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Entry version 140 (17 Jun 2020)
Sequence version 1 (01 Nov 1999)
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Protein

Phosphoribosylformylglycinamidine synthase subunit PurL

Gene

purL

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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

Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.UniRule annotation2 Publications

Miscellaneous

Purl possesses an Auxiliary ATP Binding region which is not catalytic, but able to bind additional ATP. The conformational changes associated with its binding could have a regulatory role in formation of the PurLSQ complex (PubMed:17154526).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 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 0.39 sec(-1) for FGAM synthase activity with NH4Cl as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.40 sec(-1) for FGAM synthase activity with FGAR as substrate (at pH 8 and 37 degrees Celsius). Kcat is 0.41 sec(-1) for FGAM synthase activity with ATP as substrate (at pH 8 and 37 degrees Celsius).
  1. KM=0.26 mM for ATP (at pH 8 and 37 degrees Celsius)1 Publication
  2. KM=1.05 mM for FGAR (at pH 8 and 37 degrees Celsius)1 Publication
  3. KM=158 mM for NH4Cl (at pH 8 and 37 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: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide.UniRule annotation
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Phosphoribosylformylglycinamidine synthase subunit PurL (purL), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurS (purS), Phosphoribosylformylglycinamidine synthase subunit PurQ (purQ), Phosphoribosylformylglycinamidine synthase subunit PurL (purL)
    2. Phosphoribosylformylglycinamidine cyclo-ligase (TM_1251), Phosphoribosylformylglycinamidine cyclo-ligase (Tmari_1256)
    This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    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 sitei32UniRule annotation1 Publication1
    <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 sitei35ATPUniRule annotation2 Publications1
    Binding sitei68ATPUniRule annotation2 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi70Magnesium 1UniRule annotation1 Publication1
    Active sitei72Proton acceptor1 Publication1
    Binding sitei93Substrate1
    Metal bindingi94Magnesium 2UniRule annotation1 Publication1
    Binding sitei107ATP; auxiliary1 Publication1
    Binding sitei189Substrate; via carbonyl oxygen1
    Binding sitei208Substrate1
    Metal bindingi236Magnesium 2UniRule annotation1 Publication1
    Binding sitei388ATP; via carbonyl oxygen; auxiliary1 Publication1
    Binding sitei429ATP; auxiliary1 Publication1
    Binding sitei442ATPUniRule annotation2 Publications1
    Binding sitei477ATP; via amide nitrogen and carbonyl oxygenUniRule annotation2 Publications1
    Metal bindingi478Magnesium 1UniRule annotation1 Publication1
    Binding sitei480Substrate1
    Binding sitei549ATP; auxiliary1 Publication1
    Binding sitei556ATP; auxiliary1 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 bindingi136 – 139Auxiliary ATP binding site4

    <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

    • ATP binding Source: UniProtKB
    • magnesium ion binding Source: UniProtKB
    • phosphoribosylformylglycinamidine synthase activity Source: UniProtKB

    GO - Biological processi

    • 'de novo' IMP biosynthetic process Source: UniProtKB-UniRule
    • purine nucleobase biosynthetic process Source: GO_Central
    • purine nucleotide biosynthetic process Source: UniProtKB

    <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 functionLigase
    Biological processPurine biosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    TMAR243274:G1H0Q-1626-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.3.5.3 6331

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

    More...
    UniPathwayi
    UPA00074;UER00128

    <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:
    Phosphoribosylformylglycinamidine synthase subunit PurLUniRule annotation (EC:6.3.5.3UniRule annotation)
    Short name:
    FGAM synthaseUniRule annotation
    Alternative name(s):
    Formylglycinamide ribonucleotide amidotransferase subunit IIUniRule annotation
    Short name:
    FGAR amidotransferase IIUniRule annotation
    Short name:
    FGAR-AT IIUniRule annotation
    Glutamine amidotransferase PurLUniRule annotation
    Phosphoribosylformylglycinamidine synthase subunit IIUniRule annotation
    <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:purLUniRule annotation
    Ordered Locus Names:TM_1246
    <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>OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
    <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 identifieri243274 [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 lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
    <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
    • UP000008183 <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

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    <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>Mutagenesisi32H → A: Loss of FGAM synthase activity. 1 Publication1
    Mutagenesisi32H → Q: Loss of FGAM synthase activity. 1 Publication1
    Mutagenesisi72H → A: Strong decrease of the binding affinity and 20-fold decrease of the catalytic efficiency for FGAR. It has no effect on the ATP binding site, however it affects binding of FGAR. 1 Publication1
    Mutagenesisi72H → Q: 200-fold decrease of the catalytic efficiency for FGAR. It has no effect on the ATP binding site, however it affects binding of FGAR. 1 Publication1

    <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_00001005011 – 603Phosphoribosylformylglycinamidine synthase subunit PurLAdd BLAST603

    <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

    Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits.

    UniRule annotation3 Publications

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    243274.THEMA_08105

    <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

    1603
    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
    Q9X0X3

    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
    Q9X0X3

    <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

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni71 – 74Substrate binding4
    Regioni280 – 282Substrate binding3

    <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 FGAMS family.UniRule annotation

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4108JIU Bacteria
    COG0046 LUCA

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9X0X3

    KEGG Orthology (KO)

    More...
    KOi
    K23269

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    EHCGYSH

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.30.1330.10, 2 hits
    3.30.70.1670, 1 hit
    3.90.650.10, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00420 PurL_2, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010074 PRibForGlyAmidine_synth_PurL
    IPR031652 PurL_C
    IPR038411 PurL_C_sf
    IPR041609 PurL_linker
    IPR010918 PurM-like_C_dom
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00586 AIRS, 2 hits
    PF02769 AIRS_C, 1 hit
    PF18072 FGAR-AT_linker, 1 hit
    PF16904 PurL_C, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55326 SSF55326, 2 hits
    SSF56042 SSF56042, 2 hits

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01736 FGAM_synth_II, 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.

    Q9X0X3-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MKLRYLNILK EKLGREPTFV ELQAFSVMWS EHCGYSHTKK YIRRLPKTGF
    60 70 80 90 100
    EGNAGVVNLD DYYSVAFKIE SHNHPSAIEP YNGAATGVGG IIRDVLAMGA
    110 120 130 140 150
    RPTAIFDSLH MSRIIDGIIE GIADYGNSIG VPTVGGELRI SSLYAHNPLV
    160 170 180 190 200
    NVLAAGVVRN DMLVDSKASR PGQVIVIFGG ATGRDGIHGA SFASEDLTGD
    210 220 230 240 250
    KATKLSIQVG DPFAEKMLIE AFLEMVEEGL VEGAQDLGAG GVLSATSELV
    260 270 280 290 300
    AKGNLGAIVH LDRVPLREPD MEPWEILISE SQERMAVVTS PQKASRILEI
    310 320 330 340 350
    ARKHLLFGDV VAEVIEEPVY RVMYRNDLVM EVPVQLLANA PEEDIVEYTP
    360 370 380 390 400
    GKIPEFKRVE FEEVNAREVF EQYDHMVGTD TVVPPGFGAA VMRIKRDGGY
    410 420 430 440 450
    SLVTHSRADL ALQDTYWGTL IAVLESVRKT LSVGAEPLAI TNCVNYGDPD
    460 470 480 490 500
    VDPVGLSAMM TALKNACEFS GVPVASGNAS LYNTYQGKPI PPTLVVGMLG
    510 520 530 540 550
    KVNPQKVAKP KPSKVFAVGW NDFELEREKE LWRAIRKLSE EGAFILSSSQ
    560 570 580 590 600
    LLTRTHVETF REYGLKIEVK LPEVRPAHQM VLVFSERTPV VDVPVKEIGT

    LSR
    Length:603
    Mass (Da):65,969
    Last modified:November 1, 1999 - 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:iA9F85FE258EE4914
    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
    AE000512 Genomic DNA Translation: AAD36321.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    H72276

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_229051.1, NC_000853.1
    WP_004080021.1, NZ_CP011107.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAD36321; AAD36321; TM_1246

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    898237

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    tma:TM1246
    tmw:THMA_1271

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|243274.19.peg.1249

    <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
    AE000512 Genomic DNA Translation: AAD36321.1
    PIRiH72276
    RefSeqiNP_229051.1, NC_000853.1
    WP_004080021.1, NZ_CP011107.1

    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
    1VK3X-ray2.15A1-603[»]
    2HRUX-ray2.80A1-603[»]
    2HRYX-ray2.80A1-603[»]
    2HS0X-ray2.52A1-603[»]
    2HS3X-ray2.30A1-603[»]
    2HS4X-ray2.70A1-603[»]
    3D54X-ray3.50A/E/I1-603[»]
    SMRiQ9X0X3
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    STRINGi243274.THEMA_08105

    Genome annotation databases

    EnsemblBacteriaiAAD36321; AAD36321; TM_1246
    GeneIDi898237
    KEGGitma:TM1246
    tmw:THMA_1271
    PATRICifig|243274.19.peg.1249

    Phylogenomic databases

    eggNOGiENOG4108JIU Bacteria
    COG0046 LUCA
    InParanoidiQ9X0X3
    KOiK23269
    OMAiEHCGYSH

    Enzyme and pathway databases

    UniPathwayiUPA00074;UER00128
    BioCyciTMAR243274:G1H0Q-1626-MONOMER
    BRENDAi6.3.5.3 6331

    Miscellaneous databases

    EvolutionaryTraceiQ9X0X3

    Family and domain databases

    Gene3Di3.30.1330.10, 2 hits
    3.30.70.1670, 1 hit
    3.90.650.10, 1 hit
    HAMAPiMF_00420 PurL_2, 1 hit
    InterProiView protein in InterPro
    IPR010074 PRibForGlyAmidine_synth_PurL
    IPR031652 PurL_C
    IPR038411 PurL_C_sf
    IPR041609 PurL_linker
    IPR010918 PurM-like_C_dom
    IPR036676 PurM-like_C_sf
    IPR016188 PurM-like_N
    IPR036921 PurM-like_N_sf
    PfamiView protein in Pfam
    PF00586 AIRS, 2 hits
    PF02769 AIRS_C, 1 hit
    PF18072 FGAR-AT_linker, 1 hit
    PF16904 PurL_C, 1 hit
    SUPFAMiSSF55326 SSF55326, 2 hits
    SSF56042 SSF56042, 2 hits
    TIGRFAMsiTIGR01736 FGAM_synth_II, 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 nameiPURL_THEMA
    <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: Q9X0X3
    <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: July 11, 2001
    Last sequence update: November 1, 1999
    Last modified: June 17, 2020
    This is version 140 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, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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