ID A0A6C0FX10_9BACL Unreviewed; 362 AA.
AC A0A6C0FX10;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 18-JUN-2025, entry version 16.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:QHT59499.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:QHT59499.1};
GN ORFNames=GXP70_05705 {ECO:0000313|EMBL:QHT59499.1};
OS Paenibacillus lycopersici.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=2704462 {ECO:0000313|EMBL:QHT59499.1, ECO:0000313|Proteomes:UP000476064};
RN [1] {ECO:0000313|EMBL:QHT59499.1, ECO:0000313|Proteomes:UP000476064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12200R-189 {ECO:0000313|EMBL:QHT59499.1,
RC ECO:0000313|Proteomes:UP000476064};
RA Weon H.-Y., Lee S.A.;
RT "Paenibacillus sp. nov., isolated from tomato rhizosphere.";
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP048209; QHT59499.1; -; Genomic_DNA.
DR RefSeq; WP_162355565.1; NZ_CP048209.1.
DR AlphaFoldDB; A0A6C0FX10; -.
DR KEGG; plyc:GXP70_05705; -.
DR Proteomes; UP000476064; Chromosome.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
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:QHT59499.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000476064};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 147
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 147
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 149
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 147
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 362 AA; 38574 MW; 2233EF04A3A47CC1 CRC64;
MGIVLRNMKR MDGPEADIMI EGGRIAAIVP PGTGEGEVVA EGGFVSSGWI DMHVHAFREL
KPYGDAIDEI GVKQGVTTIV DAGSCGADRI GELRAAGNLA YTRLLAFMNI SRIGLERVDE
LSNPAWLDED AILEAVRANG EFIVGLKARI SRSVVKEQGI EPLRRARLFS EATGLPLMVH
IGSGPPEISE VIGLLARGDI VTHYLNGKAN NLFDGQGRPL PGLMDAIARG VHLDVGHGSA
SFSFRVAERA REAGLPLHTI STDIYESNRL GGPVFSLANV MSKFLYLGYG LREVVDAVTV
HAAAWLGRPE LAGLRVGGTA DLTLFDVVRG EKALIDSEGE TRTAGTYIQA KGAVINGSYF
AC
//
