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 27-MAR-2024, entry version 66. 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; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Rhizobium/Agrobacterium group; 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; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 CDD; cd07569; DCase; 1. DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1. DR InterPro; IPR003010; C-N_Hydrolase. DR InterPro; IPR036526; C-N_Hydrolase_sf. DR PANTHER; PTHR43674:SF12; CN HYDROLASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR43674; NITRILASE C965.09-RELATED; 1. DR Pfam; PF00795; CN_hydrolase; 1. DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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 //