ID Q2B3T5_9BACI Unreviewed; 413 AA.
AC Q2B3T5;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=N-carbamoyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:EAR64445.1};
GN ORFNames=B14911_15705 {ECO:0000313|EMBL:EAR64445.1};
OS Bacillus sp. NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=313627 {ECO:0000313|EMBL:EAR64445.1, ECO:0000313|Proteomes:UP000004554};
RN [1] {ECO:0000313|EMBL:EAR64445.1, ECO:0000313|Proteomes:UP000004554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:EAR64445.1,
RC ECO:0000313|Proteomes:UP000004554};
RA Siefert J., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001235-1};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR001235-
CC 1};
CC -!- SIMILARITY: Belongs to the peptidase M20 family.
CC {ECO:0000256|ARBA:ARBA00006153}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAR64445.1}.
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; AAOX01000024; EAR64445.1; -; Genomic_DNA.
DR RefSeq; WP_009791830.1; NZ_CH672355.1.
DR AlphaFoldDB; Q2B3T5; -.
DR GeneID; 85551046; -.
DR HOGENOM; CLU_024588_6_0_9; -.
DR Proteomes; UP000004554; Unassembled WGS sequence.
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 CDD; cd03884; M20_bAS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR010158; Amidase_Cbmase.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF001235; Amidase_carbamoylase; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:EAR64445.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..311
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 413 AA; 44162 MW; AE709613D39F7BF8 CRC64;
MSLVKEQLAA RIEKHIEALS HFTATPGKGT TRLTYSPEDL QARNYIKGKM KEIGLEVTED
GLGNIFGKLE GTLEDAPSVL IGSHFDSVPN GGSYDGPAGV VAGLEVAALF AENNVKPKYP
LEVIAMVEEE GSRFGGGLMG SRGITGLMSE TEFFKLADRD GVLAKDAMEK IGLDPSLPKQ
RDPKTIKAFL ELHIEQGPIL EEKGIPIGVV EAIVGLTQLE VTVKGQAGHA GTTPMDRRSD
ALAAAAAIIA GLSGLAEAEG EGSVLTVGRL NVFPNGANVI PDKVVFSVDI RSGKEEHVLN
MVEKVKERIG SYDGGGIQTS VEQPLYMKPK AMNEEILTLF KEKSAQLNIP YCPINSGAGH
DAMVLSDFTD VGMLFIPSRN GLSHCPEEWS DSKDIAKAVE IFYEAAKKLT EAE
//
