside substrate, which could be useful in industry and medicine for the synthesis of different p-nitrophenyl-digalactosides. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3308963

<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_00004390211 – 552Alpha-galactosidaseAdd BLAST552

<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

Homodimer.

1 Publication

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
243274.THEMA_08370

<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

1552
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
G4FEF4

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

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>Regioni220 – 221Substrate bindingCombined sources1 Publication2
Regioni325 – 327Substrate bindingCombined sources1 Publication3

<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 glycosyl hydrolase 36 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG3345, Bacteria

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
G4FEF4

Identification of Orthologs from Complete Genome Data

More...
OMAi
ILGCGAP

Database of Orthologous Groups

More...
OrthoDBi
469334at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785, Aldolase_TIM
IPR011013, Gal_mutarotase_sf_dom
IPR017853, Glycoside_hydrolase_SF

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445, SSF51445, 1 hit
SSF74650, SSF74650, 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.

G4FEF4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEIFGKTFRE GRFVLKEKNF TVEFAVEKIH LGWKISGRVK GSPGRLEVLR
60 70 80 90 100
TKAPEKVLVN NWQSWGPCRV VDAFSFKPPE IDPNWRYTAS VVPDVLERNL
110 120 130 140 150
QSDYFVAEEG KVYGFLSSKI AHPFFAVEDG ELVAYLEYFD VEFDDFVPLE
160 170 180 190 200
PLVVLEDPNT PLLLEKYAEL VGMENNARVP KHTPTGWCSW YHYFLDLTWE
210 220 230 240 250
ETLKNLKLAK NFPFEVFQID DAYEKDIGDW LVTRGDFPSV EEMAKVIAEN
260 270 280 290 300
GFIPGIWTAP FSVSETSDVF NEHPDWVVKE NGEPKMAYRN WNKKIYALDL
310 320 330 340 350
SKDEVLNWLF DLFSSLRKMG YRYFKIDFLF AGAVPGERKK NITPIQAFRK
360 370 380 390 400
GIETIRKAVG EDSFILGCGS PLLPAVGCVD GMRIGPDTAP FWGEHIEDNG
410 420 430 440 450
APAARWALRN AITRYFMHDR FWLNDPDCLI LREEKTDLTQ KEKELYSYTC
460 470 480 490 500
GVLDNMIIES DDLSLVRDHG KKVLKETLEL LGGRPRVQNI MSEDLRYEIV
510 520 530 540 550
SSGTLSGNVK IVVDLNSREY HLEKEGKSSL KKRVVKREDG RNFYFYEEGE

RE
Length:552
Mass (Da):63,657
Last modified:December 14, 2011 - 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:i91C6E6EFA24EA9D5
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AJ001072 Genomic DNA Translation: CAA04514.1
AE000512 Genomic DNA Translation: AAD36267.1
CP004077 Genomic DNA Translation: AGL50123.1

Protein sequence database of the Protein Information Resource

More...
PIRi
E72283

NCBI Reference Sequences

More...
RefSeqi
NP_228997.1, NC_000853.1
WP_004080136.1, NZ_CP011107.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAD36267; AAD36267; TM_1192
AGL50123; AGL50123; Tmari_1199

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
tma:TM1192
tmm:Tmari_1199
tmw:THMA_1218

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|243274.17.peg.1197

<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
AJ001072 Genomic DNA Translation: CAA04514.1
AE000512 Genomic DNA Translation: AAD36267.1
CP004077 Genomic DNA Translation: AGL50123.1
PIRiE72283
RefSeqiNP_228997.1, NC_000853.1
WP_004080136.1, NZ_CP011107.1

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
1ZY9X-ray2.34A1-552[»]
5M0XX-ray1.80A1-552[»]
5M12X-ray1.53A1-552[»]
5M16X-ray1.62A1-552[»]
5M1IX-ray1.55A1-552[»]
6GTAX-ray2.20A1-552[»]
6GVDX-ray1.22A1-552[»]
6GWFX-ray1.72A1-552[»]
6GWGX-ray1.77A1-552[»]
6GX8X-ray1.42A1-552[»]
SMRiG4FEF4
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi243274.THEMA_08370

Chemistry databases

ChEMBLiCHEMBL3308963

Protein family/group databases

CAZyiGH36, Glycoside Hydrolase Family 36

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
898292

Genome annotation databases

EnsemblBacteriaiAAD36267; AAD36267; TM_1192
AGL50123; AGL50123; Tmari_1199
KEGGitma:TM1192
tmm:Tmari_1199
tmw:THMA_1218
PATRICifig|243274.17.peg.1197

Phylogenomic databases

eggNOGiCOG3345, Bacteria
InParanoidiG4FEF4
OMAiILGCGAP
OrthoDBi469334at2

Enzyme and pathway databases

BioCyciTMAR243274:G1H0Q-1680-MONOMER
BRENDAi3.2.1.22, 6331

Family and domain databases

Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785, Aldolase_TIM
IPR011013, Gal_mutarotase_sf_dom
IPR017853, Glycoside_hydrolase_SF
SUPFAMiSSF51445, SSF51445, 1 hit
SSF74650, SSF74650, 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 nameiAGAL_THEMA
<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: G4FEF4
Secondary accession number(s): O33835
<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 15, 2017
Last sequence update: December 14, 2011
Last modified: June 2, 2021
This is version 71 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, Direct protein sequencing, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  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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