Q44185 (DCAS_RHIRD) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: N-carbamoyl-D-amino acid hydrolase EC=3.5.1.77 Alternative name(s): D-N-alpha-carbamilase
Organism	Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Taxonomic identifier	358 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium › Agrobacterium tumefaciens complex

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	N-carbamoyl-D-amino acid + H2O = D-amino acid + NH3 + CO2.
Subunit structure	Homotetramer.
Sequence similarities	Contains 1 CN hydrolase domain.

Ontologies

Keywords
Molecular function	Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological_process	nitrogen compound metabolic process Inferred from electronic annotation. Source: InterPro
Molecular_function	N-carbamoyl-D-amino acid hydrolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 304

304

N-carbamoyl-D-amino acid hydrolase

PRO_0000079801

Regions

Domain

5 – 299

295

CN hydrolase

Sites

Active site

47

1

Active site

127

1

Active site

172

1

Experimental info

Mutagenesis

129

1

H → A, N or R: No activity. Ref.4

Mutagenesis

144

1

H → A: 5% activity of wild-type. Ref.4

Mutagenesis

215

1

H → A: 17% activity of wild-type. Ref.4

Sequence conflict

274

1

V → L in AAB47607. Ref.2

Secondary structure

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304

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

21 – 37

17

Beta strand

41 – 44

4

Turn

47 – 50

4

Helix

54 – 56

3

Helix

62 – 67

6

Beta strand

69 – 74

6

Turn

76 – 78

3

Helix

79 – 88

10

Beta strand

91 – 102

12

Beta strand

105 – 115

11

Beta strand

121 – 126

6

Beta strand

140 – 142

3

Helix

146 – 149

4

Beta strand

159 – 162

4

Beta strand

165 – 169

5

Helix

172 – 176

5

Helix

178 – 186

9

Beta strand

190 – 196

7

Helix

206 – 211

6

Helix

212 – 226

15

Beta strand

230 – 236

7

Beta strand

238 – 240

3

Beta strand

243 – 245

3

Beta strand

250 – 252

3

Beta strand

258 – 261

4

Beta strand

264 – 275

12

Helix

276 – 279

4

Helix

280 – 283

4

Turn

284 – 287

4

Helix

289 – 292

4

Helix

295 – 297

3

Helix

299 – 302

4

Sequences

	Sequence		Length	Mass (Da)
	Q44185 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 02436D8CEF925211	FASTA	304	34,152
	10 20 30 40 50 60 MTRQMILAVG QQGPIARAET REQVVGRLLD MLTNAASRGV NFIVFPELAL TTFFPRWHFT 70 80 90 100 110 120 DEAELDSFYE TEMPGPVVRP LFETAAELGI GFNLGYAELV VEGGVKRRFN TSILVDKSGK 130 140 150 160 170 180 IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF EPGDLGFPVY DVDAAKMGMF ICNDRRWPET 190 200 210 220 230 240 WRVMGLKGAE IICGGYNTPT HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME 250 260 270 280 290 300 EGCMLLGHSC IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK AHRQPQHYGL IAEF

References

[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U59376 Genomic DNA. Translation: AAB47607.1.
X91070 Genomic DNA. Translation: CAA62550.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q44185.

SMR

Q44185. Positions 3-304.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

3.60.110.10. 1 hit.

InterPro

IPR003010. C-N_Hydrolase.
[Graphical view]

Pfam

PF00795. CN_hydrolase. 1 hit.
[Graphical view]

SUPFAM

SSF56317. Ntlse/CNhydtse. 1 hit.

PROSITE

PS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q44185.

Entry information

Entry name

DCAS_RHIRD

Accession

Primary (citable) accession number: Q44185
Secondary accession number(s): Q44203

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2003
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program