Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q44185

- DCAS_RHIRD

UniProt

Q44185 - DCAS_RHIRD

Protein

N-carbamoyl-D-amino acid hydrolase

Gene
N/A
Organism
Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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
    OrganismiRhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
    Taxonomic identifieri358 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi129 – 1291H → A, N or R: No activity. 1 Publication
    Mutagenesisi144 – 1441H → A: 5% activity of wild-type. 1 Publication
    Mutagenesisi215 – 2151H → A: 17% activity of wild-type. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 304304N-carbamoyl-D-amino acid hydrolasePRO_0000079801Add
    BLAST

    Interactioni

    Subunit structurei

    Homotetramer.

    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 – 676
    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 – 22615
    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
    1FO6X-ray1.95A/B/C/D1-304[»]
    2GGKX-ray2.30A/B/C/D1-304[»]
    2GGLX-ray2.40A/B/C/D1-304[»]
    ProteinModelPortaliQ44185.
    SMRiQ44185. Positions 3-304.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ44185.

    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.

    Q44185-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRQMILAVG QQGPIARAET REQVVGRLLD MLTNAASRGV NFIVFPELAL    50
    TTFFPRWHFT DEAELDSFYE TEMPGPVVRP LFETAAELGI GFNLGYAELV 100
    VEGGVKRRFN TSILVDKSGK IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF 150
    EPGDLGFPVY DVDAAKMGMF ICNDRRWPET WRVMGLKGAE IICGGYNTPT 200
    HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME EGCMLLGHSC 250
    IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK AHRQPQHYGL 300
    IAEF 304
    Length:304
    Mass (Da):34,152
    Last modified:November 1, 1996 - v1
    Checksum:i02436D8CEF925211
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti274 – 2741V → L in AAB47607. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59376 Genomic DNA. Translation: AAB47607.1.
    X91070 Genomic DNA. Translation: CAA62550.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59376 Genomic DNA. Translation: AAB47607.1 .
    X91070 Genomic DNA. Translation: CAA62550.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FO6 X-ray 1.95 A/B/C/D 1-304 [» ]
    2GGK X-ray 2.30 A/B/C/D 1-304 [» ]
    2GGL X-ray 2.40 A/B/C/D 1-304 [» ]
    ProteinModelPortali Q44185.
    SMRi Q44185. Positions 3-304.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei Q44185.

    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. "Identification, sequencing and mutagenesis of the gene for a D-carbamoylase from Agrobacterium radiobacter."
      Buson A., Negro A., Grassato L., Tagliaro M., Basaglia M., Grandi C., Fontana A., Nuti M.P.
      FEMS Microbiol. Lett. 145:55-62(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NRRL B-11291.
    2. Grifantini R.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: NRRL B-11291.
    3. "Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid amidohydrolase and their role in enzymatic activity."
      Grifantini R., Pratesi C., Galli G., Grandi G.
      J. Biol. Chem. 271:9326-9331(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Strain: NRRL B-11291.
    4. "Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft."
      Wang W.-C., Hsu W.-H., Chien F.-T., Chen C.-Y.
      J. Mol. Biol. 306:251-261(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), MUTAGENESIS OF HIS-129; HIS-144 AND HIS-215.

    Entry informationi

    Entry nameiDCAS_RHIRD
    AccessioniPrimary (citable) accession number: Q44185
    Secondary accession number(s): Q44203
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 68 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