ID A0A2V1HR15_9MICO Unreviewed; 444 AA.
AC A0A2V1HR15;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:PVZ94781.1};
GN ORFNames=DDQ50_13995 {ECO:0000313|EMBL:PVZ94781.1};
OS Amnibacterium flavum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Amnibacterium.
OX NCBI_TaxID=2173173 {ECO:0000313|EMBL:PVZ94781.1, ECO:0000313|Proteomes:UP000244893};
RN [1] {ECO:0000313|EMBL:PVZ94781.1, ECO:0000313|Proteomes:UP000244893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8JJ-5 {ECO:0000313|EMBL:PVZ94781.1,
RC ECO:0000313|Proteomes:UP000244893};
RA Tuo L.;
RT "Amnibacterium sp. M8JJ-5, whole genome shotgun sequence.";
RL Submitted (MAY-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:PVZ94781.1}.
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DR EMBL; QEOP01000002; PVZ94781.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1HR15; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000244893; 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:PVZ94781.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244893};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT DOMAIN 248..346
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 162
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 417
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 444 AA; 45983 MW; AF7A44F3826A2865 CRC64;
MAALPRLGRR GGLHRSREGG SSGVEVTDGG ERGLTVDGDR LVADLERLAE FGVNEAGGID
RTSFSAADLA ARQWLIARCE EAGLEVAVDG IGNIVVSSPD LEAGLADQAP VWTGSHIDAV
PNGGRFDGPL GSLAAIECLR RLHEERVPLA RPVRAVVYTD EEGNYAHLFG SSALTRGFSV
AELSNLVGRD GDRFADTFAA SGGDLDAAAE VRLAPGALHA TVELHIEQGP LLERQGIQIG
VVTGIVAIGG GAVRFTGQAD HAGTTPMIGR RDSVVAAAEF ITLLPALAPR VGPAAVVTTG
IVRAEPGGSN VIAEAAEVVV DYRDPSTDNA RELEALIAAV ADEVASRHGS RVETHWEDIV
PAAPLHSEVR DAIRASAEQL GYSSVDIASG AGHDSQNLAT LAPTGMIFVP STGGRSHSPA
EHTPWPDVVR GADTLLGTVI RLAS
//
