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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: 3 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 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 – 129Combined sources
Helixi21 – 3717Combined sources
Beta strandi41 – 444Combined sources
Turni47 – 504Combined sources
Helixi54 – 563Combined sources
Helixi62 – 676Combined sources
Beta strandi69 – 746Combined sources
Turni76 – 783Combined sources
Helixi79 – 8810Combined sources
Beta strandi91 – 10212Combined sources
Beta strandi105 – 11511Combined sources
Beta strandi121 – 1266Combined sources
Beta strandi140 – 1423Combined sources
Helixi146 – 1494Combined sources
Beta strandi159 – 1624Combined sources
Beta strandi165 – 1695Combined sources
Helixi172 – 1765Combined sources
Helixi178 – 1869Combined sources
Beta strandi190 – 1967Combined sources
Helixi206 – 2116Combined sources
Helixi212 – 22615Combined sources
Beta strandi230 – 2367Combined sources
Beta strandi238 – 2403Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi250 – 2523Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 27512Combined sources
Helixi276 – 2794Combined sources
Helixi280 – 2834Combined sources
Turni284 – 2874Combined sources
Helixi289 – 2924Combined sources
Helixi295 – 2973Combined sources
Helixi299 – 3024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MTRQMILAVG QQGPIARAET REQVVGRLLD MLTNAASRGV NFIVFPELAL
60 70 80 90 100
TTFFPRWHFT DEAELDSFYE TEMPGPVVRP LFETAAELGI GFNLGYAELV
110 120 130 140 150
VEGGVKRRFN TSILVDKSGK IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF
160 170 180 190 200
EPGDLGFPVY DVDAAKMGMF ICNDRRWPET WRVMGLKGAE IICGGYNTPT
210 220 230 240 250
HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME EGCMLLGHSC
260 270 280 290 300
IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK AHRQPQHYGL

IAEF
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:
EMBLi
GenBanki
DDBJi
Links Updated
U59376 Genomic DNA. Translation: AAB47607.1.
X91070 Genomic DNA. Translation: CAA62550.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U59376 Genomic DNA. Translation: AAB47607.1 .
X91070 Genomic DNA. Translation: CAA62550.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 69 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