Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 48 (07 Apr 2021)
Sequence version 1 (22 Nov 2005)
Previous versions | rss
Add a publicationFeedback
Protein

4-hydroxyphenylacetate decarboxylase glycyl radical subunit

Gene

csdB

Organism
Clostridium scatologenes
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

Glycyl radical subunit of the HPA decarboxylase that decarboxylates phenylacetates with a hydroxyl group in the p-position. Active toward 4-hydroxyphenylacetate and 3,4-dihydroxyphenylacetate, forming 4-methylphenol and 4-methylcatechol, respectively. Is likely involved in the catabolism of aromatic amino acids such as tyrosine fermentation. 4-methylphenol (p-cresol) formation provides metabolic toxicity, which allows an active suppression of other microbes and may provide growth advantages for the producers in highly competitive environments (PubMed:16878993). The large subunit is the catalytic subunit that binds the substrate (PubMed:21823587).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 '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 135 sec(-1) for the decarboxylation of 4-hydroxyphenylacetate. kcat is 67 sec(-1) for the decarboxylation of 3,4-hydroxyphenylacetate.1 Publication
  1. KM=358 µM for 4-hydroxyphenylacetate1 Publication
  2. KM=388 µM for 3,4-dihydroxyphenylacetate1 Publication
  1. Vmax=18.45 µmol/min/mg enzyme for the decarboxylation of 4-hydroxyphenylacetate1 Publication
  2. Vmax=9.12 µmol/min/mg enzyme for the decarboxylation of 3,4-hydroxyphenylacetate1 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 sitei3444-hydroxyphenylacetateCombined 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 sitei503Cysteine radical intermediate1 Publication1
Binding sitei5034-hydroxyphenylacetateCombined sources1 Publication1
Active sitei505Proton donor1 Publication1
Binding sitei5364-hydroxyphenylacetateCombined sources1 Publication1
Binding sitei6374-hydroxyphenylacetateCombined 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

<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 functionLyase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.83, 9686

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q38HX4

<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:
4-hydroxyphenylacetate decarboxylase glycyl radical subunit1 Publication (EC:4.1.1.831 Publication)
Short name:
HPA decarboxylase glycyl radical subunit
Alternative name(s):
4-hydroxyphenylacetate decarboxylase catalytic beta subunit1 Publication
4-hydroxyphenylacetate decarboxylase large subunitImported
p-hydroxyphenylacetate decarboxylase large subunitBy similarity
<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:csdBImported
<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>OrganismiClostridium scatologenes
<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 identifieri1548 [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 lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

<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_00004036911 – 8974-hydroxyphenylacetate decarboxylase glycyl radical subunitAdd BLAST897

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei873Glycine radicalPROSITE-ProRule annotation1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Requires the activating protein CsdA to generate the key active site glycyl radical that is involved in catalysis.1 Publication
Phosphorylated on serine. Phosphorylation may trigger the formation of the active heterooctamers and thereby regulates enzyme activity.1 Publication

Keywords - PTMi

Organic radical, Phosphoprotein

<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

Heterooctamer consisting of 4 large (HpdB) subunits and 4 small (HpdC) subunits, arranged as a tetramer of heterodimers (PubMed:16878993, PubMed:21823587). Also forms a catalytically inactive homodimer (PubMed:16878993).

2 Publications

<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

1897
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
Q38HX4

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini35 – 770PFLPROSITE-ProRule annotationAdd BLAST736
Domaini778 – 897Glycine radicalPROSITE-ProRule annotationAdd BLAST120

<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

Database of Orthologous Groups

More...
OrthoDBi
116406at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001150, Gly_radical
IPR004184, PFL_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01228, Gly_radical, 1 hit
PF02901, PFL-like, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51149, GLY_RADICAL_2, 1 hit
PS51554, PFL, 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.

Q38HX4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNVKETKLED VLKSRGIDMK DAYNISEADI PEAKESTQKL MDIYYTLKVT
60 70 80 90 100
ADMEAAYWYN RTWWENDGEV IEVRRAKAVA ASLSHMTPTI LPYEKLVMNK
110 120 130 140 150
TKNVRGAFPF PWVCASFFNA QAEALMNEVD APAENEADSV SVVGAGGGNV
160 170 180 190 200
TESYGNVISI AKKFGMRKEE IPVLVKTSKP WEGISVEELS NKYSKMTPGY
210 220 230 240 250
DQFKNIMESV ICMFDSFAIP QGREVINYYM PLQYGFDGII KLCDEKIAEV
260 270 280 290 300
MGEAGDDGDF GMSRGYYYAA MKEITKGLSA WCENYSKRAK YLASIETDSE
310 320 330 340 350
IKANYEKIEE VMGNIAHKKP ANFWEAIQMT LCCHFGVVNE DPQSGLSIGR
360 370 380 390 400
LGQVLQPFYE KDVEDGIMTD EEVIELLELY RIKITCIECF ASAGVSGGVL
410 420 430 440 450
SGNTFNNLSL GGQNYDGLSA VTPLEYLIVE AGMRNQTPQP TLSVLYDEKT
460 470 480 490 500
PEDFLMKAAS CTKLGLGYPA WMNNQTGMNF MMRNYGPEGM DLHDARAWCL
510 520 530 540 550
GGCLESAPGC FLPLEYNGKV TMIPGGASPT CGTGVHFIGM PKVLELVLTN
560 570 580 590 600
GLDKRTGKQV YPPHNKKLDS YETMVNQWKE YMELTTDVVN RCNNIQMDIW
610 620 630 640 650
RKYNMPAVNS LLKPDCFKKG KHIGTMGARY NSCINFESCG TITFVNSLSS
660 670 680 690 700
IKKNVFDDSK FTIEEMTDAM LNNFGFKTAY ETEVFSPDFR ESTDKSTKYE
710 720 730 740 750
KIFAACVNAP KYGNADKYAD EIFKAYHYYI YDMTHKFRSY YGKPLYLCQI
760 770 780 790 800
SVSTHGPQGF VTLATADGRL AGTTYSDGSV SAAAGTDKNG IYAIFESATV
810 820 830 840 850
YDHSMHQNAQ MNLKLHPTAV KGINGTRKLL DLVRAYMRKG GFHVQFNVVD
860 870 880 890
SKTLRDAQLT PEKYRELMVR VAGFTQYWCE IGKPIQDEVI YRTEYDK
Length:897
Mass (Da):100,637
Last modified:November 22, 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:iDF8FC6541E459550
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
DQ227741 Genomic DNA Translation: ABB05046.1

NCBI Reference Sequences

More...
RefSeqi
WP_029163539.1, NZ_CP009933.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ227741 Genomic DNA Translation: ABB05046.1
RefSeqiWP_029163539.1, NZ_CP009933.1

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
2Y8NX-ray1.75A/C1-897[»]
2YAJX-ray1.81A/C1-897[»]
SMRiQ38HX4
ModBaseiSearch...
PDBe-KBiSearch...

Phylogenomic databases

OrthoDBi116406at2

Enzyme and pathway databases

BRENDAi4.1.1.83, 9686
SABIO-RKiQ38HX4

Family and domain databases

InterProiView protein in InterPro
IPR001150, Gly_radical
IPR004184, PFL_dom
PfamiView protein in Pfam
PF01228, Gly_radical, 1 hit
PF02901, PFL-like, 1 hit
PROSITEiView protein in PROSITE
PS51149, GLY_RADICAL_2, 1 hit
PS51554, PFL, 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 nameiHPDL_CLOSL
<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: Q38HX4
<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: January 11, 2011
Last sequence update: November 22, 2005
Last modified: April 7, 2021
This is version 48 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again