ID A0A395YGA3_9CLOT Unreviewed; 409 AA.
AC A0A395YGA3;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:RGY95850.1};
GN ORFNames=DXA13_18290 {ECO:0000313|EMBL:RGY95850.1};
OS Clostridium sp. AM58-1XD.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2292307 {ECO:0000313|EMBL:RGY95850.1, ECO:0000313|Proteomes:UP000266320};
RN [1] {ECO:0000313|EMBL:RGY95850.1, ECO:0000313|Proteomes:UP000266320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM58-1XD {ECO:0000313|EMBL:RGY95850.1,
RC ECO:0000313|Proteomes:UP000266320};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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:RGY95850.1}.
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DR EMBL; QSDR01000040; RGY95850.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395YGA3; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000266320; 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:0000313|EMBL:RGY95850.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000266320};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 213..310
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 214
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 273
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 286
FT /ligand="allantoate"
FT /ligand_id="ChEBI:CHEBI:17536"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-2"
FT BINDING 381
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 409 AA; 44067 MW; 245C93321F02E3D3 CRC64;
MTVNQERIFS RLKELGEIGK QEDGIYCMAL SEEDNQAYEL VRRYMEEAGM KVSTDAAGNL
IGRKEGKNPK APAVMTGSHI DTVYGGGIFD GRLGVIGGIE AVQTMNEQGI ETESPIEVVA
YRDEEGTRFM GSYSGARFRT GRPLAGILDH VDKDGISVRE ALRSCGIDPE NVHQAALPAG
YGKAHLELHI EQGAVLESKD LAVGIVTGIC TQIRGEYTIT GQSAHAGTTP IALRKDALCA
ASEAVLAIEE ETAASDQCVA TVGRIAAEPG GVNIVPGRVK FSLDIRHQDP DVRDELLERI
NKRIDEICKR RKVSWDLNVM SLETAGKPCS PDVQDVIANA CEEAGYPVYR MASGAGHDSG
AFVNFCPMGM IFIRSKDGLS HNGAEYSSPE DCAAGVEVLY RSMLKLAKN
//
