ID A0A3P1XZR7_9BACT Unreviewed; 405 AA.
AC A0A3P1XZR7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:RRD63388.1};
GN ORFNames=EII26_11735 {ECO:0000313|EMBL:RRD63388.1};
OS Fretibacterium sp. OH1220_COT-178.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=2491047 {ECO:0000313|EMBL:RRD63388.1, ECO:0000313|Proteomes:UP000267192};
RN [1] {ECO:0000313|EMBL:RRD63388.1, ECO:0000313|Proteomes:UP000267192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OH1220_COT-178 {ECO:0000313|EMBL:RRD63388.1,
RC ECO:0000313|Proteomes:UP000267192};
RA Coil D.A., Jospin G., Darling A.E., Wallis C., Davis I.J., Harris S.,
RA Eisen J.A., Holcombe L.J., O'Flynn C.;
RT "Genomes From Bacteria Associated with the Canine Oral Cavity: a Test Case
RT for Automated Genome-Based Taxonomic Assignment.";
RL Submitted (NOV-2018) 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:RRD63388.1}.
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DR EMBL; RQYL01000034; RRD63388.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1XZR7; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000267192; 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 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:RRD63388.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000267192};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 405 AA; 43403 MW; 0E565796A9FDD903 CRC64;
MLRINRNRLW SDLEALGRIG AGARGRTRLA FSSEDLEARR LLVRWMEELG LEVHSDAHAN
LWGVRMATEP TLAPVVAGSH IDTVREAGMF DGTLGVLSGL AAVRAMNEAG IVTRRPVAVA
SFSDEEGGRF AAGGLAGSRA MAGLLTDGEL GAKRDEAGIS WLEAAAQSGF VGSDRLEPHA
YLEYHIEQGP VLCDEGTPIG VVEGIVSLSW LRFTFRGQAN HAGAFPMDRR HDAGLAAACA
SVALNRLALE LGEGTVVTAG QLELKPNLAN IVPGEAVLTV DVRQFRPELF EEALERAERT
VRAEADRLGV EVTVERLSRA EGAVFLPEMT AMVERHARAL GYRTRRMPSG AGHDAQILNR
LCPTAMIFCP SAGGRSHCPE EFSSLDEVGA GADVLLNGLL ELAER
//