AMAB1_GEOSE
ID AMAB1_GEOSE Reviewed; 409 AA.
AC P37113; P94345;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=N-carbamoyl-L-amino acid hydrolase;
DE EC=3.5.1.87 {ECO:0000269|PubMed:9023955};
DE AltName: Full=L-carbamoylase {ECO:0000303|PubMed:9023955};
GN Name=amaB {ECO:0000303|PubMed:9023955};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=9023955; DOI=10.1128/aem.63.2.763-766.1997;
RA Batisse N., Weigel P., Lecocq M., Sakanyan V.;
RT "Two amino acid amidohydrolase genes encoding L-stereospecific carbamoylase
RT and aminoacylase are organized in a common operon in Bacillus
RT stearothermophilus.";
RL Appl. Environ. Microbiol. 63:763-766(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-409.
RC STRAIN=NCIMB 8224 / CCM 2186 / NCA C-1235.1 / VKM B-718;
RX PubMed=8285691; DOI=10.1128/aem.59.11.3878-3888.1993;
RA Sakanyan V., Desmarez L., Legrain C., Charlier D.R.M., Mett I.,
RA Kochikyan A., Savchenko A., Boyen A., Falmagne P., Pirard A.,
RA Glansdorff N.;
RT "Gene cloning, sequence analysis, purification, and characterization of a
RT thermostable aminoacylase from Bacillus stearothermophilus.";
RL Appl. Environ. Microbiol. 59:3878-3888(1993).
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:9023955};
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}.
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DR EMBL; Y08752; CAA69999.1; -; Genomic_DNA.
DR EMBL; X74289; CAA52341.1; -; Genomic_DNA.
DR AlphaFoldDB; P37113; -.
DR SMR; P37113; -.
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 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 Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..409
FT /note="N-carbamoyl-L-amino acid hydrolase"
FT /id="PRO_0000061952"
FT REGION 124..125
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 189..192
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 211..324
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT REGION 355..356
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 79
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 125
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 189
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 380
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT BINDING 380
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q8VXY9"
FT SITE 234
FT /note="Necessary for dimerization"
FT /evidence="ECO:0000250|UniProtKB:Q53389"
FT CONFLICT 60..62
FT /note="LIG -> DRE (in Ref. 2; CAA52341)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 44167 MW; 9A91F767C9AEFBBB CRC64;
MIQGERLWQR LMELGEVGKQ PSGGVTRLSF TAEERRAKDL VASYMREAGL FVYEDAAGNL
IGRKEGTNPD ATVVLVGSHL DSVYNGGCFD GPLGVLAGVE VVQTMNEHGV VTHHPIEVVA
FTDEEGARFR FGMIGSRAMA GTLPPEALEC RDAEGISLAE AMKQAGLDPD RLPQAARKPG
TVKAYVELHI EQGRVLEEAG LPVGIVTGIA GLIWVKFTIA GPAEHAGATP MSLRRDPMAA
AAQIIIVIEE EARRTGTTVG TVGQLHVYPG GINVIPERVE FVLDLRDLKA EVRDQVWKAI
AVRAETIAKE RNVRLTTERL QEMAPVLCSE VVKQAAERAC KQLGYPPFWL PSGAAHDGVQ
LAPICPIGMI FVRSQDGVSH SPAEWSTKED CAVGAEVLYH TVWQLAQGE
