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Entry version 44 (11 Dec 2019)
Sequence version 1 (16 Nov 2011)
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Protein

N-carbamoyl-L-amino-acid hydrolase

Gene

hyuC

Organism
Rhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
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

May be involved in the asymmetric conversion of racemic 5-substituted hydantoins to the corresponding L-amino acids. Catalyzes specifically the conversion of N-carbamoyl-L-amino acids to free L-amino acids in an irreversible reaction. N-carbamoyl-L-methionine is the best substrate. HyuC of R.meliloti is the first L-N-carbamoylase that hydrolyzes N-carbamoyl-L-tryptophan as well as N-carbamoyl-L-amino acids with aliphatic substituents.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Mn2+1 Publication, Ni2+1 Publication, Co2+1 Publication, Fe2+1 PublicationNote: Binds 2 divalent metal cations per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Ni2+, Mn2+, Co2+ and Fe2+ ions greatly increase hydrolase activity. Strongly inhibited by Hg2+, Cu2+, Zn2+, Pb2+ and Fe3+ ions, and slightly inhibited by Na+ and K+ ions. Beta-mercaptoethanol and 5,5'-dithiobis-(2-nitrobenzoic acid)(DTNB) cause 34% and 42% inhibition, respectively.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 91.66 sec(-1) for formyl-L-methionine as substrate (at 40 degrees Celsius). Kcat is 66.84 sec(-1) for N-acetyl-L-methionine as substrate (at 40 degrees Celsius). Kcat is 16.9 sec(-1) for N-carbamoyl-L-valine as substrate (at 40 degrees Celsius). Kcat is 14.46 sec(-1) for N-carbamoyl-L-methionine as substrate (at 40 degrees Celsius). Kcat is 13.55 sec(-1) for N-carbamoyl-L-cysteine as substrate (at 40 degrees Celsius). Kcat is 4.26 sec(-1) for N-carbamoyl-L-phenylalanine as substrate (at 40 degrees Celsius). Kcat is 2.59 sec(-1) for N-carbamoyl-L-alanine as substrate (at 40 degrees Celsius). Kcat is 1.52 sec(-1) for N-carbamoyl-L-glutamic acid as substrate (at 40 degrees Celsius). Kcat is 0.30 sec(-1) for N-carbamoyl-L-tyrosine as substrate (at 40 degrees Celsius). Kcat is 0.15 sec(-1) for N-carbamoyl-L-tryptophan as substrate (at 40 degrees Celsius).1 Publication
  1. KM=0.65 mM for N-carbamoyl-L-tryptophan (at 40 degrees Celsius)1 Publication
  2. KM=0.69 mM for N-carbamoyl-L-methionine (at 40 degrees Celsius)1 Publication
  3. KM=0.94 mM for N-carbamoyl-L-alanine (at 40 degrees Celsius)1 Publication
  4. KM=2.61 mM for N-carbamoyl-L-phenylalanine (at 40 degrees Celsius)1 Publication
  5. KM=4.80 mM for N-carbamoyl-L-tyrosine (at 40 degrees Celsius)1 Publication
  6. KM=4.91 mM for N-carbamoyl-L-cysteine (at 40 degrees Celsius)1 Publication
  7. KM=5.5 mM for N-acetyl-L-methionine (at 40 degrees Celsius)1 Publication
  8. KM=12.9 mM for N-formyl-L-methionine (at 40 degrees Celsius)1 Publication
  9. KM=34.47 mM for N-carbamoyl-L-valine (at 40 degrees Celsius)1 Publication
  10. KM=51.23 mM for N-carbamoyl-L-glutamic acid (at 40 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi87Divalent metal cation 1; via tele nitrogenBy similarity1
    Metal bindingi98Divalent metal cation 1By similarity1
    Metal bindingi98Divalent metal cation 2By similarity1
    Metal bindingi133Divalent metal cation 2By similarity1
    Metal bindingi194Divalent metal cation 1; via tele nitrogenBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei230SubstrateBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei239Necessary for dimerizationBy similarity1
    Binding sitei279SubstrateBy similarity1
    Binding sitei292SubstrateBy similarity1
    Metal bindingi386Divalent metal cation 2; via tele nitrogenBy similarity1
    Binding sitei386SubstrateBy similarity1

    <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 processAmino-acid biosynthesis
    LigandManganese, Metal-binding

    <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_and_taxonomy_section">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:
    N-carbamoyl-L-amino-acid hydrolase1 Publication (EC:3.5.1.871 Publication)
    Alternative name(s):
    Hydantoin utilization protein CBy similarity
    L-N-carbamoylase1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:hyuC1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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>OrganismiRhizobium meliloti (Ensifer meliloti) (Sinorhizobium meliloti)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 identifieri382 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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 lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium

    <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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004399311 – 416N-carbamoyl-L-amino-acid hydrolaseAdd BLAST416

    <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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homodimer.

    1 Publication

    <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
    Q6DTN4

    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

    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>Regioni132 – 133SubstrateBy similarity2
    Regioni194 – 197SubstrateBy similarity4
    Regioni216 – 330Involved in dimerizationBy similarityAdd BLAST115
    Regioni361 – 362SubstrateBy similarity2

    <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 peptidase M20 family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    ENOG4105CE7 Bacteria
    COG0624 LUCA

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR010158 Amidase_Cbmase
    IPR036264 Bact_exopeptidase_dim_dom
    IPR002933 Peptidase_M20
    IPR011650 Peptidase_M20_dimer

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR32494 PTHR32494, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF07687 M20_dimer, 1 hit
    PF01546 Peptidase_M20, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001235 Amidase_carbamoylase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF55031 SSF55031, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01879 hydantase, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

    Q6DTN4-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MAAPGENRRV NADRLWDSLM EMAKIGPGVA GGNNRQTLTD ADGEGRRLFQ
    60 70 80 90 100
    SWCEEAGLSM GVDKMGTMFL TRPGTDPDAL PVHIGSHLDT QPTGGKFDGV
    110 120 130 140 150
    LGVLSGLEAV RTMNDLGIKT KHPIVVTNWT NEEGARFAPA MLASGVFAGV
    160 170 180 190 200
    HTLEYAYARK DPEGKSFGDE LKRIGWLGDE EVGARKMHAY FEYHIEQGPI
    210 220 230 240 250
    LEAENKQIGV VTHCQGLWWL EFTLTGREAH TGSTPMDMRV NAGLAMARIL
    260 270 280 290 300
    EMVQTVAMEN QPGAVGGVGQ MFFSPNSRNV LPGKVVFTVD IRSPDQAKLD
    310 320 330 340 350
    GMRARIEAEA PKICERLGVG CSIEAVGHFD PVTFDPKLVE TVRGAAEKLG
    360 370 380 390 400
    YSHMNLVSGA GHDACWAAKV APTTMIMCPC VGGLSHNEAE DISREWAAAG
    410
    ADVLFHAVLE TAEIVE
    Length:416
    Mass (Da):44,857
    Last modified:November 16, 2011 - 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:i85BA5F11BD855B97
    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
    AY646850 Genomic DNA Translation: AAT66633.1

    NCBI Reference Sequences

    More...
    RefSeqi
    WP_010969946.1, NZ_RPNY01000039.1

    Genome annotation databases

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|382.52.peg.2781

    <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
    AY646850 Genomic DNA Translation: AAT66633.1
    RefSeqiWP_010969946.1, NZ_RPNY01000039.1

    3D structure databases

    SMRiQ6DTN4
    ModBaseiSearch...

    Genome annotation databases

    PATRICifig|382.52.peg.2781

    Phylogenomic databases

    eggNOGiENOG4105CE7 Bacteria
    COG0624 LUCA

    Family and domain databases

    InterProiView protein in InterPro
    IPR010158 Amidase_Cbmase
    IPR036264 Bact_exopeptidase_dim_dom
    IPR002933 Peptidase_M20
    IPR011650 Peptidase_M20_dimer
    PANTHERiPTHR32494 PTHR32494, 1 hit
    PfamiView protein in Pfam
    PF07687 M20_dimer, 1 hit
    PF01546 Peptidase_M20, 1 hit
    PIRSFiPIRSF001235 Amidase_carbamoylase, 1 hit
    SUPFAMiSSF55031 SSF55031, 1 hit
    TIGRFAMsiTIGR01879 hydantase, 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 nameiHYUC_RHIML
    <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: Q6DTN4
    <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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2017
    Last sequence update: November 16, 2011
    Last modified: December 11, 2019
    This is version 44 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

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Peptidase families
      Classification of peptidase families and list of entries
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