ID Q9S427_9GAMM Unreviewed; 361 AA. AC Q9S427; DT 01-MAY-2000, integrated into UniProtKB/TrEMBL. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 88. DE SubName: Full=Protein-tyrosine-phosphatase {ECO:0000313|EMBL:AAD45611.1}; DE EC=3.1.3.48 {ECO:0000313|EMBL:AAD45611.1}; GN Name=PPI {ECO:0000313|EMBL:AAD45611.1}; OS Shewanella sp. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales; OC Shewanellaceae; Shewanella. OX NCBI_TaxID=50422 {ECO:0000313|EMBL:AAD45611.1}; RN [1] {ECO:0000313|EMBL:AAD45611.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=10731677; RA Tsuruta H., Aizono Y.; RT "Cloning of phosphatase I gene from a psychrophile, Shewanella sp., and RT some properties of the recombinant enzyme."; RL J. Biochem. 127:143-149(2000). RN [2] {ECO:0007829|PDB:1V73} RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 22-361 IN COMPLEX WITH CALCIUM, RP AND DISULFIDE BONDS. RX PubMed=15713885; DOI=10.1093/jb/mvi010; RA Tsuruta H., Mikami B., Aizono Y.; RT "Crystal structure of cold-active protein-tyrosine phosphatase from a RT psychrophile, Shewanella sp."; RL J. Biochem. 137:69-77(2005). RN [3] {ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM} RP X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) OF 22-361 IN COMPLEX WITH ZINC, AND RP DISULFIDE BONDS. RX PubMed=18647345; DOI=10.1111/j.1742-4658.2008.06575.x; RA Tsuruta H., Mikami B., Yamamoto C., Yamagata H.; RT "The role of group bulkiness in the catalytic activity of psychrophile RT cold-active protein tyrosine phosphatase."; RL FEBS J. 275:4317-4328(2008). 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; AF164202; AAD45611.1; -; Genomic_DNA. DR PIR; JC7171; JC7171. DR PDB; 1V73; X-ray; 1.82 A; A=22-361. DR PDB; 2Z72; X-ray; 1.10 A; A=22-361. DR PDB; 2ZBM; X-ray; 1.50 A; A=22-355. DR PDBsum; 1V73; -. DR PDBsum; 2Z72; -. DR PDBsum; 2ZBM; -. DR AlphaFoldDB; Q9S427; -. DR SMR; Q9S427; -. DR DrugBank; DB05260; Gallium nitrate. DR BRENDA; 3.1.3.48; 5708. DR EvolutionaryTrace; Q9S427; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd07425; MPP_Shelphs; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR041787; MPP_Shelphs. DR PANTHER; PTHR46546; SHEWANELLA-LIKE PROTEIN PHOSPHATASE 1; 1. DR PANTHER; PTHR46546:SF4; SHEWANELLA-LIKE PROTEIN PHOSPHATASE 1; 1. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1V73, ECO:0007829|PDB:2Z72}; KW Calcium {ECO:0007829|PDB:1V73}; Hydrolase {ECO:0000313|EMBL:AAD45611.1}; KW Metal-binding {ECO:0007829|PDB:1V73, ECO:0007829|PDB:2Z72}; KW Signal {ECO:0000256|SAM:SignalP}; KW Zinc {ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..361 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004331960" FT DOMAIN 91..306 FT /note="Calcineurin-like phosphoesterase" FT /evidence="ECO:0000259|Pfam:PF00149" FT BINDING 97 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 97 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 97 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 99 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 99 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 133 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 133 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 168 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 168 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2ZBM" FT BINDING 226 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT BINDING 305 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:1V73" FT BINDING 305 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2Z72, ECO:0007829|PDB:2ZBM" FT DISULFID 46..66 FT /evidence="ECO:0007829|PDB:1V73, ECO:0007829|PDB:2Z72" SQ SEQUENCE 361 AA; 40815 MW; D44CF9FC13D08039 CRC64; MNKIYCLAVL SLTLLSPLAL ANTATEFDGP YVITPISGQS TAYWICDNRL KTTSIEKLQV NRPEHCGDLP ETKLSSEIKQ IMPDTYLGIK KVVALSDVHG QYDVLLTLLK KQKIIDSDGN WAFGEGHMVM TGDIFDRGHQ VNEVLWFMYQ LDQQARDAGG MVHLLMGNHE QMVLGGDLRY VHQRYDIATT LINRPYNKLY GADTEIGQWL RSKNTIIKIN DVLYMHGGIS SEWISRELTL DKANALYRAN VDASKKSLKA DDLLNFLFFG NGPTWYRGYF SETFTEAELD TILQHFNVNH IVVGHTSQER VLGLFHNKVI AVDSSIKVGK SGELLLLENN RLIRGLYDGT RETLQENSLN Q //