AMAB2_GEOSE
ID AMAB2_GEOSE Reviewed; 409 AA.
AC Q53389;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=N-carbamoyl-L-amino acid hydrolase {ECO:0000303|PubMed:7764340};
DE EC=3.5.1.87 {ECO:0000269|PubMed:22904279};
DE AltName: Full=L-carbamoylase {ECO:0000303|PubMed:7764340};
GN Name=amaB {ECO:0000303|PubMed:7764340};
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NS1122A;
RX PubMed=7764340; DOI=10.1271/bbb.57.1935;
RA Mukohara Y., Ishikawa T., Watabe K., Nakamura H.;
RT "Molecular cloning and sequencing of the gene for a thermostable N-
RT carbamyl-L-amino acid amidohydrolase from Bacillus stearothermophilus
RT strain NS1122A.";
RL Biosci. Biotechnol. Biochem. 57:1935-1937(1993).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 1-408 IN COMPLEX WITH COBALT,
RP MUTAGENESIS OF HIS-225; ARG-234; THR-261; ASN-273; ASP-284 AND ARG-286,
RP SUBUNIT, COFACTOR, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=22904279; DOI=10.1128/jb.01056-12;
RA Martinez-Rodriguez S., Garcia-Pino A., Las Heras-Vazquez F.J.,
RA Clemente-Jimenez J.M., Rodriguez-Vico F., Garcia-Ruiz J.M., Loris R.,
RA Gavira J.A.;
RT "Mutational and structural analysis of L-N-carbamoylase reveals new
RT insights into a peptidase M20/M25/M40 family member.";
RL J. Bacteriol. 194:5759-5768(2012).
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:22904279};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22904279};
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:0000269|PubMed:22904279};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000250|UniProtKB:Q8VXY9};
CC -!- ACTIVITY REGULATION: Ni(2+) and Co(2+) ions greatly increase hydrolase
CC activity. {ECO:0000269|PubMed:22904279}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22904279}.
CC -!- INTERACTION:
CC Q53389; Q53389: amaB; NbExp=3; IntAct=EBI-6421173, EBI-6421173;
CC -!- SIMILARITY: Belongs to the peptidase M20 family. {ECO:0000305}.
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DR EMBL; S67784; AAC60456.1; -; Genomic_DNA.
DR PIR; JN0885; JN0885.
DR PDB; 3N5F; X-ray; 2.75 A; A/B=1-408.
DR PDBsum; 3N5F; -.
DR AlphaFoldDB; Q53389; -.
DR SMR; Q53389; -.
DR BRENDA; 3.5.1.87; 623.
DR GO; GO:0050897; F:cobalt ion binding; IDA:UniProtKB.
DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IDA:UniProtKB.
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 3D-structure; Hydrolase; Manganese; Metal-binding.
FT CHAIN 1..409
FT /note="N-carbamoyl-L-amino acid hydrolase"
FT /id="PRO_0000061953"
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:0000269|PubMed:22904279"
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:0000269|PubMed:22904279,
FT ECO:0007744|PDB:3N5F"
FT BINDING 90
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:22904279,
FT ECO:0007744|PDB:3N5F"
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:0000269|PubMed:22904279,
FT ECO:0007744|PDB:3N5F"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22904279"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22904279"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22904279"
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:0000269|PubMed:22904279"
FT MUTAGEN 225
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22904279"
FT MUTAGEN 234
FT /note="R->A: Loss of activity and impaired dimerization."
FT /evidence="ECO:0000269|PubMed:22904279"
FT MUTAGEN 261
FT /note="T->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22904279"
FT MUTAGEN 273
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22904279"
FT MUTAGEN 284
FT /note="D->E: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22904279"
FT MUTAGEN 286
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:22904279"
FT HELIX 4..15
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 16..18
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 32..48
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 92..107
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 127..130
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 158..164
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 169..175
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 182..190
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 211..220
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 237..255
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 259..269
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 290..311
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 314..323
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 330..343
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 349..354
FT /evidence="ECO:0007829|PDB:3N5F"
FT TURN 357..364
FT /evidence="ECO:0007829|PDB:3N5F"
FT STRAND 367..372
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:3N5F"
FT HELIX 388..405
FT /evidence="ECO:0007829|PDB:3N5F"
SQ SEQUENCE 409 AA; 44249 MW; 332515C62A1A2F31 CRC64;
MIQGERLWQR LMELGEVGKQ PSGGVTRLSF TAEERRAKDL VASYMREAGL FVYEDAAGNL
IGRKEGTNPD ATVVLVGSHL DSVYNGGCFD GPLGVLAGVE VVQTMNEHGV VTHHPIEVVA
FTDEEGARFR FGMIGSRAMA GTLPPEALEC RDAEGISLAE AMKQAGLDPD RLPQAARKPG
TVKAYVELHI EQGRVLEETG LPVGIVTGIA GLIWVKFTIE GKAEHAGATP MSLRRDPMAA
AAQIIIVIEE EARRTGTTVG TVGQLHVYPG GINVIPERVE FVLDLRDLKA EVRDQVWKAI
AVRAETIAKE RNVRVTTERL QEMPPVLCSD EVKRAAEAAC QKLGYPSFWL PSGAAHDSVQ
LAPICPIGMI FVRSQDGVSH SPAEWSTKED CAAGAEVLYH TVWQLAQGE
