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Protein

4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic

Gene

GLU1

Organism
Zea mays (Maize)
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

Is implicated in many functions such as ABA metabolism, hydrolysis of conjugated gibberellins, conversion of storage forms of cytokinins to active forms. Also acts in defense of young plant parts against pests via the production of hydroxamic acids from hydroxamic acid glucosides. Enzymatic activity is highly correlated with plant growth. The preferred substrate is DIMBOA-beta-D-glucoside. Hydrolyzes the chromogenic substrate 6-bromo-2-naphthyl-beta-D-glucoside (6BNGlc) and various artificial aryl beta-glucosides. No activity with cellobiose, arbutin, gentiobiose, linamarin or dhurrin as substrates.3 Publications

<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

  • Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose. EC:3.2.1.21

<p>This subsection of the ‘Function’ 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

Reversibly inhibited by micromolar concentrations of Hg2+ or Ag+, but irreversibly inhibited by alkylation in presence of urea. Competitive inhibition by p-nitrophenyl beta-D-thioglucoside (pNPTGlc), glucotetrazole, and para-hydroxy-S-mandelonitrile beta-glucoside (dhurrin).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

  1. KM=0.14 mM for 4-methylumbelliferyl beta-D-glucopyranoside (MUG)5 Publications
  2. KM=0.64 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG)5 Publications
  3. KM=0.41 mM for p-nitrophenyl beta-D-glucopyranoside (PNPG) (with recombinant enzyme)5 Publications
  4. KM=98 µM for DIMBOA-beta-D-glucoside5 Publications
  5. KM=0.251 mM for n-octyl-beta-D-glucopyranoside5 Publications
  6. KM=0.394 mM for p-nitrophenyl beta-D-xyloside5 Publications
  7. KM=0.648 mM for p-nitrophenyl beta-D-fucopyranoside5 Publications
  8. KM=0.674 mM for p-nitrophenyl beta-D-cellobioside5 Publications
  9. KM=0.769 mM for p-nitrophenyl beta-D-mannopyranoside5 Publications
  10. KM=1.64 mM for o-nitrophenyl beta-D-glucopyranoside5 Publications
  11. KM=1.42 mM for o-nitrophenyl beta-D-glucopyranoside (with recombinant enzyme)5 Publications
  12. KM=4.32 mM for p-nitrophenyl beta-D-galactopyranoside5 Publications
  1. Vmax=225.4 µmol/h/µg enzyme with p-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)5 Publications
  2. Vmax=282.7 µmol/h/µg enzyme with o-nitrophenyl beta-D-glucopyranoside as substrate (with recombinant enzyme)5 Publications

pH dependencei

Optimum pH is 5.8.5 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius. Loses activity when is heated at 55 degrees Celsius.5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei92SubstrateCombined sources2 Publications1
Binding sitei196SubstrateCombined sources1 Publication1
Binding sitei244SubstrateCombined sources1 Publication1
<p>This subsection of the ‘Function’ 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 sitei245Proton donorBy similarity1
Binding sitei387SubstrateCombined sources1 Publication1
Active sitei460NucleophileBy similarity1
Binding sitei511SubstrateCombined sources2 Publications1
Binding sitei527SubstrateCombined 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
Biological processCytokinin signaling pathway

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-10621

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.2.1.182 6752
3.2.1.21 6752

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P49235

Protein family/group databases

Carbohydrate-Active enZymes

More...
CAZyi
GH1 Glycoside Hydrolase Family 1

<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:
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplastic (EC:3.2.1.182)
Alternative name(s):
Beta-D-glucoside glucohydrolase
Beta-glucosidase 1 (EC:3.2.1.21)
Short name:
ZmGlu1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:GLU1
<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>OrganismiZea mays (Maize)
<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 identifieri4577 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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
  • UP000007305 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">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 10

Organism-specific databases

Maize Genetics and Genomics Database

More...
MaizeGDBi
13870

<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 Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

<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_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>Mutagenesisi245E → D or Q: Loss of activity. 3 Publications1
Mutagenesisi252F → I, W or Y: Reduced substrate affinity. 1 Publication1
Mutagenesisi264C → A, D, R or S: Loss of activity due to impaired dimerization. 1
Mutagenesisi270C → A, D, R or S: Loss of activity due to impaired dimerization. 1
Mutagenesisi317M → F, I or V: No effect. 1 Publication1
Mutagenesisi460E → D: Loss of activity and impaired dimerization. 1 Publication1
Mutagenesisi460E → Q: Loss of activity. 1 Publication1
Mutagenesisi463I → D: Loss of activity due to impaired dimerization. 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 describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 54Chloroplast2 PublicationsAdd BLAST54
<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_000001176355 – 5664-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase 1, chloroplasticAdd BLAST512

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 bondi264 ↔ 2703 Publications

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P49235

PRoteomics IDEntifications database

More...
PRIDEi
P49235

Protein Mass spectra EXtraction

More...
ProMEXi
P49235

<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 all seedling parts. Most abundant in the coleoptile.1 Publication

Gene expression databases

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P49235 baseline and differential

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homo- and heterodimer.6 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
4577.GRMZM2G016890_P01

<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

1566
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P49235

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

More...
SMRi
P49235

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P49235

<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>Regioni325 – 361DimerizationAdd BLAST37
Regioni394 – 405DimerizationAdd BLAST12
Regioni450 – 453Dimerization4
Regioni518 – 519Substrate bindingCombined sources2 Publications2

<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 1 family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0626 Eukaryota
COG2723 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000088630

KEGG Orthology (KO)

More...
KOi
K01188

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001360 Glyco_hydro_1
IPR018120 Glyco_hydro_1_AS
IPR033132 Glyco_hydro_1_N_CS
IPR017853 Glycoside_hydrolase_SF

The PANTHER Classification System

More...
PANTHERi
PTHR10353 PTHR10353, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00232 Glyco_hydro_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00131 GLHYDRLASE1

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51445 SSF51445, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00572 GLYCOSYL_HYDROL_F1_1, 1 hit
PS00653 GLYCOSYL_HYDROL_F1_2, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

P49235-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPLLAAAMN HAAAHPGLRS HLVGPNNESF SRHHLPSSSP QSSKRRCNLS
60 70 80 90 100
FTTRSARVGS QNGVQMLSPS EIPQRDWFPS DFTFGAATSA YQIEGAWNED
110 120 130 140 150
GKGESNWDHF CHNHPERILD GSNSDIGANS YHMYKTDVRL LKEMGMDAYR
160 170 180 190 200
FSISWPRILP KGTKEGGINP DGIKYYRNLI NLLLENGIEP YVTIFHWDVP
210 220 230 240 250
QALEEKYGGF LDKSHKSIVE DYTYFAKVCF DNFGDKVKNW LTFNEPQTFT
260 270 280 290 300
SFSYGTGVFA PGRCSPGLDC AYPTGNSLVE PYTAGHNILL AHAEAVDLYN
310 320 330 340 350
KHYKRDDTRI GLAFDVMGRV PYGTSFLDKQ AEERSWDINL GWFLEPVVRG
360 370 380 390 400
DYPFSMRSLA RERLPFFKDE QKEKLAGSYN MLGLNYYTSR FSKNIDISPN
410 420 430 440 450
YSPVLNTDDA YASQEVNGPD GKPIGPPMGN PWIYMYPEGL KDLLMIMKNK
460 470 480 490 500
YGNPPIYITE NGIGDVDTKE TPLPMEAALN DYKRLDYIQR HIATLKESID
510 520 530 540 550
LGSNVQGYFA WSLLDNFEWF AGFTERYGIV YVDRNNNCTR YMKESAKWLK
560
EFNTAKKPSK KILTPA
Length:566
Mass (Da):64,237
Last modified:February 1, 1996 - 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:i4EA241258AE3641B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1D6IX61A0A1D6IX61_MAIZE
Beta-glucosidase, chloroplastic
542414 ZEAMMB73_Zm00001d023994
248Annotation score:

Annotation score:1 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>
A0A1D6IX59A0A1D6IX59_MAIZE
Beta-glucosidase, chloroplastic
542414 ZEAMMB73_Zm00001d023994
463Annotation score:

Annotation score:1 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 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 conflicti477A → D in CAA52293 (PubMed:8235622).Curated1
Sequence conflicti551E → Q in CAA52293 (PubMed:8235622).Curated1
Sequence conflicti554T → A in CAA52293 (PubMed:8235622).Curated1

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
U25157 mRNA Translation: AAA65946.1
X74217 mRNA Translation: CAA52293.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A48860

NCBI Reference Sequences

More...
RefSeqi
NP_001105454.1, NM_001111984.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Zm.94498

Genome annotation databases

Ensembl plant genome annotation project

More...
EnsemblPlantsi
Zm00001d023994_T002; Zm00001d023994_P002; Zm00001d023994

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
542414

Gramene; a comparative resource for plants

More...
Gramenei
Zm00001d023994_T002; Zm00001d023994_P002; Zm00001d023994

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
zma:542414

<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
U25157 mRNA Translation: AAA65946.1
X74217 mRNA Translation: CAA52293.1
PIRiA48860
RefSeqiNP_001105454.1, NM_001111984.1
UniGeneiZm.94498

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
1E1EX-ray2.50A/B55-566[»]
1E1FX-ray2.60A/B55-566[»]
1E4LX-ray2.20A/B55-566[»]
1E4NX-ray2.10A/B55-566[»]
1E55X-ray2.00A/B55-566[»]
1E56X-ray2.10A/B55-566[»]
1H49X-ray1.90A/B55-566[»]
1HXJX-ray2.05A/B60-566[»]
1V08X-ray1.90A/B55-566[»]
ProteinModelPortaliP49235
SMRiP49235
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4577.GRMZM2G016890_P01

Protein family/group databases

CAZyiGH1 Glycoside Hydrolase Family 1

Proteomic databases

PaxDbiP49235
PRIDEiP49235
ProMEXiP49235

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiZm00001d023994_T002; Zm00001d023994_P002; Zm00001d023994
GeneIDi542414
GrameneiZm00001d023994_T002; Zm00001d023994_P002; Zm00001d023994
KEGGizma:542414

Organism-specific databases

MaizeGDBi13870

Phylogenomic databases

eggNOGiKOG0626 Eukaryota
COG2723 LUCA
HOGENOMiHOG000088630
KOiK01188

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-10621
BRENDAi3.2.1.182 6752
3.2.1.21 6752
SABIO-RKiP49235

Miscellaneous databases

EvolutionaryTraceiP49235

Gene expression databases

ExpressionAtlasiP49235 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR001360 Glyco_hydro_1
IPR018120 Glyco_hydro_1_AS
IPR033132 Glyco_hydro_1_N_CS
IPR017853 Glycoside_hydrolase_SF
PANTHERiPTHR10353 PTHR10353, 1 hit
PfamiView protein in Pfam
PF00232 Glyco_hydro_1, 1 hit
PRINTSiPR00131 GLHYDRLASE1
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00572 GLYCOSYL_HYDROL_F1_1, 1 hit
PS00653 GLYCOSYL_HYDROL_F1_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiHGGL1_MAIZE
<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: P49235
<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: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 126 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
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