DCAS_AGRSK
ID DCAS_AGRSK Reviewed; 304 AA.
AC P60327;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 02-FEB-2004, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=N-carbamoyl-D-amino acid hydrolase;
DE EC=3.5.1.77;
DE AltName: Full=D-N-alpha-carbamilase;
OS Agrobacterium sp. (strain KNK712).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC unclassified Agrobacterium.
OX NCBI_TaxID=252128;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9648217; DOI=10.1271/bbb.62.875;
RA Nanba H., Ikenaka Y., Yamada Y., Yajima K., Takano M., Takahashi S.;
RT "Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-
RT amino acid amidohydrolase, cloning of the gene for this enzyme, and
RT properties of the enzyme.";
RL Biosci. Biotechnol. Biochem. 62:875-881(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=10903946; DOI=10.1016/s0969-2126(00)00160-x;
RA Nakai T., Hasegawa T., Yamashita E., Yamamoto M., Kumasaka T., Ueki T.,
RA Nanba H., Ikenaka Y., Takahashi S., Sato M., Tsukihara T.;
RT "Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel
RT catalytic framework common to amidohydrolases.";
RL Structure 8:729-737(2000).
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;
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DR EMBL; AB007368; BAD00007.1; -; Genomic_DNA.
DR PIR; JW0082; JW0082.
DR PDB; 1ERZ; X-ray; 1.70 A; A/B=2-304.
DR PDB; 1UF4; X-ray; 2.15 A; A/B=2-304.
DR PDB; 1UF5; X-ray; 1.60 A; A/B=2-304.
DR PDB; 1UF7; X-ray; 1.90 A; A/B=2-304.
DR PDB; 1UF8; X-ray; 1.80 A; A/B=2-304.
DR PDBsum; 1ERZ; -.
DR PDBsum; 1UF4; -.
DR PDBsum; 1UF5; -.
DR PDBsum; 1UF7; -.
DR PDBsum; 1UF8; -.
DR AlphaFoldDB; P60327; -.
DR SMR; P60327; -.
DR DrugBank; DB04058; N-Carbamoylphenylalanine.
DR DrugBank; DB03364; N-Carbamyl-D-Methionine.
DR DrugBank; DB01847; N-Carbamyl-D-Valine.
DR EvolutionaryTrace; P60327; -.
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_0000079800"
FT DOMAIN 5..276
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 47
FT ACT_SITE 127
FT ACT_SITE 172
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 21..37
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1UF5"
FT TURN 47..50
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:1UF5"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 91..102
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:1UF4"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 172..176
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 212..227
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1UF5"
FT STRAND 264..275
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 276..279
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1UF5"
FT TURN 284..287
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:1UF5"
FT HELIX 299..302
FT /evidence="ECO:0007829|PDB:1UF5"
SQ SEQUENCE 304 AA; 34285 MW; C64290139C1C7E61 CRC64;
MTRQMILAVG QQGPIARAET REQVVVRLLD MLTKAASRGA NFIVFPELAL TTFFPRWHFT
DEAELDSFYE TEMPGPVVRP LFEKAAELGI GFNLGYAELV VEGGVKRRFN TSILVDKSGK
IVGKYRKIHL PGHKEYEAYR PFQHLEKRYF EPGDLGFPVY DVDAAKMGMF ICNDRRWPEA
WRVMGLRGAE IICGGYNTPT HNPPVPQHDH LTSFHHLLSM QAGSYQNGAW SAAAGKVGME
ENCMLLGHSC IVAPTGEIVA LTTTLEDEVI TAAVDLDRCR ELREHIFNFK QHRQPQHYGL
IAEL
