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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: 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 Publication1
Active sitei1271 Publication1
Active sitei1721 Publication1

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
OrganismiRhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Taxonomic identifieri358 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacteriumAgrobacterium tumefaciens complex

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi129H → A, N or R: No activity. 1 Publication1
Mutagenesisi144H → A: 5% activity of wild-type. 1 Publication1
Mutagenesisi215H → A: 17% activity of wild-type. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000798011 – 304N-carbamoyl-D-amino acid hydrolaseAdd BLAST304

Interactioni

Subunit structurei

Homotetramer.

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 – 67Combined sources6
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 – 226Combined sources15
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
1FO6X-ray1.95A/B/C/D1-304[»]
2GGKX-ray2.30A/B/C/D1-304[»]
2GGLX-ray2.40A/B/C/D1-304[»]
ProteinModelPortaliQ44185.
SMRiQ44185.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ44185.

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti274V → L in AAB47607 (Ref. 2) Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ44185.

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_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 2, 2016
This is version 74 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.