HYUC_PSESN
ID HYUC_PSESN Reviewed; 414 AA.
AC Q01264;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000305|PubMed:1732229};
DE EC=3.5.1.87 {ECO:0000250|UniProtKB:Q6DTN4};
DE AltName: Full=Hydantoin utilization protein C {ECO:0000303|PubMed:1732229};
DE AltName: Full=L-N-carbamoylase {ECO:0000305|PubMed:1732229};
GN Name=hyuC {ECO:0000303|PubMed:1732229};
OS Pseudomonas sp. (strain NS671).
OG Plasmid pHN671.
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=29441;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, FUNCTION,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=NS671;
RX PubMed=1732229; DOI=10.1128/jb.174.3.962-969.1992;
RA Watabe K.;
RT "Cloning and sequencing of the genes involved in the conversion of 5-
RT substituted hydantoins to the corresponding L-amino acids from the native
RT plasmid of Pseudomonas sp. strain NS671.";
RL J. Bacteriol. 174:962-969(1992).
CC -!- FUNCTION: Involved in the asymmetric conversion of racemic 5-
CC substituted hydantoins to the corresponding L-amino acids. Catalyzes
CC the conversion of N-carbamoyl-L-methionine to L-methionine in an
CC irreversible reaction. Unable to convert N-carbamoyl-D-methionine.
CC {ECO:0000269|PubMed:1732229}.
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:0000250|UniProtKB:Q6DTN4};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q8VXY9};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000250|UniProtKB:Q6DTN4};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:Q53389};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q8VXY9};
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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; D10494; BAA01379.1; -; Genomic_DNA.
DR EMBL; M72717; AAA25847.1; -; Genomic_DNA.
DR AlphaFoldDB; Q01264; -.
DR SMR; Q01264; -.
DR MEROPS; M20.A07; -.
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; IDA:UniProtKB.
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 InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR32494; PTHR32494; 1.
DR Pfam; PF07687; M20_dimer; 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; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Plasmid.
FT CHAIN 1..414
FT /note="N-carbamoyl-L-amino-acid hydrolase"
FT /id="PRO_0000061955"
FT REGION 128..129
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 195..198
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 217..332
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 363..364
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 83
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 94
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 129
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 195
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 294
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 388
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 388
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT SITE 240
FT /note="Necessary for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q53389"
SQ SEQUENCE 414 AA; 45683 MW; B2DCDE7CEA81977C CRC64;
MKTVTISKER LRIHIEQLGE IGKTKDKGVQ RLALSKEDRE ATLLVSEWMR EAGLTVTHDH
FGNLIGRKEG ETPSLPSVMI GSHIDSVRNG GKFDGVIGVL AGIEIVHAIS EANVVHEHSI
EVVAFCEEEG SRFNDGLFGS RGMVGKVKPE DLQKVDDNNV TRYEALKTFG FGIDPDFTHQ
SIREIGDIKH YFEMHIEQGP YLEKNNYPIG IVSGIAGPSW FKVRLVGEAG HAGTVPMSLR
KDPLVGAAEV IKEVETLCMN DPNAPTVGTV GRIAAFPGGS NIIPESVEFT LDIRDIELER
RNKIIEKIEE KIKLVSNTRG LEYQIEKNMA AVPVKCSENL INSLKQSCKE LEIDAPIIVS
GAGHDAMFLA EITEIGMVFV RCRNGISHSP KEWAEIDDIL TGTKVLYESI IKHI
