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UniProtKB - P0AET8 (HDHA_ECOLI)

Entry version 120 (17 Jun 2020)
Sequence version 1 (20 Dec 2005)
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Protein

7-alpha-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

Catalyzes the oxidation of the 7-alpha-hydroxy group of primary bile acids such as cholate, chenodeoxycholate and taurochenodeoxycholate (PubMed:2007545, PubMed:9722677). To a lesser extent, also able to use taurocholate and glycocholate (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) for cholate as substrate (PubMed:2007545). Kcat is 491 sec(-1) for chenodeoxycholate as substrate (PubMed:2007545). Kcat is 206 sec(-1) for taurochenodeoxycholate as substrate (PubMed:2007545). Kcat is 188 sec(-1) for taurocholate as substrate (PubMed:2007545). Kcat is 151 sec(-1) for cholate as substrate (PubMed:9722677). Kcat is 25 sec(-1) for glycocholate as substrate (PubMed:2007545).2 Publications
  1. KM=0.19 mM for taurochenodeoxycholate1 Publication
  2. KM=0.279 mM for NAD1 Publication
  3. KM=0.361 mM for cholate1 Publication
  4. KM=0.43 mM for chenodeoxycholate1 Publication
  5. KM=1.2 mM for cholate1 Publication
  6. KM=1.25 mM for glycocholate1 Publication
  7. KM=2 mM for taurocholate1 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 sitei95NAD; via carbonyl oxygenCombined sources1 Publication1
    Binding sitei99Substrate; via amide nitrogenCombined sources1 Publication1
    Binding sitei146SubstrateCombined sources1 Publication1
    Binding sitei151SubstrateCombined 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 sitei163NADCombined sources1 Publication1

    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 bindingi18 – 24NADCombined sources1 Publication7
    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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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
    ECOL316407:JW1611-MONOMER
    MetaCyc: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:
    7-alpha-hydroxysteroid dehydrogenase1 Publication (EC:1.1.1.1592 Publications)
    Short name:
    7-alpha-HSDH1 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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
    <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

    GO - Cellular componenti

    Complete GO annotation on QuickGO ...

    <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 – 2557-alpha-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

    Complete GO annotation on QuickGO ...

    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

    Belongs to the short-chain dehydrogenases/reductases (SDR) family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		ENOG4107ZQV Bacteria
    ENOG410XPR5 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_010194_1_3_6

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P0AET8

    KEGG Orthology (KO)

    More...    KOi    		K00076

    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[»]
    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

    eggNOGiENOG4107ZQV Bacteria
    ENOG410XPR5 LUCA
    HOGENOMiCLU_010194_1_3_6
    InParanoidiP0AET8
    KOiK00076
    PhylomeDBiP0AET8

    Enzyme and pathway databases

    BioCyciEcoCyc:7-ALPHA-HYDROXYSTEROID-DEH-MONOMER
    ECOL316407:JW1611-MONOMER
    MetaCyc: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

    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 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: June 17, 2020
    This is version 120 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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