ID A0A6I2GK55_9LACT Unreviewed; 374 AA.
AC A0A6I2GK55;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE SubName: Full=Amidohydrolase/deacetylase family metallohydrolase {ECO:0000313|EMBL:MRI85901.1};
DE EC=3.5.2.3 {ECO:0000313|EMBL:MRI85901.1};
GN ORFNames=GIY09_08485 {ECO:0000313|EMBL:MRI85901.1};
OS Fundicoccus ignavus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Aerococcaceae;
OC Fundicoccus.
OX NCBI_TaxID=2664442 {ECO:0000313|EMBL:MRI85901.1, ECO:0000313|Proteomes:UP000430975};
RN [1] {ECO:0000313|EMBL:MRI85901.1, ECO:0000313|Proteomes:UP000430975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WS4759 {ECO:0000313|EMBL:MRI85901.1,
RC ECO:0000313|Proteomes:UP000430975};
RA Siebert A., Huptas C., Wenning M., Scherer S., Doll E.V.;
RT "Characterisation of Fundicoccus ignavus gen. nov. sp. nov., a novel genus
RT of the family Aerococcaceae isolated from bulk tank milk.";
RL Submitted (NOV-2019) 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:MRI85901.1}.
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DR EMBL; WJQS01000007; MRI85901.1; -; Genomic_DNA.
DR RefSeq; WP_311454122.1; NZ_WJQS01000007.1.
DR AlphaFoldDB; A0A6I2GK55; -.
DR Proteomes; UP000430975; Unassembled WGS sequence.
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; 2.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:MRI85901.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000430975};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 154
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 154
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 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 156
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 154
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 374 AA; 41167 MW; 459D31C25F530384 CRC64;
MIDLLIKNAK TIDGQLIEVA IHQGSIVDVA SKVAYEVADV KEVIDLKGES YVSAGWIDGH
VHCFEKMDLY YDFPDKVGVE SGVTTVIDAG TTGAENVGQF YDLAKQAKTN VFALLNISKW
GIVEQDELAD LSKIQRDLIE EALAQYGDFI IGFKARMSKT VIGDNGIIPL EMAKEIQAKH
FKDLPLMVHI GSAPPELEET LSLLTPGDIV THCFNGKDNG IYDASKESIK PFAWEHYRRG
LVFDIGHGTD SFNFTAAERA FKEGMKAHTI STDIYSRNRL NGPVFNFATT LAKLHVVGYS
WPEIIDKVTA APAKVFQLAG KGHLAAGYDA DLTIFKLVEG EQTLVDSNGN ERQANEWLEP
VKVIVGGKQY DINL
//
