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Entry version 132 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
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Protein

S-inosyl-L-homocysteine hydrolase

Gene

MJ1388

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score:

Annotation score:4 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 hydrolysis of S-inosyl-L-homocysteine (SIH) to L-homocysteine (Hcy) and inosine. Likely functions in a S-adenosyl-L-methionine (SAM) recycling pathway from S-adenosyl-L-homocysteine (SAH) produced from SAM-dependent methylation reactions. Can also catalyze the reverse reaction in vitro, i.e. the synthesis of SIH from Hcy and inosine. Is specific for SIH and inosine as it is unable to either hydrolyze SAH or synthesize SAH from adenosine and Hcy.

1 Publication

Miscellaneous

SAH is a product of SAM methyltransferases and is known to be a feedback inhibitor of these enzymes. As a result of this inhibition, organisms have evolved efficient enzymes to metabolize SAH via different pathways. The pathway found in methanogens differs from the canonical pathway, it uses the deamination of S-adenosyl-L-homocysteine to form S-inosyl-L-homocysteine for the regeneration of SAM from S-adenosyl-L-homocysteine.1 Publication

<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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

NAD+1 PublicationNote: Binds 1 NAD+ per subunit.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 0.83 sec(-1) for the synthesis of SIH from inosine and L-homocysteine. kcat is 0.42 sec(-1) for the hydrolysis of SIH (at pH 7.0 and 70 degrees Celsius).1 Publication
  1. KM=0.64 mM for inosine (at pH 7.0 and 70 degrees Celsius)1 Publication
  2. KM=0.0054 mM for L-homocysteine (at pH 7.0 and 70 degrees Celsius)1 Publication
  3. KM=0.22 mM for S-inosyl-L-homocysteine (at pH 7.0 and 70 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 7.0-7.5 and pH 9.6 for the reaction in the direction of SIH synthesis. Shows no activity at either pH 6.5 or pH 11.5 in the synthetic direction. The activity of SIHH in the hydrolysis direction shows essentially the same activity over the pH range 6.5-11.5.1 Publication

    Temperature dependencei

    Optimum temperature is about 70 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: S-adenosyl-L-methionine biosynthesis

    This protein is involved in the pathway S-adenosyl-L-methionine biosynthesis, which is part of Amino-acid biosynthesis.1 Publication
    View all proteins of this organism that are known to be involved in the pathway S-adenosyl-L-methionine biosynthesis and in Amino-acid biosynthesis.

    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 sitei123SubstrateUniRule annotation1
    Binding sitei148SubstrateUniRule annotation1
    Binding sitei178SubstrateUniRule annotation1
    Binding sitei182SubstrateUniRule annotation1
    Binding sitei183NADUniRule annotation1
    Binding sitei235NADUniRule annotation1
    Binding sitei337NADUniRule annotation1

    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 bindingi149 – 151NADUniRule annotation3
    Nucleotide bindingi212 – 217NADUniRule annotation6
    Nucleotide bindingi291 – 293NADUniRule annotation3

    <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 functionHydrolase
    Biological processOne-carbon metabolism
    LigandNAD

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MJAN243232:G1GKE-1503-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    3.13.1.9, 3260
    3.3.1.B1, 3260

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

    More...
    UniPathwayi
    UPA00315

    <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:
    S-inosyl-L-homocysteine hydrolase1 Publication (EC:3.13.1.9UniRule annotation1 Publication)
    Short name:
    SIHH1 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
    Ordered Locus Names:MJ1388
    <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>OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
    <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 identifieri243232 [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 lineageiArchaeaEuryarchaeotaMethanomada groupMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
    <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
    • UP000000805 <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

    <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

    Keywords - Cellular componenti

    Cytoplasm

    <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_00001170041 – 415S-inosyl-L-homocysteine hydrolaseAdd BLAST415

    <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

    Exists both as a homotetramer and a homodimer, in a 4:1 ratio.

    1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243232.MJ_1388

    <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

    More...
    SMRi
    Q58783

    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

    Belongs to the adenosylhomocysteinase family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    arCOG04137, Archaea

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_025194_2_1_2

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q58783

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    MPAINVN

    Database of Orthologous Groups

    More...
    OrthoDBi
    17629at2157

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q58783

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00401, SAHH, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.1480, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00563, AdoHcyase, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR042172, Adenosylhomocyst_ase-like_sf
    IPR000043, Adenosylhomocysteinase-like
    IPR015878, Ado_hCys_hydrolase_NAD-bd
    IPR036291, NAD(P)-bd_dom_sf
    IPR020082, S-Ado-L-homoCys_hydrolase_CS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR23420, PTHR23420, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF05221, AdoHcyase, 2 hits
    PF00670, AdoHcyase_NAD, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001109, Ad_hcy_hydrolase, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00996, AdoHcyase, 1 hit
    SM00997, AdoHcyase_NAD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51735, SSF51735, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00936, ahcY, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00738, ADOHCYASE_1, 1 hit
    PS00739, ADOHCYASE_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%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.

    Q58783-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MYEVRDINLW KEGERKIQWA KQHMPVLNLI RERFKEEKPF KGITIGMALH
    60 70 80 90 100
    LEAKTAVLAE TLMEGGAEIA ITGCNPLSTQ DDVAAACAKK GMHVYAWRGE
    110 120 130 140 150
    TVEEYYENLN KVLDHKPDIV IDDGCDLIFL LHTKRTELLD NIMGGCEETT
    160 170 180 190 200
    TGIIRLKAME KEGALKFPVM DVNDAYTKHL FDNRYGTGQS ALDGILRATN
    210 220 230 240 250
    LLIAGKTVVV AGYGWCGRGV AMRAKGLGAE VVVTEVNPIR ALEARMDGFR
    260 270 280 290 300
    VMKMEKAAEI GDIFITTTGC KDVIRKEHIL KMRNGAILAN AGHFDNEINK
    310 320 330 340 350
    KHLEELAKSI KEVRNCVTEY DLGNKKIYLL GEGRLVNLAC ADGHPCEVMD
    360 370 380 390 400
    MSFANQALAA EYILKNHEKL EPRVYNIPYE QDLMIASLKL KAMGIEIDEL
    410
    TKEQKKYLED WREGT
    Length:415
    Mass (Da):46,607
    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:i16B1456E74D180F5
    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
    L77117 Genomic DNA Translation: AAB99397.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    C64473

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010870905.1, NC_000909.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAB99397; AAB99397; MJ_1388

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    1452291

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    mja:MJ_1388

    <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
    L77117 Genomic DNA Translation: AAB99397.1
    PIRiC64473
    RefSeqiWP_010870905.1, NC_000909.1

    3D structure databases

    SMRiQ58783
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi243232.MJ_1388

    Genome annotation databases

    EnsemblBacteriaiAAB99397; AAB99397; MJ_1388
    GeneIDi1452291
    KEGGimja:MJ_1388

    Phylogenomic databases

    eggNOGiarCOG04137, Archaea
    HOGENOMiCLU_025194_2_1_2
    InParanoidiQ58783
    OMAiMPAINVN
    OrthoDBi17629at2157
    PhylomeDBiQ58783

    Enzyme and pathway databases

    UniPathwayiUPA00315
    BioCyciMJAN243232:G1GKE-1503-MONOMER
    BRENDAi3.13.1.9, 3260
    3.3.1.B1, 3260

    Family and domain databases

    CDDicd00401, SAHH, 1 hit
    Gene3Di3.40.50.1480, 1 hit
    HAMAPiMF_00563, AdoHcyase, 1 hit
    InterProiView protein in InterPro
    IPR042172, Adenosylhomocyst_ase-like_sf
    IPR000043, Adenosylhomocysteinase-like
    IPR015878, Ado_hCys_hydrolase_NAD-bd
    IPR036291, NAD(P)-bd_dom_sf
    IPR020082, S-Ado-L-homoCys_hydrolase_CS
    PANTHERiPTHR23420, PTHR23420, 1 hit
    PfamiView protein in Pfam
    PF05221, AdoHcyase, 2 hits
    PF00670, AdoHcyase_NAD, 1 hit
    PIRSFiPIRSF001109, Ad_hcy_hydrolase, 1 hit
    SMARTiView protein in SMART
    SM00996, AdoHcyase, 1 hit
    SM00997, AdoHcyase_NAD, 1 hit
    SUPFAMiSSF51735, SSF51735, 1 hit
    TIGRFAMsiTIGR00936, ahcY, 1 hit
    PROSITEiView protein in PROSITE
    PS00738, ADOHCYASE_1, 1 hit
    PS00739, ADOHCYASE_2, 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 nameiSIHH_METJA
    <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: Q58783
    <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 15, 1998
    Last sequence update: November 1, 1996
    Last modified: June 2, 2021
    This is version 132 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

    Reference proteome

    Documents

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