ID A0A1G8BYF5_9RHOO Unreviewed; 418 AA.
AC A0A1G8BYF5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:SDH38256.1};
GN ORFNames=SAMN05660652_01629 {ECO:0000313|EMBL:SDH38256.1};
OS Propionivibrio dicarboxylicus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Propionivibrio.
OX NCBI_TaxID=83767 {ECO:0000313|EMBL:SDH38256.1, ECO:0000313|Proteomes:UP000198607};
RN [1] {ECO:0000313|EMBL:SDH38256.1, ECO:0000313|Proteomes:UP000198607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5885 {ECO:0000313|EMBL:SDH38256.1,
RC ECO:0000313|Proteomes:UP000198607};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNCY01000005; SDH38256.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8BYF5; -.
DR STRING; 83767.SAMN05660652_01629; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000198607; 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 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 NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE DEIMINASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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:SDH38256.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198607};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 418 AA; 45372 MW; 1D7432CA8BA5D292 CRC64;
MDTKTLRPIA EKLFDDIRAL SFDGVGVSRD SYGTKETATA DFLRAFATDA GFKVSADRAG
NLVIGFADTP ADAPTIWCGS HIDSVPQGGN FDGLAGVVAG LLCLLEQQRS GVRSPIPLQV
LGFRGEESAW FGKAYVGSGA LLGQLEAEDL ALRHRDSGET LGQCMERIGA DMEAIAAQRL
LFDPKKVRAF LELHIEQGPV MEARKLPVAV VSGIRGNIRH NHVQCFGASG HSGAIPRWLR
RDAMFAVADL IMRVDEHWSE LLERGTDLVV TTGMLSTNAA EHAASRIPGH VKFSFEVRSK
SIDTLEAFYQ LMRAECTAIS RERQVRFEFD RRILSSPATM DPSLCTLLSK VCTELGTPFE
VLPSGAGHDA SMFANAGIPS GMVFVRNQNG SHNPEEAMDI GDFMAGVQVL HQGIQEIR
//
