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Entry version 112 (22 Apr 2020)
Sequence version 1 (01 Apr 1988)
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Protein

Steroid Delta-isomerase

Gene

ksi

Organism
Pseudomonas putida (Arthrobacter siderocapsulatus)
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

<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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei16Proton donor1
Active sitei40Proton acceptor1
<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 sitei103Substrate1 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

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
Biological processLipid metabolism, Steroid metabolism

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
5.3.3.1 5092

<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:
Steroid Delta-isomerase (EC:5.3.3.1)
Alternative name(s):
Delta(5)-3-ketosteroid isomerase
<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:ksi
<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>OrganismiPseudomonas putida (Arthrobacter siderocapsulatus)
<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 identifieri303 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

<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>Mutagenesisi16Y → F: Reduces activity 2000-fold. Reduces activity 10000-fold; when associated with E-103; N-103 or L-103. 3 Publications1
Mutagenesisi16Y → S: Reduces activity 20-fold. 3 Publications1
Mutagenesisi32Y → S: Reduces activity 4-fold. 1 Publication1
Mutagenesisi57Y → S: Reduces activity 100-fold. 1
Mutagenesisi92W → A: Slightly reduces activity. Reduces protein stability. 1
Mutagenesisi103D → A or L: Reduces activity 100-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi103D → E: Slightly reduces activity. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi103D → N: Reduces activity 4-fold. Reduces activity 10000-fold; when associated with F-16. 2 Publications1
Mutagenesisi125L → A: Slightly reduces activity and reduces protein stability; when associated with A-127. 1 Publication1
Mutagenesisi127V → A: Slightly reduces activity and reduces protein stability; when associated with A-125. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2321641

Drug and drug target database

More...
DrugBanki
DB03619 Deoxycholic acid
DB03515 Equilenin
DB01708 Prasterone

DrugCentral

More...
DrugCentrali
P07445

<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_00000976461 – 131Steroid Delta-isomeraseAdd BLAST131

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P07445

<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 steroids.

<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

Homodimer.

3 Publications

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P07445

<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

1131
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
P07445

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
P07445

<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

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00781 ketosteroid_isomerase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039256 Ketosteroid_isomerase
IPR032710 NTF2-like_dom_sf
IPR037401 SnoaL-like

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12680 SnoaL_2, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54427 SSF54427, 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.

P07445-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLPTAQEVQ GLMARYIELV DVGDIEAIVQ MYADDATVED PFGQPPIHGR
60 70 80 90 100
EQIAAFYRQG LGGGKVRACL TGPVRASHNG CGAMPFRVEM VWNGQPCALD
110 120 130
VIDVMRFDEH GRIQTMQAYW SEVNLSVREP Q
Length:131
Mass (Da):14,536
Last modified:April 1, 1988 - 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:i08711198C13CF014
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
L13127 Genomic DNA Translation: AAA64437.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A25216 SIPSDP

<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
L13127 Genomic DNA Translation: AAA64437.1
PIRiA25216 SIPSDP

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
1C7HX-ray2.50A1-131[»]
1CQSX-ray1.90A/B1-131[»]
1DMMX-ray1.90A1-131[»]
1DMNX-ray2.05A1-131[»]
1DMQX-ray2.15A1-131[»]
1E3RX-ray2.50A/B1-131[»]
1E3VX-ray2.00A/B1-131[»]
1E97X-ray2.00A1-131[»]
1EA2X-ray1.80A1-131[»]
1GS3X-ray2.10A1-131[»]
1K41X-ray2.20A/B1-131[»]
1OGXX-ray2.00A/B1-131[»]
1OH0X-ray1.10A/B1-131[»]
1OHOX-ray1.90A1-131[»]
1OPYX-ray1.90A1-131[»]
1VZZX-ray2.30A/B1-131[»]
1W00X-ray2.20A/B1-131[»]
1W01X-ray2.20A/B1-131[»]
1W02X-ray2.30A1-131[»]
1W6YX-ray2.10A1-131[»]
2INXX-ray1.50A1-131[»]
2PZVX-ray1.25A/B/C/D1-131[»]
3CPOX-ray1.24A1-131[»]
3FZWX-ray1.32A/B1-131[»]
3IPTX-ray1.63A/B/C/D1-131[»]
3OWSX-ray1.71A/B/C/D1-131[»]
3OWUX-ray1.70A/B/C/D1-131[»]
3OWYX-ray2.30A/B/C/D/E/F/G/H1-131[»]
3OX9X-ray2.00A/B/C/D1-131[»]
3OXAX-ray1.89A/B/C/D1-131[»]
3RGRX-ray1.59A1-131[»]
3SEDX-ray1.30A3-127[»]
3T8NX-ray1.47A/B/D/F1-131[»]
3VGNX-ray1.30A/B1-131[»]
3VSYX-ray1.50A/B3-131[»]
4CDLX-ray2.50A1-131[»]
4K1UX-ray2.00A/B1-131[»]
4K1VX-ray1.80A1-131[»]
5AI1X-ray2.10A1-131[»]
5D81X-ray1.39A1-131[»]
5D82X-ray1.37A/B1-131[»]
5D83X-ray1.70A/B1-131[»]
5G2GX-ray1.60A/B2-128[»]
5KP1X-ray1.22A/B/C/D1-131[»]
5KP3X-ray1.70A/B1-131[»]
5KP4X-ray1.71A/B1-131[»]
6C17X-ray1.10A1-131[»]
6C1JX-ray1.06A1-131[»]
6C1XX-ray1.05A1-131[»]
6F4YX-ray1.92A/B3-127[»]
6F50X-ray2.00A/B3-127[»]
6F53X-ray1.49A3-127[»]
6F54X-ray1.08A/B3-127[»]
SMRiP07445
ModBaseiSearch...
PDBe-KBiSearch...

Chemistry databases

BindingDBiP07445
ChEMBLiCHEMBL2321641
DrugBankiDB03619 Deoxycholic acid
DB03515 Equilenin
DB01708 Prasterone
DrugCentraliP07445

Proteomic databases

PRIDEiP07445

Enzyme and pathway databases

BRENDAi5.3.3.1 5092

Miscellaneous databases

EvolutionaryTraceiP07445

Family and domain databases

CDDicd00781 ketosteroid_isomerase, 1 hit
InterProiView protein in InterPro
IPR039256 Ketosteroid_isomerase
IPR032710 NTF2-like_dom_sf
IPR037401 SnoaL-like
PfamiView protein in Pfam
PF12680 SnoaL_2, 1 hit
SUPFAMiSSF54427 SSF54427, 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 nameiSDIS_PSEPU
<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: P07445
<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: April 1, 1988
Last sequence update: April 1, 1988
Last modified: April 22, 2020
This is version 112 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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