DCAS_RHIRD
ID DCAS_RHIRD Reviewed; 304 AA.
AC Q44185; Q44203;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=N-carbamoyl-D-amino acid hydrolase;
DE EC=3.5.1.77;
DE AltName: Full=D-N-alpha-carbamilase;
OS Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium
OS radiobacter).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC Agrobacterium tumefaciens complex.
OX NCBI_TaxID=358;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCRC 13814 / CECT 4067 / NRRL B-11291;
RX PubMed=8931327; DOI=10.1111/j.1574-6968.1996.tb08556.x;
RA Buson A., Negro A., Grassato L., Tagliaro M., Basaglia M., Grandi C.,
RA Fontana A., Nuti M.P.;
RT "Identification, sequencing and mutagenesis of the gene for a D-
RT carbamoylase from Agrobacterium radiobacter.";
RL FEMS Microbiol. Lett. 145:55-62(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BCRC 13814 / CECT 4067 / NRRL B-11291;
RA Grifantini R.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CHARACTERIZATION.
RC STRAIN=BCRC 13814 / CECT 4067 / NRRL B-11291;
RX PubMed=8621596; DOI=10.1074/jbc.271.16.9326;
RA Grifantini R., Pratesi C., Galli G., Grandi G.;
RT "Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid
RT amidohydrolase and their role in enzymatic activity.";
RL J. Biol. Chem. 271:9326-9331(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND MUTAGENESIS OF HIS-129; HIS-144
RP AND HIS-215.
RX PubMed=11237598; DOI=10.1006/jmbi.2000.4380;
RA Wang W.-C., Hsu W.-H., Chien F.-T., Chen C.-Y.;
RT "Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-
RT amino-acid amidohydrolase from Agrobacterium radiobacter reveals a
RT homotetramer and insight into a catalytic cleft.";
RL J. Mol. Biol. 306:251-261(2001).
CC -!- FUNCTION: The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino
CC acids to the corresponding which are useful intermediates in the
CC preparation of beta-lactam antibiotics. Industrial production of beta-
CC lactam antibiotics is now being developed using this enzyme.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-carbamoyl-D-amino acid + 2 H(+) + H2O = a D-alpha-amino
CC acid + CO2 + NH4(+); Xref=Rhea:RHEA:11000, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:59871, ChEBI:CHEBI:85602; EC=3.5.1.77;
CC -!- SUBUNIT: Homotetramer.
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DR EMBL; U59376; AAB47607.1; -; Genomic_DNA.
DR EMBL; X91070; CAA62550.1; -; Genomic_DNA.
DR PDB; 1FO6; X-ray; 1.95 A; A/B/C/D=1-304.
DR PDB; 2GGK; X-ray; 2.30 A; A/B/C/D=1-304.
DR PDB; 2GGL; X-ray; 2.40 A; A/B/C/D=1-304.
DR PDBsum; 1FO6; -.
DR PDBsum; 2GGK; -.
DR PDBsum; 2GGL; -.
DR AlphaFoldDB; Q44185; -.
DR SMR; Q44185; -.
DR EvolutionaryTrace; Q44185; -.
DR GO; GO:0047417; F:N-carbamoyl-D-amino acid hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase.
FT CHAIN 1..304
FT /note="N-carbamoyl-D-amino acid hydrolase"
FT /id="PRO_0000079801"
FT DOMAIN 5..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 47
FT /evidence="ECO:0000305|PubMed:11237598"
FT ACT_SITE 127
FT /evidence="ECO:0000305|PubMed:11237598"
FT ACT_SITE 172
FT /evidence="ECO:0000305|PubMed:11237598"
FT MUTAGEN 129
FT /note="H->A,N,R: No activity."
FT /evidence="ECO:0000269|PubMed:11237598"
FT MUTAGEN 144
FT /note="H->A: 5% activity of wild-type."
FT /evidence="ECO:0000269|PubMed:11237598"
FT MUTAGEN 215
FT /note="H->A: 17% activity of wild-type."
FT /evidence="ECO:0000269|PubMed:11237598"
FT CONFLICT 274
FT /note="V -> L (in Ref. 2; AAB47607)"
FT /evidence="ECO:0000305"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1FO6"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1FO6"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 212..226
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1FO6"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1FO6"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1FO6"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1FO6"
SQ SEQUENCE 304 AA; 34152 MW; 02436D8CEF925211 CRC64;
MTRQMILAVG QQGPIARAET REQVVGRLLD MLTNAASRGV NFIVFPELAL TTFFPRWHFT
DEAELDSFYE TEMPGPVVRP LFETAAELGI GFNLGYAELV VEGGVKRRFN TSILVDKSGK
IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF EPGDLGFPVY DVDAAKMGMF ICNDRRWPET
WRVMGLKGAE IICGGYNTPT HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME
EGCMLLGHSC IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK AHRQPQHYGL
IAEF
