ID A0A364K459_9BACL Unreviewed; 384 AA.
AC A0A364K459;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:RAL24136.1};
GN ORFNames=DL897_10630 {ECO:0000313|EMBL:RAL24136.1};
OS Thermoflavimicrobium daqui.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales;
OC Thermoactinomycetaceae; Thermoflavimicrobium.
OX NCBI_TaxID=2137476 {ECO:0000313|EMBL:RAL24136.1, ECO:0000313|Proteomes:UP000251213};
RN [1] {ECO:0000313|EMBL:RAL24136.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL24136.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Wang X., Zhou H.;
RT "Thermoflavimicrobium daqus sp. nov., a thermophilic microbe isolated from
RT Moutai-flavour Daqu.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RAL24136.1, ECO:0000313|Proteomes:UP000251213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FBKL4.011 {ECO:0000313|EMBL:RAL24136.1,
RC ECO:0000313|Proteomes:UP000251213};
RA Zhirakovskaya E.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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:RAL24136.1}.
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DR EMBL; QJKK01000005; RAL24136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364K459; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000251213; Unassembled WGS sequence.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR047601; EF_0837-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03583; EF_0837; 1.
DR NCBIfam; NF006689; PRK09237.1; 1.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR Pfam; PF22647; EF_0837-like_N; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:RAL24136.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000251213};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 163
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 165
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 163
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 384 AA; 42603 MW; 18E2F3BEC377FC95 CRC64;
MGDILFGRCG REGNTVLVIK NARFVDESIK DILIEDNRIH AVVEQYQGDG EIIDLEGKSY
ISSGWIDLHT HAFPKYAPYC SHPDLIGYST GVTTVVDAGS TGANDIAEFY ELSRNCKTRV
FAFCNVSKIG LKRIDELADL TNLELEPIRK LYEKHPDFIV GLKARMSASV IGENGITPLK
IAKSFTKQLK LPLMVHIGSE PPKIEEILAE LESGDILTHC FNGKDNNIFR DQDFPLSELI
RAIERGIILD IGHGTASFSF HIAKKAITAG VLFDTISTDI YMRNKENGPV YDMATTLTKF
LALGYRLDKV IHAVTEKPAQ ILKQPLLGRI RPGNYADLTI FQLQEKPIKL VDSHGVTMEA
TQRVVPTAVV LGGKHIELTN NRPS
//
