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Q44185

- DCAS_RHIRD

UniProt

Q44185 - DCAS_RHIRD

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Protein
N-carbamoyl-D-amino acid hydrolase
Gene
N/A
Organism
Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 hydrolase
PRO_0000079801Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ44185.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 299295CN hydrolase
Add
BLAST

Sequence similaritiesi

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

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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

Sequence conflict

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

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: June 11, 2014
This is version 67 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

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