ID S7VCI7_9BACT Unreviewed; 332 AA.
AC S7VCI7;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Putative phosphotriesterase {ECO:0000313|EMBL:EPR67257.1};
GN ORFNames=ADICYQ_3812 {ECO:0000313|EMBL:EPR67257.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR67257.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR67257.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR67257.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR601559-51};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR601559-51};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000256|PROSITE-ProRule:PRU00679}.
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:EPR67257.1}.
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DR EMBL; ATNM01000134; EPR67257.1; -; Genomic_DNA.
DR RefSeq; WP_020890736.1; NZ_ATNM01000134.1.
DR AlphaFoldDB; S7VCI7; -.
DR STRING; 641524.ADICYQ_3812; -.
DR eggNOG; COG1735; Bacteria.
DR OrthoDB; 105927at2; -.
DR Proteomes; UP000014974; Unassembled WGS sequence.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1.
DR PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1.
DR Pfam; PF02126; PTE; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601559-51}.
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 48
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-51"
FT MOD_RES 164
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-50,
FT ECO:0000256|PROSITE-ProRule:PRU00679"
SQ SEQUENCE 332 AA; 37001 MW; A3808AFE97C5E03E CRC64;
MDGSIKVCIS ILITIISGCS LGSKKLFVQD LSGKHEASLD QIWLSHEHIL VDFIGADSID
SNDWSQALVI EEMTPYLEEL KQFNVTYFVD ATPNFLGRDV LLLEKIANRT GLKILTNTGL
YGVRNNQFIP DYAKKATAKE LSEMWIQEFD VGIDGSSIRP GFIKIGIDKA DPLTPMHNKL
IEAAALTHLE TGMAIASHTG KAKGLWPQLA QLKSLRVSPE AFIWVHAQAE DNPEEYLKAA
ATGCWISLDG LGWDLEKILF AKKHGFLNRI LIAHDAGWYD PQKDKQSIQG FTNIFTQLIP
ALKAHDFTDE DIKLLLSTNP AQAFSIRIRK VK
//
