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Protein

Enamidase

Gene

Ena

Organism
Eubacterium barkeri (Clostridium barkeri)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Decyclization of 6-oxo-1,4,5,6-tetrahydronicotinate to form 2-(enamine)glutarate, followed by hydrolysis to form (S)-2-formylglutarate.2 Publications

Catalytic activityi

6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Fe cationNote: Binds 1 Fe cation per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Kineticsi

  1. KM=5 mM for 6-oxo-1,4,5,6-tetrahydronicotinate1 Publication

    Pathwayi: nicotinate degradation

    This protein is involved in step 2 of the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate.1 Publication
    Proteins known to be involved in the 8 steps of the subpathway in this organism are:
    1. 6-hydroxynicotinate reductase (Hnr)
    2. Enamidase (Ena)
    3. 2-(hydroxymethyl)glutarate dehydrogenase (Hgd)
    4. no protein annotated in this organism
    5. 2-methyleneglutarate mutase (mgm)
    6. 3-methylitaconate isomerase (mii)
    7. 2,3-dimethylmalate dehydratase small subunit (DmdB), 2,3-dimethylmalate dehydratase large subunit (dmdA)
    8. 2,3-dimethylmalate lyase (Dml)
    This subpathway is part of the pathway nicotinate degradation, which is itself part of Cofactor degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes propanoate and pyruvate from 6-hydroxynicotinate, the pathway nicotinate degradation and in Cofactor degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Metal bindingi67Zinc; via tele nitrogen1 Publication1
    Metal bindingi69Zinc; via tele nitrogen1 Publication1
    Metal bindingi164Iron1 Publication1
    Metal bindingi164Zinc1 Publication1
    Metal bindingi193Iron; via pros nitrogen1 Publication1
    Metal bindingi220Iron; via tele nitrogen1 Publication1
    Metal bindingi276Zinc1 Publication1

    GO - Molecular functioni

    • enamidase activity Source: UniProtKB
    • metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    • cofactor catabolic process Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Iron, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13673.
    BRENDAi3.5.2.18. 1459.
    UniPathwayiUPA01010; UER01013.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EnamidaseImported (EC:3.5.2.18)
    Gene namesi
    Name:EnaImported
    OrganismiEubacterium barkeri (Clostridium barkeri)
    Taxonomic identifieri1528 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved1 Publication
    ChainiPRO_00004039982 – 386Enamidase1 PublicationAdd BLAST385

    Interactioni

    Subunit structurei

    Homotetramer. Dimer of dimers.2 Publications

    Protein-protein interaction databases

    DIPiDIP-61252N.

    Structurei

    Secondary structure

    1386
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi3 – 8Combined sources6
    Beta strandi10 – 13Combined sources4
    Beta strandi25 – 30Combined sources6
    Beta strandi33 – 39Combined sources7
    Helixi40 – 43Combined sources4
    Beta strandi50 – 53Combined sources4
    Beta strandi58 – 61Combined sources4
    Beta strandi63 – 68Combined sources6
    Helixi77 – 79Combined sources3
    Beta strandi81 – 83Combined sources3
    Helixi84 – 89Combined sources6
    Turni90 – 92Combined sources3
    Beta strandi93 – 98Combined sources6
    Helixi111 – 127Combined sources17
    Helixi130 – 132Combined sources3
    Beta strandi134 – 136Combined sources3
    Helixi148 – 156Combined sources9
    Beta strandi161 – 165Combined sources5
    Beta strandi167 – 169Combined sources3
    Helixi173 – 185Combined sources13
    Beta strandi189 – 193Combined sources5
    Helixi207 – 213Combined sources7
    Beta strandi216 – 219Combined sources4
    Turni220 – 222Combined sources3
    Beta strandi224 – 226Combined sources3
    Helixi230 – 239Combined sources10
    Beta strandi243 – 250Combined sources8
    Helixi252 – 265Combined sources14
    Helixi268 – 270Combined sources3
    Beta strandi271 – 274Combined sources4
    Beta strandi277 – 279Combined sources3
    Helixi287 – 298Combined sources12
    Helixi303 – 310Combined sources8
    Helixi312 – 318Combined sources7
    Beta strandi333 – 337Combined sources5
    Helixi347 – 353Combined sources7
    Beta strandi358 – 364Combined sources7
    Beta strandi367 – 372Combined sources6
    Beta strandi374 – 376Combined sources3
    Beta strandi379 – 381Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2VUNX-ray1.89A/B/C/D1-386[»]
    ProteinModelPortaliQ0QLE9.
    SMRiQ0QLE9.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ0QLE9.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the adenine deaminase family.Curated

    Phylogenomic databases

    KOiK15358.

    Family and domain databases

    Gene3Di2.30.40.10. 3 hits.
    InterProiIPR006680. Amidohydro-rel.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q0QLE9-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSKTIIKNIG KIVSGDIKSP VLQADTIVVE DGLIAAIGGE ELMKDAGDAT
    60 70 80 90 100
    IIDAAGSTVT PGLLDTHVHV SGGDYAPRQK TMDFISSALH GGVTTMISAG
    110 120 130 140 150
    SPHFPGRPKD AAGTKALAIT LSKSYYNARP AGVKVHGGAV ILEKGLTEED
    160 170 180 190 200
    FIEMKKEGVW IVGEVGLGTI KNPEDAAPMV EWAHKHGFKV QMHTGGTSIP
    210 220 230 240 250
    GSSTVTADDV IKTKPDVVSH INGGPTAISV QEVDRIMDET DFAMEIVQCG
    260 270 280 290 300
    NPKIADYVAR RAAEKGQLGR VIFGNDAPSG TGLIPLGILR NMCQIASMSD
    310 320 330 340 350
    IDPEVAVCMA TGNSTAVYGL NTGVIAPGKE ADLIIMDTPL GSVAEDAMGA
    360 370 380
    IAAGDIPGIS VVLIDGEAVV TKSRNTPPAK RAAKIL
    Length:386
    Mass (Da):39,923
    Last modified:September 5, 2006 - v1
    Checksum:i84AF39771B54B87D
    GO

    Mass spectrometryi

    Molecular mass is 39750±40 Da from positions 2 - 386. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88401.1.

    Genome annotation databases

    KEGGiag:ABC88401.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    DQ310789 Genomic DNA. Translation: ABC88401.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2VUNX-ray1.89A/B/C/D1-386[»]
    ProteinModelPortaliQ0QLE9.
    SMRiQ0QLE9.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-61252N.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    KEGGiag:ABC88401.

    Phylogenomic databases

    KOiK15358.

    Enzyme and pathway databases

    UniPathwayiUPA01010; UER01013.
    BioCyciMetaCyc:MONOMER-13673.
    BRENDAi3.5.2.18. 1459.

    Miscellaneous databases

    EvolutionaryTraceiQ0QLE9.

    Family and domain databases

    Gene3Di2.30.40.10. 3 hits.
    InterProiIPR006680. Amidohydro-rel.
    IPR011059. Metal-dep_hydrolase_composite.
    IPR032466. Metal_Hydrolase.
    [Graphical view]
    PfamiPF01979. Amidohydro_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51338. SSF51338. 2 hits.
    SSF51556. SSF51556. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiENA_EUBBA
    AccessioniPrimary (citable) accession number: Q0QLE9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 8, 2011
    Last sequence update: September 5, 2006
    Last modified: November 2, 2016
    This is version 36 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.