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Entry version 127 (23 Feb 2022)
Sequence version 1 (20 Dec 2005)
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Protein

7alpha-hydroxysteroid dehydrogenase

Gene

hdhA

Organism
Escherichia coli (strain K12)
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

7alpha-hydroxysteroid dehydrogenase involved in the metabolism of bile acids. Catalyzes the NAD+-dependent oxidation of the 7alpha-hydroxy group of 7alpha-hydroxysteroids, such as the major human bile acids cholate and chenodeoxycholate, to the corresponding 7-oxosteroids. To a lesser extent, can also act on taurochenodeoxycholate, taurocholate and glycocholate (PubMed:2007545).

Can also use glycochenodeoxycholate as substrate (PubMed:8672472).

Is not able to use NADP+ instead of NAD+ as the electron acceptor (PubMed:2007545).

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 N-bromosuccinimide, diethyl pyrocarbonate, and some metal ions such as Co2+, Fe2+ and Cu2+.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

kcat is 3798 sec(-1) with cholate as substrate (PubMed:2007545). kcat is 491 sec(-1) with chenodeoxycholate as substrate (PubMed:2007545). kcat is 206 sec(-1) with taurochenodeoxycholate as substrate (PubMed:2007545). kcat is 188 sec(-1) with taurocholate as substrate (PubMed:2007545). kcat is 25 sec(-1) with glycocholate as substrate (PubMed:2007545). kcat is 151 sec(-1) with cholate as substrate (PubMed:9722677).2 Publications
  1. KM=0.19 mM for taurochenodeoxycholate1 Publication
  2. KM=0.43 mM for chenodeoxycholate1 Publication
  3. KM=1.2 mM for cholate1 Publication
  4. KM=1.25 mM for glycocholate1 Publication
  5. KM=2.0 mM for taurocholate1 Publication
  6. KM=0.279 mM for NAD+1 Publication
  7. KM=0.361 mM for cholate1 Publication

pH dependencei

Optimum pH is 8.5 (PubMed:2007545). The enzyme is stable between pH 8 and 9 (PubMed:2007545).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 sitei23NAD; via amide nitrogenCombined sources1 Publication1
Binding sitei95NAD; via carbonyl oxygenCombined sources1 Publication1
Binding sitei99Glycochenodeoxycholate; via amide nitrogenCombined sources1 Publication1
Binding sitei146GlycochenodeoxycholateCombined sources1 Publication1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei146Transition state stabilizer2 Publications1
Binding sitei151GlycochenodeoxycholateCombined 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 sitei159Proton acceptor2 Publications1
Binding sitei159GlycochenodeoxycholateCombined sources1 Publication1
Binding sitei159NADCombined sources1 Publication1
Binding sitei163NADCombined sources1 Publication1
Sitei163Lowers pKa of active site Tyr2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi42 – 43NADCombined sources1 Publication2
Nucleotide bindingi68 – 69NADCombined sources1 Publication2
Nucleotide bindingi192 – 194NADCombined sources1 Publication3

<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 functionOxidoreductase
Biological processBile acid catabolism, Lipid degradation, Lipid metabolism, Steroid metabolism
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.159, 2026

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001736

<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:
7alpha-hydroxysteroid dehydrogenase1 Publication (EC:1.1.1.1592 Publications)
Short name:
7alpha-HSDH1 Publication
Alternative name(s):
NAD-dependent 7alpha-hydroxysteroid dehydrogenase1 Publication
<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:hdhA
Synonyms:hsdH1 Publication
Ordered Locus Names:b1619, JW1611
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<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
  • UP000000318 <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
  • UP000000625 Componenti: Chromosome

<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

<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>Mutagenesisi146S → A or H: Reduction of the catalytic efficiency by over 65%. No effect on the affinity for cholate and NAD. 1 Publication1
Mutagenesisi159Y → F: Loss of activity. 1 Publication1
Mutagenesisi159Y → H: Reduction of the catalytic efficiency by 87.7%. No effect on the affinity for cholate and NAD. 1 Publication1
Mutagenesisi163K → I: Reduction of the catalytic efficiency by 95%. No effect on the affinity for cholate and NAD. 1 Publication1
Mutagenesisi163K → R: Reduction of the catalytic efficiency by 35%. No effect on the affinity for cholate and NAD. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02123, Glycochenodeoxycholic Acid

<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_00000547081 – 2557alpha-hydroxysteroid dehydrogenaseAdd BLAST255

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AET8

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

More...
PaxDbi
P0AET8

PRoteomics IDEntifications database

More...
PRIDEi
P0AET8

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0AET8

<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

Homotetramer.

2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4259598, 31 interactors

Database of interacting proteins

More...
DIPi
DIP-9875N

Protein interaction database and analysis system

More...
IntActi
P0AET8, 5 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b1619

<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

1255
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
P0AET8

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0AET8

<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
COG1028, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010194_1_3_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AET8

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AET8

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00081, GDHRDH
PR00080, SDRFAMILY

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735, SSF51735, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00061, ADH_SHORT, 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.

P0AET8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNSDNLRLD GKCAIITGAG AGIGKEIAIT FATAGASVVV SDINADAANH
60 70 80 90 100
VVDEIQQLGG QAFACRCDIT SEQELSALAD FAISKLGKVD ILVNNAGGGG
110 120 130 140 150
PKPFDMPMAD FRRAYELNVF SFFHLSQLVA PEMEKNGGGV ILTITSMAAE
160 170 180 190 200
NKNINMTSYA SSKAAASHLV RNMAFDLGEK NIRVNGIAPG AILTDALKSV
210 220 230 240 250
ITPEIEQKML QHTPIRRLGQ PQDIANAALF LCSPAASWVS GQILTVSGGG

VQELN
Length:255
Mass (Da):26,779
Last modified:December 20, 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:i66CF70E85BD67B6D
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
D10497 Genomic DNA Translation: BAA01384.1
U00096 Genomic DNA Translation: AAC74691.1
AP009048 Genomic DNA Translation: BAA15370.1
M14641 Genomic DNA Translation: AAA68921.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A38527

NCBI Reference Sequences

More...
RefSeqi
NP_416136.1, NC_000913.3
WP_000483353.1, NZ_STEB01000003.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74691; AAC74691; b1619
BAA15370; BAA15370; BAA15370

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946151

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ag:BAA01384
ecj:JW1611
eco:b1619

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.642

<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
D10497 Genomic DNA Translation: BAA01384.1
U00096 Genomic DNA Translation: AAC74691.1
AP009048 Genomic DNA Translation: BAA15370.1
M14641 Genomic DNA Translation: AAA68921.1
PIRiA38527
RefSeqiNP_416136.1, NC_000913.3
WP_000483353.1, NZ_STEB01000003.1

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
1AHHX-ray2.30A/B1-255[»]
1AHIX-ray2.30A/B1-255[»]
1FMCX-ray1.80A/B1-255[»]
7ENYX-ray2.70A/B/C/D/E/F/G/H1-255[»]
SMRiP0AET8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4259598, 31 interactors
DIPiDIP-9875N
IntActiP0AET8, 5 interactors
STRINGi511145.b1619

Chemistry databases

DrugBankiDB02123, Glycochenodeoxycholic Acid
SwissLipidsiSLP:000001736

2D gel databases

SWISS-2DPAGEiP0AET8

Proteomic databases

jPOSTiP0AET8
PaxDbiP0AET8
PRIDEiP0AET8

Genome annotation databases

EnsemblBacteriaiAAC74691; AAC74691; b1619
BAA15370; BAA15370; BAA15370
GeneIDi946151
KEGGiag:BAA01384
ecj:JW1611
eco:b1619
PATRICifig|1411691.4.peg.642

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0420

Phylogenomic databases

eggNOGiCOG1028, Bacteria
HOGENOMiCLU_010194_1_3_6
InParanoidiP0AET8
PhylomeDBiP0AET8

Enzyme and pathway databases

BioCyciEcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER
BRENDAi1.1.1.159, 2026

Miscellaneous databases

EvolutionaryTraceiP0AET8

Protein Ontology

More...
PROi
PR:P0AET8

Family and domain databases

InterProiView protein in InterPro
IPR036291, NAD(P)-bd_dom_sf
IPR020904, Sc_DH/Rdtase_CS
IPR002347, SDR_fam
PRINTSiPR00081, GDHRDH
PR00080, SDRFAMILY
SUPFAMiSSF51735, SSF51735, 1 hit
PROSITEiView protein in PROSITE
PS00061, ADH_SHORT, 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 nameiHDHA_ECOLI
<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: P0AET8
Secondary accession number(s): P25529
<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: December 20, 2005
Last sequence update: December 20, 2005
Last modified: February 23, 2022
This is version 127 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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