ID A0A103E7Y1_9BURK Unreviewed; 421 AA.
AC A0A103E7Y1;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Zn-dependent hydrolase {ECO:0000313|EMBL:KVE30062.1};
GN ORFNames=WS67_04165 {ECO:0000313|EMBL:KVE30062.1};
OS Burkholderia singularis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=1503053 {ECO:0000313|EMBL:KVE30062.1, ECO:0000313|Proteomes:UP000062788};
RN [1] {ECO:0000313|EMBL:KVE30062.1, ECO:0000313|Proteomes:UP000062788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSV85 {ECO:0000313|EMBL:KVE30062.1,
RC ECO:0000313|Proteomes:UP000062788};
RA Sahl J., Keim P., Wagner D.;
RT "Expanding the genomic diversity of Burkholderia species for the
RT development of highly accurate diagnostics.";
RL Submitted (NOV-2015) 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:KVE30062.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LOWA01000008; KVE30062.1; -; Genomic_DNA.
DR RefSeq; WP_059512784.1; NZ_LOWA01000008.1.
DR AlphaFoldDB; A0A103E7Y1; -.
DR OrthoDB; 9808195at2; -.
DR Proteomes; UP000062788; 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 NCBIfam; TIGR01879; hydantase; 1.
DR PANTHER; PTHR32494:SF5; ALLANTOATE AMIDOHYDROLASE; 1.
DR PANTHER; PTHR32494; ALLANTOATE DEIMINASE-RELATED; 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:KVE30062.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001235-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000062788};
KW Zinc {ECO:0000256|PIRSR:PIRSR001235-1}.
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
FT BINDING 391
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001235-1"
SQ SEQUENCE 421 AA; 45064 MW; 0155CDEFA504DC4B CRC64;
MTATTEVALP TSVKVDGERL WNSLMALAKI GATEKGGVCR LALTDLDRAG RDLIVGWAKE
AGCSVSIDRM GNVFMRRKGR NDALPPVMTG SHADSQPTGG RFDGIYGVLG GLEVIRTLND
LGIETERPVE TVIWTNEEGS RFAPAMVASG VFAGVFSLEY GLSRQDVDGK TIGEELARIG
YAGDLPCGGR PIHAAFELHI EQGPILEAEG KTIGVVTDAQ GQRWYEVVLS GQEAHAGPTP
MPRRRDALLG ASRVVQLVNE IGLRHAPLAC ATVGMMQVHP NSRNVIPGRV FFTVDFRHPR
DDVLAQMDAQ LRAGIARIAA DGKLDAQVDQ IFYYAPVAFD AGCVRSVRAA AERFGYTHRD
IVSGAGHDAC YLAQVAPTSM VFVPCIGGIS HNEIEDATPE WIAAGANVLL HAMLERASEP
G
//