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Protein

N-carbamoyl-D-amino acid hydrolase

Gene
N/A
Organism
Agrobacterium sp. (strain KNK712)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei471
Active sitei1271
Active sitei1721

GO - Molecular functioni

GO - Biological processi

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000798001 – 304N-carbamoyl-D-amino acid hydrolaseAdd BLAST304

Structurei

Secondary structure

1304
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Helixi21 – 37Combined sources17
Beta strandi41 – 44Combined sources4
Turni47 – 50Combined sources4
Helixi54 – 56Combined sources3
Helixi62 – 66Combined sources5
Beta strandi69 – 74Combined sources6
Turni76 – 78Combined sources3
Helixi79 – 88Combined sources10
Beta strandi91 – 102Combined sources12
Beta strandi105 – 115Combined sources11
Beta strandi121 – 126Combined sources6
Beta strandi140 – 142Combined sources3
Helixi146 – 149Combined sources4
Beta strandi159 – 162Combined sources4
Beta strandi165 – 169Combined sources5
Helixi172 – 176Combined sources5
Helixi178 – 186Combined sources9
Beta strandi190 – 196Combined sources7
Helixi206 – 211Combined sources6
Helixi212 – 227Combined sources16
Beta strandi230 – 236Combined sources7
Beta strandi238 – 240Combined sources3
Beta strandi243 – 245Combined sources3
Beta strandi250 – 252Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi264 – 275Combined sources12
Helixi276 – 279Combined sources4
Helixi280 – 283Combined sources4
Turni284 – 287Combined sources4
Helixi289 – 292Combined sources4
Helixi295 – 297Combined sources3
Helixi299 – 302Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60327.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 299CN hydrolasePROSITE-ProRule annotationAdd BLAST295

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:
EMBLi
GenBanki
DDBJi
Links Updated
AB007368 Genomic DNA. Translation: BAD00007.1.
PIRiJW0082.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB007368 Genomic DNA. Translation: BAD00007.1.
PIRiJW0082.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP60327.

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]
ProtoNetiSearch...

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: November 2, 2016
This is version 48 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.