ID Q21XZ5_ALBFT Unreviewed; 305 AA. AC Q21XZ5; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 96. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Rfer_1628 {ECO:0000313|EMBL:ABD69358.1}; OS Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118) OS (Rhodoferax ferrireducens). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Rhodoferax. OX NCBI_TaxID=338969 {ECO:0000313|EMBL:ABD69358.1, ECO:0000313|Proteomes:UP000008332}; RN [1] {ECO:0000313|Proteomes:UP000008332} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-621 / DSM 15236 / T118 RC {ECO:0000313|Proteomes:UP000008332}; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., RA Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M., RA Kyrpides N., Ivanova N., Richardson P.; RT "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."; RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:83421; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001512}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA- CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:61977; EC=3.1.3.16; CC Evidence={ECO:0000256|ARBA:ARBA00001482}; 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; CP000267; ABD69358.1; -; Genomic_DNA. DR RefSeq; WP_011463926.1; NC_007908.1. DR AlphaFoldDB; Q21XZ5; -. DR STRING; 338969.Rfer_1628; -. DR KEGG; rfr:Rfer_1628; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_5_0_4; -. DR OrthoDB; 9801841at2; -. DR Proteomes; UP000008332; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. DR CDD; cd00143; PP2Cc; 1. DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1. DR InterPro; IPR015655; PP2C. DR InterPro; IPR036457; PPM-type-like_dom_sf. DR InterPro; IPR001932; PPM-type_phosphatase-like_dom. DR PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1. DR PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1. DR Pfam; PF13672; PP2C_2; 1. DR SMART; SM00331; PP2C_SIG; 1. DR SMART; SM00332; PP2Cc; 1. DR SUPFAM; SSF81606; PP2C-like; 1. DR PROSITE; PS51746; PPM_2; 1. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000008332}. FT DOMAIN 2..241 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 305 AA; 33318 MW; D818762B9A609FD3 CRC64; MKFSIFQISR KGSREKNEDR MGYCYTRESG IFFLADGMGG HPQGEVAAQL ALQTIAAMYQ KEAQPKIVDI AAFLTSAVLT AHRQILQHAI QNGMLDTPRT TAVVALVQDG AVSWIHCGDS RLYLVRQGQL LVRTRDHSFL EQQRATAAGK KPAERINRNV LFTCLGSPTK PVFDIAGPVG LQQGDKLMLC SDGLWDRLSE ADIVDCLAHK PVSEAVPQLV ESALRTAGDR SDNVTCIALE WEMPDGFEST RGSISTDTLS DGFFASTFQA DTLDAALEDL DDAAIERSIA EINEAIRRSA LKKSA //