ID Y349_MYCPN Reviewed; 281 AA. AC P75429; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 117. DE RecName: Full=Putative phosphatase/phosphodiesterase MPN_349 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=MPN_349; ORFNames=H91_orf281, MP487; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). RN [2] {ECO:0007744|PDB:1T71} RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH IRON, AND COFACTOR. RA Shin D.H., Jancarik J., Kim R., Yokota H., Kim S.-H.; RT "Crystal structure of a novel phosphatase from Mycoplasma pneumoniae."; RL Submitted (MAY-2004) to the PDB data bank. CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000305|Ref.2}; CC -!- SIMILARITY: Belongs to the YmdB-like family. {ECO:0000305}. 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; U00089; AAB96135.1; -; Genomic_DNA. DR PIR; S73813; S73813. DR RefSeq; NP_110037.1; NC_000912.1. DR RefSeq; WP_010874705.1; NZ_OU342337.1. DR PDB; 1T71; X-ray; 2.10 A; A=1-281. DR PDBsum; 1T71; -. DR AlphaFoldDB; P75429; -. DR SMR; P75429; -. DR IntAct; P75429; 1. DR STRING; 272634.MPN_349; -. DR EnsemblBacteria; AAB96135; AAB96135; MPN_349. DR GeneID; 66608994; -. DR KEGG; mpn:MPN_349; -. DR PATRIC; fig|272634.6.peg.376; -. DR HOGENOM; CLU_068238_0_0_14; -. DR OrthoDB; 9801109at2; -. DR BioCyc; MPNE272634:G1GJ3-551-MONOMER; -. DR EvolutionaryTrace; P75429; -. DR Proteomes; UP000000808; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR CDD; cd07382; MPP_DR1281; 1. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR005235; YmdB-like. DR NCBIfam; TIGR00282; TIGR00282 family metallophosphoesterase; 1. DR PANTHER; PTHR36303; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE; 1. DR PANTHER; PTHR36303:SF1; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE; 1. DR Pfam; PF13277; YmdB; 1. DR PIRSF; PIRSF004789; DR1281; 1. DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1. PE 1: Evidence at protein level; KW 3D-structure; Hydrolase; Iron; Metal-binding; Reference proteome. FT CHAIN 1..281 FT /note="Putative phosphatase/phosphodiesterase MPN_349" FT /id="PRO_0000210486" FT ACT_SITE 72 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:O31775" FT BINDING 12 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 43 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 43 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 44 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 71 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 158 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 183 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT BINDING 185 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:1T71" FT STRAND 6..10 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 12..14 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 15..23 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 26..33 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 36..41 FT /evidence="ECO:0007829|PDB:1T71" FT TURN 45..48 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 66..68 FT /evidence="ECO:0007829|PDB:1T71" FT TURN 71..74 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 77..79 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 80..83 FT /evidence="ECO:0007829|PDB:1T71" FT TURN 100..103 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 104..112 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 117..124 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 137..145 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 151..158 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 162..172 FT /evidence="ECO:0007829|PDB:1T71" FT TURN 173..175 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 176..186 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 199..202 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 219..226 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 241..249 FT /evidence="ECO:0007829|PDB:1T71" FT TURN 252..254 FT /evidence="ECO:0007829|PDB:1T71" FT STRAND 259..267 FT /evidence="ECO:0007829|PDB:1T71" FT HELIX 270..272 FT /evidence="ECO:0007829|PDB:1T71" SQ SEQUENCE 281 AA; 31431 MW; 909EE2FC9141C2CD CRC64; MMNSIKFIFL GDVYGKAGRN IIKNNLAQLK SKYQADLVIV NAENTTHGKG LSLKHYEFLK EAGVNYITMG NHTWFQKLDL AVVINKKDLV RPLNLDTSFA FHNLGQGSLV FEFNKAKIRI TNLLGTSVPL PFKTTNPFKV LKELILKRDC DLHIVDFHAE TTSEKNAFCM AFDGYVTTIF GTHTHVPSAD LRITPKGSAY ITDVGMCGPG FGSVIGANPE QSIRLFCAGS REHFEVSKCG AQLNGVFFEV DVNTKKVIKT EAIRIVEDDP RYLKQDYFNL I //