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P60327

- DCAS_AGRSK

UniProt

P60327 - DCAS_AGRSK

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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

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
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.

Miscellaneous databases

EvolutionaryTraceiP60327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 299295CN hydrolaseAdd
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.

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 16, 2013
This is version 42 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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