ID A0A1B1MVN0_9BACL Unreviewed; 386 AA.
AC A0A1B1MVN0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 18-JUN-2025, entry version 29.
DE SubName: Full=Amidohydrolase {ECO:0000313|EMBL:ANS73240.1};
GN ORFNames=AWM70_00440 {ECO:0000313|EMBL:ANS73240.1};
OS Paenibacillus yonginensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=1462996 {ECO:0000313|EMBL:ANS73240.1, ECO:0000313|Proteomes:UP000092573};
RN [1] {ECO:0000313|EMBL:ANS73240.1, ECO:0000313|Proteomes:UP000092573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY84 {ECO:0000313|EMBL:ANS73240.1,
RC ECO:0000313|Proteomes:UP000092573};
RA Kim Y.J., Yang D.C., Sukweenadhi J.;
RT "Complete Genome Sequence of Paenibacillus yonginensis DCY84, a novel Plant
RT Growth-Promoting Bacteria with Elicitation of Induced Systemic
RT Resistance.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP014167; ANS73240.1; -; Genomic_DNA.
DR RefSeq; WP_068693368.1; NZ_CP014167.1.
DR AlphaFoldDB; A0A1B1MVN0; -.
DR STRING; 1462996.AWM70_00440; -.
DR KEGG; pyg:AWM70_00440; -.
DR OrthoDB; 9796020at2; -.
DR Proteomes; UP000092573; Chromosome.
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; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ANS73240.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092573};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 167
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 167
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 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 283
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 169
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 167
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 386 AA; 42201 MW; 197D2F1BB3C2D28A CRC64;
MGRRLLRNLR QTDGRLIDLV ITDGILTEVR VQGEDLSDVH GEGNPDSGGC FDGFDVWEAP
AGTYVSSGWI DMHVHAFPEF DPYGDEIDEI GIKQGVTTIV DAGSCGADRI ADLEASGRKA
DTRLLAFLNI SQIGLKRIDE LSDMSWINRD KVVQAVRDYP DFIVGLKARI SRSVVKESGI
QPLVAARELS EQTGLSLMVH IGSAPPDIRE VVPLLQRKDI ITHYLNGKAN NLFDADGNPL
DVLTDAVRRG VHLDVGHGTA SFSFSTAEAA KRHGIHPDTI STDIYRGNRL NGPVYSMANV
LSKFLELGYG LEETVRRVTV NAADWLGRPE LGRIQAGDSA NLTFFTVADE ATELVDSEGE
RRTSNRRIEA KGAVVGDKFF SSEIRA
//
