ID A0A1N7LJ85_9RHOB Unreviewed; 416 AA.
AC A0A1N7LJ85;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:SIS73872.1};
GN ORFNames=SAMN05421795_103115 {ECO:0000313|EMBL:SIS73872.1};
OS Phaeovulum vinaykumarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Phaeovulum.
OX NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS73872.1, ECO:0000313|Proteomes:UP000186098};
RN [1] {ECO:0000313|Proteomes:UP000186098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; FTOM01000003; SIS73872.1; -; Genomic_DNA.
DR RefSeq; WP_076365160.1; NZ_OBMN01000003.1.
DR AlphaFoldDB; A0A1N7LJ85; -.
DR STRING; 407234.SAMN05421795_103115; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000186098; 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:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SIS73872.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186098};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..314
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
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 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 133
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 386
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 416 AA; 44464 MW; 778315C473D73151 CRC64;
MTELGANTRI NSARLWDSLM EMARIGPGIA GGCNRQTVTD ADAEGRALFQ RWCEAAGMSM
GVDRMGTMFA TRPGTDPEAL PVYVGSHLDT QPTGGKFDGV LGVLGALEVV RTMNDLGIRT
RHPIVVTNWT NEEGARFAPA MLASGVFAGV HTLEYAYDRE DGEGLKFGAE LARIGWVGDE
EVGARKMHAY YELHIEQGPI LEAENKEIGV VTHCQGLWWL EFTLTGKEAH TGSTPMPMRV
NAGLAMARIM EMVQEVAMAA QPDAVGGVGQ MRFSPNSRNV LPGTVVFTVD IRSPDQAKLD
GMRAEIEARA AEICAALKVE CAVEAVGHFD PVTFDPALVG AVRRAAEKLG YGHMDIVSGA
GHDACWAARV APATMVMCPC VDGLSHNEAE DITPAWAAAG TDVLFHAVLE TAEVVA
//
