HYUC_PAEAU
ID HYUC_PAEAU Reviewed; 412 AA.
AC Q9F464;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000305};
DE EC=3.5.1.87 {ECO:0000269|PubMed:10194852};
DE AltName: Full=L-N-carbamoylase {ECO:0000303|PubMed:10194852};
GN Name=hyuC {ECO:0000303|PubMed:10194852};
OS Paenarthrobacter aurescens (Arthrobacter aurescens).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=43663;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 3747;
RX PubMed=10194852; DOI=10.1016/s0168-1656(98)00183-7;
RA Wilms B., Wiese A., Syldatk C., Mattes R., Altenbuchner J., Pietzsch M.;
RT "Cloning, nucleotide sequence and expression of a new L-N-carbamoylase gene
RT from Arthrobacter aurescens DSM 3747 in E. coli.";
RL J. Biotechnol. 68:101-113(1999).
RN [2]
RP BIOTECHNOLOGY.
RC STRAIN=DSM 3747;
RX PubMed=11339957; DOI=10.1016/s0141-0229(01)00311-8;
RA Ragnitz K., Syldatk C., Pietzsch M.;
RT "Optimization of the immobilization parameters and operational stability of
RT immobilized hydantoinase and L-N-carbamoylase from Arthrobacter aurescens
RT for the production of optically pure l-amino acids.";
RL Enzyme Microb. Technol. 28:713-720(2001).
CC -!- FUNCTION: Involved in the asymmetric conversion of racemic 5-
CC substituted hydantoins to the corresponding L-amino acids. Prefers L-
CC carbamoyl-L-tryptophan and N-carbamoyl-L-tyrosine. Has weaker activity
CC with N-carbamoyl-D,L-phenylalanine and N-carbamoyl-L-thienyalanine.
CC Carbamoyl derivatives of beta-alanine and charged aliphatic amino acids
CC are not accepted as substrates. {ECO:0000269|PubMed:10194852}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-carbamoyl-L-alpha-amino acid + 2 H(+) + H2O = an L-alpha-
CC amino acid + CO2 + NH4(+); Xref=Rhea:RHEA:17581, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58865, ChEBI:CHEBI:59869; EC=3.5.1.87;
CC Evidence={ECO:0000269|PubMed:10194852};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:Q8VXY9};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q8VXY9};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 5.1 sec(-1) with L-carbamoyl-L-tryptophan as substrate.
CC kcat is 6.5 sec(-1) with N-carbamoyl-L-tyrosine as substrate. kcat is
CC 5.0 sec(-1) with N-carbamoyl-D,L-phenylalanine as substrate. kcat is
CC 16.1 sec(-1) with N-carbamoyl-L-thienyalanine as substrate.
CC {ECO:0000269|PubMed:10194852};
CC pH dependence:
CC Optimum pH is 8.5. {ECO:0000269|PubMed:10194852};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:10194852};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10194852}.
CC -!- BIOTECHNOLOGY: Can be used for the industrial production of optically
CC pure L-amino acids. {ECO:0000269|PubMed:11339957}.
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; AF146701; AAG02131.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9F464; -.
DR SMR; Q9F464; -.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008652; P:cellular amino acid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01879; hydantase; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Hydrolase; Metal-binding.
FT CHAIN 1..412
FT /note="N-carbamoyl-L-amino-acid hydrolase"
FT /id="PRO_0000449272"
FT REGION 127..128
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 193..196
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 360..361
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 82
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 93
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 128
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 193
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 385
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT SITE 238
FT /note="Necessary for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q53389"
SQ SEQUENCE 412 AA; 44084 MW; 6E8B76F923FBA2CA CRC64;
MTLQKAQAER IEKEIRELSR FSAEGPGVTR LTYTPEHAAA RETLIAAMKA AALSVREDAL
GNIIGRREGT DPELPAIAVG SHFDSVRNGG MFDGTAGVVC ALEAARVMLE NGYVNRHPFE
FIAIVEEEGA RFSSGMLGGR AIAGLVADRE LDSLVDEDGV SVRQAATAFG LKPGELQAAA
RSAADLRAFI ELHIEQGPIL EQEQIEIGVV TSIVGVRALR VAVKGRSDHA GTTPMHLRQD
ALVPAALMVR EVNRFVNEIA DGTVATVGHL TVAPGGGNQV PGEVDFTLDL RSPHEESLRV
LIDRISVMVG EVASQAGVAA DVDEFFNLSP VQLAPTMVDA VREAASALQF THRDISSGAG
HDSMFIAQVT DVGMVFVPSR AGRSHVPEEW TDFDDLRKGT EVVLRVMKAL DR
