ID A0A1G8J369_9RHOB Unreviewed; 416 AA.
AC A0A1G8J369;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=N-carbamoyl-L-amino-acid hydrolase {ECO:0000313|EMBL:SDI25571.1};
GN ORFNames=SAMN04487993_1002289 {ECO:0000313|EMBL:SDI25571.1};
OS Salipiger marinus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=555512 {ECO:0000313|EMBL:SDI25571.1, ECO:0000313|Proteomes:UP000199093};
RN [1] {ECO:0000313|EMBL:SDI25571.1, ECO:0000313|Proteomes:UP000199093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26424 {ECO:0000313|EMBL:SDI25571.1,
RC ECO:0000313|Proteomes:UP000199093};
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; FNEJ01000002; SDI25571.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8J369; -.
DR STRING; 555512.SAMN04487993_1002289; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000199093; 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:SDI25571.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199093};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 215..312
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; 44488 MW; 5625F6797E41CC7E CRC64;
MAAAGENLRI NGDRLWDSLM EMARIGPGVA GGNNRQTLTD ADAEGRALFQ RWCEAAGMTM
GLDAMGTMFA TRAGEDPEAL PVYMGSHLDT QPTGGKYDGV LGVLGALEVV RSMNDLGIRT
RHPIVVTNWS NEEGARFAPA MLASGVFAGV HTLDYAYGRT DPEGRSYGEE LARIGWKGTE
EVGARRMHAY YELHIEQGPI LEAEGRQIGV VTHCQGLWWL EFTLTGRAAH TGSTPMAMRI
NAGLAMARII EMVQEVAMAA QPDAMGGVGQ ARFLPNSRNV LPGSVVFTVD LRSPDQAKLD
ALRAEVEARA PAICAELGVG CAVEVVGHFD PVTFAPDLVR SVRGAAERLG YSHMDVVSGA
GHDACWAAKV APATMIMCPC VDGLSHNEAE EISKDWAAAG TEVLFHAVLE TAELLR
//
