Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P60327

- DCAS_AGRSK

UniProt

P60327 - DCAS_AGRSK

(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)

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 – 129Combined sources
Helixi21 – 3717Combined sources
Beta strandi41 – 444Combined sources
Turni47 – 504Combined sources
Helixi54 – 563Combined sources
Helixi62 – 665Combined 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 – 22716Combined 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:
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

        10         20         30         40         50
MTRQMILAVG QQGPIARAET REQVVVRLLD MLTKAASRGA NFIVFPELAL
60 70 80 90 100
TTFFPRWHFT DEAELDSFYE TEMPGPVVRP LFEKAAELGI GFNLGYAELV
110 120 130 140 150
VEGGVKRRFN TSILVDKSGK IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF
160 170 180 190 200
EPGDLGFPVY DVDAAKMGMF ICNDRRWPEA WRVMGLRGAE IICGGYNTPT
210 220 230 240 250
HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME ENCMLLGHSC
260 270 280 290 300
IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK QHRQPQHYGL

IAEL
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 29, 2014
This is version 44 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