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Entry version 89 (07 Oct 2020)
Sequence version 1 (13 Sep 2005)
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Protein

3-hydroxylaminophenol mutase

Gene

Reut_A2057

Organism
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134))
Status
Reviewed-Annotation score:

Annotation score:4 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 isomerization of 3-hydroxylaminophenol (3HAP) to aminohydroquinone, a step in the degradative pathway of 3-nitrophenol. The enzymatic reaction is regiospecific since it leads to the formation of aminohydroquinone exclusively, without producing the isomeric 4-aminocatechol. Can also isomerize other hydroxylaminoaromatic compounds, such as hydroxylaminobenzene to a mixture of 2-aminophenol and 4-aminophenol, 4-hydroxylaminotoluene to 6-amino-m-cresol, and 2-chloro-5-hydroxylaminophenol to 2-amino-5-chlorohydroquinone. Does not act on 4-hydroxylaminobenzoate.1 Publication

Miscellaneous

3HAP mutase requires neither a cofactor nor oxygen for the enzymatic reaction. This indicates that the enzyme catalyzes a Bamberger-type rearrangement.

<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

Is inhibited by H2O2. 1,10-phenanthroline inhibits the activity slightly, but other metal cation chelators such as EDTA or tiron have no effect on the activity. Divalent metal cations and hydroxylamine have also no effect on the activity. Due to the relationship of the protein with glutamine synthetases, glutamate and glutamine were tested as inhibitors; neither preincubation of the compounds with the enzyme nor their addition to the assay buffer affected 3HAP mutase activity.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

The values are approximate data due to the instability of the substrate.
  1. KM=0.1 mM for 3-hydroxyaminophenol1 Publication
  1. Vmax=4.8 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 6.5.1 Publication

Temperature dependencei

Optimum temperature is above 30 degrees Celsius. Heating to 60 degrees Celsius for 1 minute abolishes 72% of the original mutase activity, and no activity remains after 8 minutes.1 Publication

<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

  • 3-(hydroxyamino)phenol mutase activity Source: UniProtKB
  • glutamate-ammonia ligase activity Source: InterPro

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 functionIsomerase

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-15839

<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:
3-hydroxylaminophenol mutase (EC:5.4.4.3)
Short name:
3HAP mutase
Alternative name(s):
3-(hydroxyamino)phenol mutase
<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
Ordered Locus Names:Reut_A2057
<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>OrganismiCupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134))
<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 identifieri264198 [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 lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
<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
  • UP000002697 <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 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00004186462 – 4713-hydroxylaminophenol mutaseAdd BLAST470

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q46ZL2

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
264198.Reut_A2057

<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

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

More...
SMRi
Q46ZL2

Database of comparative protein structure models

More...
ModBasei
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

<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 glutamine synthetase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0174, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_017290_1_2_4

KEGG Orthology (KO)

More...
KOi
K20712

Identification of Orthologs from Complete Genome Data

More...
OMAi
PHPHEFE

Database of Orthologous Groups

More...
OrthoDBi
416474at2

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.10.20.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR008147, Gln_synt_b-grasp
IPR036651, Gln_synt_N
IPR014746, Gln_synth/guanido_kin_cat_dom
IPR008146, Gln_synth_cat_dom
IPR027303, Gln_synth_gly_rich_site
IPR004809, Gln_synth_I
IPR001637, Gln_synth_I_adenylation_site
IPR027302, Gln_synth_N_conserv_site

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00120, Gln-synt_C, 1 hit
PF03951, Gln-synt_N, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM01230, Gln-synt_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54368, SSF54368, 1 hit
SSF55931, SSF55931, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00653, GlnA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00180, GLNA_1, 1 hit
PS00182, GLNA_ADENYLATION, 1 hit
PS00181, GLNA_ATP, 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.

Q46ZL2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAQSVADVMK LVKENDVKFV DFRFTDTKGK EQHVSVPTSH FDDDKFESGH
60 70 80 90 100
AFDGSSIAGW KGIEASDMLL MPDSNTAFID PFYEEPTLVL TCDVVEPSDG
110 120 130 140 150
KGYDRDPRSI AKRAEAYLKS TGLGDTAFFG PEPEFFIFDG VTWNVDMQGC
160 170 180 190 200
FVKVHSEEAP WSSGKEFEHG NSGHRPGKKG GYFPVAPIDT FQDMRSEMCL
210 220 230 240 250
ILESLGIPVE VHHHEVAGQG QNEIGTRFST LVQRADWTQL QKYVIQNVAH
260 270 280 290 300
TYGKTATFMP KPIVGDNGSG MHVHQSVWKD GQNLFAGNGY AGLSEFALYY
310 320 330 340 350
IGGIIKHARA LNAITNPGTN SYKRLVPGFE APVKLAYSAR NRSASIRIPY
360 370 380 390 400
VANPKGRRIE TRFPDPLMNP YLGFSALLMA GLDGVMNKIH PGEAADKNLY
410 420 430 440 450
DLPPEEDAKI PTVCNSLDQS LEYLDNDREF LTRGGVFSNS MLDAYIELKM
460 470
EEVTRFRMTT HPVEFEMYYS L
Length:471
Mass (Da):52,494
Last modified:September 13, 2005 - 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:i8B3B55E47D7857F1
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000090 Genomic DNA Translation: AAZ61421.1

NCBI Reference Sequences

More...
RefSeqi
WP_011298219.1, NC_007347.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAZ61421; AAZ61421; Reut_A2057

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
reu:Reut_A2057

<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
CP000090 Genomic DNA Translation: AAZ61421.1
RefSeqiWP_011298219.1, NC_007347.1

3D structure databases

SMRiQ46ZL2
ModBaseiSearch...

Protein-protein interaction databases

STRINGi264198.Reut_A2057

Proteomic databases

PRIDEiQ46ZL2

Genome annotation databases

EnsemblBacteriaiAAZ61421; AAZ61421; Reut_A2057
KEGGireu:Reut_A2057

Phylogenomic databases

eggNOGiCOG0174, Bacteria
HOGENOMiCLU_017290_1_2_4
KOiK20712
OMAiPHPHEFE
OrthoDBi416474at2

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15839

Family and domain databases

Gene3Di3.10.20.70, 1 hit
InterProiView protein in InterPro
IPR008147, Gln_synt_b-grasp
IPR036651, Gln_synt_N
IPR014746, Gln_synth/guanido_kin_cat_dom
IPR008146, Gln_synth_cat_dom
IPR027303, Gln_synth_gly_rich_site
IPR004809, Gln_synth_I
IPR001637, Gln_synth_I_adenylation_site
IPR027302, Gln_synth_N_conserv_site
PfamiView protein in Pfam
PF00120, Gln-synt_C, 1 hit
PF03951, Gln-synt_N, 1 hit
SMARTiView protein in SMART
SM01230, Gln-synt_C, 1 hit
SUPFAMiSSF54368, SSF54368, 1 hit
SSF55931, SSF55931, 1 hit
TIGRFAMsiTIGR00653, GlnA, 1 hit
PROSITEiView protein in PROSITE
PS00180, GLNA_1, 1 hit
PS00182, GLNA_ADENYLATION, 1 hit
PS00181, GLNA_ATP, 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 namei3HAPM_CUPPJ
<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: Q46ZL2
<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: September 5, 2012
Last sequence update: September 13, 2005
Last modified: October 7, 2020
This is version 89 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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