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P60327

- DCAS_AGRSK

UniProt

P60327 - DCAS_AGRSK

Protein

N-carbamoyl-D-amino acid hydrolase

Gene
N/A
Organism
Agrobacterium sp. (strain KNK712)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 43 (01 Oct 2014)
      Sequence version 1 (02 Feb 2004)
      Previous versions | rss
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    Functioni

    The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.

    Catalytic activityi

    N-carbamoyl-D-amino acid + H2O = D-amino acid + NH3 + CO2.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei47 – 471
    Active sitei127 – 1271
    Active sitei172 – 1721

    GO - Molecular functioni

    1. N-carbamoyl-D-amino acid hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. nitrogen compound metabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-carbamoyl-D-amino acid hydrolase (EC:3.5.1.77)
    Alternative name(s):
    D-N-alpha-carbamilase
    OrganismiAgrobacterium sp. (strain KNK712)
    Taxonomic identifieri252128 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304N-carbamoyl-D-amino acid hydrolasePRO_0000079800Add
    BLAST

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 129
    Helixi21 – 3717
    Beta strandi41 – 444
    Turni47 – 504
    Helixi54 – 563
    Helixi62 – 665
    Beta strandi69 – 746
    Turni76 – 783
    Helixi79 – 8810
    Beta strandi91 – 10212
    Beta strandi105 – 11511
    Beta strandi121 – 1266
    Beta strandi140 – 1423
    Helixi146 – 1494
    Beta strandi159 – 1624
    Beta strandi165 – 1695
    Helixi172 – 1765
    Helixi178 – 1869
    Beta strandi190 – 1967
    Helixi206 – 2116
    Helixi212 – 22716
    Beta strandi230 – 2367
    Beta strandi238 – 2403
    Beta strandi243 – 2453
    Beta strandi250 – 2523
    Beta strandi258 – 2614
    Beta strandi264 – 27512
    Helixi276 – 2794
    Helixi280 – 2834
    Turni284 – 2874
    Helixi289 – 2924
    Helixi295 – 2973
    Helixi299 – 3024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ERZX-ray1.70A/B2-304[»]
    1UF4X-ray2.15A/B2-304[»]
    1UF5X-ray1.60A/B2-304[»]
    1UF7X-ray1.90A/B2-304[»]
    1UF8X-ray1.80A/B2-304[»]
    ProteinModelPortaliP60327.
    SMRiP60327. Positions 2-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60327.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 299295CN hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

    Family and domain databases

    Gene3Di3.60.110.10. 1 hit.
    InterProiIPR003010. C-N_Hydrolase.
    [Graphical view]
    PfamiPF00795. CN_hydrolase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56317. SSF56317. 1 hit.
    PROSITEiPS50263. CN_HYDROLASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P60327-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRQMILAVG QQGPIARAET REQVVVRLLD MLTKAASRGA NFIVFPELAL    50
    TTFFPRWHFT DEAELDSFYE TEMPGPVVRP LFEKAAELGI GFNLGYAELV 100
    VEGGVKRRFN TSILVDKSGK IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF 150
    EPGDLGFPVY DVDAAKMGMF ICNDRRWPEA WRVMGLRGAE IICGGYNTPT 200
    HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME ENCMLLGHSC 250
    IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK QHRQPQHYGL 300
    IAEL 304
    Length:304
    Mass (Da):34,285
    Last modified:February 2, 2004 - v1
    Checksum:iC64290139C1C7E61
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007368 Genomic DNA. Translation: BAD00007.1.
    PIRiJW0082.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB007368 Genomic DNA. Translation: BAD00007.1 .
    PIRi JW0082.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ERZ X-ray 1.70 A/B 2-304 [» ]
    1UF4 X-ray 2.15 A/B 2-304 [» ]
    1UF5 X-ray 1.60 A/B 2-304 [» ]
    1UF7 X-ray 1.90 A/B 2-304 [» ]
    1UF8 X-ray 1.80 A/B 2-304 [» ]
    ProteinModelPortali P60327.
    SMRi P60327. Positions 2-304.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P60327.

    Family and domain databases

    Gene3Di 3.60.110.10. 1 hit.
    InterProi IPR003010. C-N_Hydrolase.
    [Graphical view ]
    Pfami PF00795. CN_hydrolase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56317. SSF56317. 1 hit.
    PROSITEi PS50263. CN_HYDROLASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme."
      Nanba H., Ikenaka Y., Yamada Y., Yajima K., Takano M., Takahashi S.
      Biosci. Biotechnol. Biochem. 62:875-881(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases."
      Nakai T., Hasegawa T., Yamashita E., Yamamoto M., Kumasaka T., Ueki T., Nanba H., Ikenaka Y., Takahashi S., Sato M., Tsukihara T.
      Structure 8:729-737(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).

    Entry informationi

    Entry nameiDCAS_AGRSK
    AccessioniPrimary (citable) accession number: P60327
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 2, 2004
    Last sequence update: February 2, 2004
    Last modified: October 1, 2014
    This is version 43 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

    Documents

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

    External Data

    Dasty 3