ID A0A0P1GVG6_9RHOB Unreviewed; 397 AA.
AC A0A0P1GVG6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=N-carbamoyl-L-amino acid hydrolase {ECO:0000313|EMBL:CUH86809.1};
DE EC=3.5.1.87 {ECO:0000313|EMBL:CUH86809.1};
GN Name=amaB_2 {ECO:0000313|EMBL:CUH86809.1};
GN ORFNames=PH5382_00722 {ECO:0000313|EMBL:CUH86809.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH86809.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH86809.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH86809.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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; CYSG01000002; CUH86809.1; -; Genomic_DNA.
DR RefSeq; WP_058332962.1; NZ_CYSG01000002.1.
DR AlphaFoldDB; A0A0P1GVG6; -.
DR STRING; 1712645.PH5382_00722; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000050782; 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 GO; GO:0050538; F:N-carbamoyl-L-amino-acid hydrolase activity; IEA:UniProtKB-EC.
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 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:CUH86809.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 397 AA; 42025 MW; E0073A333ABE1AD1 CRC64;
MALNPARFLE DLHQLRSFGA SGVDKGVVRP AFTVVDIAAR RWLASRMQEA GLTVHLDPIG
NLFGLNGEKS LLIGSHSDSQ PEGGWLDGAL GVVAGLEIAR ASKEDGGPPI SVANFQDEEG
RFGILTGSDV WTGNATLAEA DRFTDTDGLT LGAARARMSG RAKEFLPHEM FSGFIEMHIE
QGPGMDVSGN QIGVVSDIVG IREIRIKICG RQNHAGTTPM ALRQDAFQAL SDFNQRINVA
FGALATPATV WTLGHAEISP NASSVVPGTA RFSLQWRDGD PGRLSRMGKA VQEIAEAISQ
ERGVTVELGD IGGIEPAAMD ARLKGALQDA AQDLAPGKWL DLPSGALHDA ANVSRVMPSA
MLFVPSIGGI SHAFDEDTHE DDLVLGLQVL NQAALSL
//
