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Entry version 86 (18 Sep 2019)
Sequence version 1 (01 Nov 1996)
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Protein

4-hydroxyphenylacetate 3-monooxygenase oxygenase component

Gene

hpaB

Organism
Escherichia coli
Status
Reviewed-Annotation score:

Annotation score:3 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

Utilizes FADH2 supplied by HpaC or by another flavin reductase, to catalyze the hydroxylation of 4-hydroxyphenylacetic acid, leading to the production of 3,4-DHPA. Can also oxidize phenol to catechol, and hydroxylate other phenol derivatives.1 Publication

Miscellaneous

E.coli K12 lacks the oxygenase component HpaB.

<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 <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 4-hydroxyphenylacetate degradation

This protein is involved in step 1 of the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate.
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. 4-hydroxyphenylacetate 3-monooxygenase oxygenase component (hpaB), 4-hydroxyphenylacetate 3-monooxygenase reductase component (hpaC)
  2. 3,4-dihydroxyphenylacetate 2,3-dioxygenase (hpcB)
  3. 5-carboxymethyl-2-hydroxymuconate semialdehyde dehydrogenase (hpcC)
  4. Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (hpcE), 5-carboxymethyl-2-hydroxymuconate Delta-isomerase (hpcD), 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase (hpaG)
  5. Homoprotocatechuate catabolism bifunctional isomerase/decarboxylase (hpcE), 4-hydroxyphenylacetate degradation bifunctional isomerase/decarboxylase (hpaG)
  6. 2-oxo-hept-4-ene-1,7-dioate hydratase (hpcG)
  7. 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (rhmA_2), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (rhmA), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpcH), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (rhmA), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (rhmA), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI), 4-hydroxy-2-oxo-heptane-1,7-dioate aldolase (hpaI)
This subpathway is part of the pathway 4-hydroxyphenylacetate degradation, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate and succinate semialdehyde from 4-hydroxyphenylacetate, the pathway 4-hydroxyphenylacetate degradation and in Aromatic compound metabolism.

<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 functionMonooxygenase, Oxidoreductase
Biological processAromatic hydrocarbons catabolism
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-2841

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.14.14.9 2026

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00208;UER00416

<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-hydroxyphenylacetate 3-monooxygenase oxygenase component (EC:1.14.14.9)
Alternative name(s):
4-HPA 3-hydroxylase
4-HPA 3-monooxygenase large component
<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:hpaB
<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>OrganismiEscherichia coli
<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 identifieri562 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000840321 – 5204-hydroxyphenylacetate 3-monooxygenase oxygenase componentAdd BLAST520

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
Q57160

<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 reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By 4-hydroxyphenylacetic acid.

<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

4-HPA 3-monooxygenase consists of a reductase component HpaC and an oxygenase component HpaB.

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
481805.EcolC_3710

<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

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SMRi
Q57160

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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105EFA Bacteria
COG2368 LUCA

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036250 AcylCo_DH-like_C
IPR009100 AcylCoA_DH/oxidase_NM_dom
IPR024677 HpaB/PvcC
IPR004925 HpaB/PvcC/4-BUDH
IPR024719 HpaB/PvcC/4-BUDH_C
IPR024674 HpaB/PvcC/4-BUDH_N
IPR012688 HpaB_gammaproteobact

The PANTHER Classification System

More...
PANTHERi
PTHR36117 PTHR36117, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03241 HpaB, 1 hit
PF11794 HpaB_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF500125 4_HPA_large, 1 hit
PIRSF000331 HpaA_HpaB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02310 HpaB-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>. 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.

Q57160-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPEDFRAST QRPFTGEEYL KSLQDGREIY IYGERVKDVT THPAFRNAAA
60 70 80 90 100
SVAQLYDALH KPEMQDSLCW NTDTGSGGYT HKFFRVAKSA DDLRHERDAI
110 120 130 140 150
AEWSRLSYGW MGRTPDYKAA FGCALGGTPG FYGQFEQNAR NWYTRIQETG
160 170 180 190 200
LYFNHAIVNP PIDRHLPTDK VKDVYIKLEK ETDAGIIVSG AKVVATNSAL
210 220 230 240 250
THYNMIGFGS AQVMGENPDF ALMFVAPMDA DGVKLISRAS YEMVAGATGS
260 270 280 290 300
PYDYPLSSRF DENDAILVMD NVLIPWENVL LYRDFDRCRR WTMEGGFARM
310 320 330 340 350
YPLQACVRLA VKLDFITALL KKSLECTGTL EFRGVQADLG EVVAWRNTFW
360 370 380 390 400
ALSDSMCSEA TPWVNGAYLP DHAALQTYRV LAPMAYAKIK NIIERNVTSG
410 420 430 440 450
LIYLPSSARD LNNPQIDQYL AKYVRGSNGM DHVQRIKILK LMWDAIGSEF
460 470 480 490 500
GGRHELYEIN YSGSQDEIRL QCLRQAQSSG NMDKMMAMVD RCLSEYDQNG
510 520
WTVPHLHNND DINMLDKLLK
Length:520
Mass (Da):58,848
Last modified:November 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:i1E93BBCC29BBB55C
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
Z37980 Genomic DNA Translation: CAA86048.1
Z29081 Genomic DNA Translation: CAA82321.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B55349

<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
Z37980 Genomic DNA Translation: CAA86048.1
Z29081 Genomic DNA Translation: CAA82321.1
PIRiB55349

3D structure databases

SMRiQ57160
ModBaseiSearch...

Protein-protein interaction databases

STRINGi481805.EcolC_3710

Proteomic databases

PRIDEiQ57160

Phylogenomic databases

eggNOGiENOG4105EFA Bacteria
COG2368 LUCA

Enzyme and pathway databases

UniPathwayiUPA00208;UER00416
BioCyciMetaCyc:MONOMER-2841
BRENDAi1.14.14.9 2026

Family and domain databases

InterProiView protein in InterPro
IPR036250 AcylCo_DH-like_C
IPR009100 AcylCoA_DH/oxidase_NM_dom
IPR024677 HpaB/PvcC
IPR004925 HpaB/PvcC/4-BUDH
IPR024719 HpaB/PvcC/4-BUDH_C
IPR024674 HpaB/PvcC/4-BUDH_N
IPR012688 HpaB_gammaproteobact
PANTHERiPTHR36117 PTHR36117, 1 hit
PfamiView protein in Pfam
PF03241 HpaB, 1 hit
PF11794 HpaB_N, 1 hit
PIRSFiPIRSF500125 4_HPA_large, 1 hit
PIRSF000331 HpaA_HpaB, 1 hit
SUPFAMiSSF47203 SSF47203, 1 hit
SSF56645 SSF56645, 1 hit
TIGRFAMsiTIGR02310 HpaB-2, 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 nameiHPAB_ECOLX
<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: Q57160
<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: May 2, 2002
Last sequence update: November 1, 1996
Last modified: September 18, 2019
This is version 86 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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