ID Q21RG3_ALBFT Unreviewed; 261 AA. AC Q21RG3; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 18-APR-2006, sequence version 1. DT 27-MAR-2024, entry version 91. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=Rfer_3941 {ECO:0000313|EMBL:ABD71640.1}; 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:ABD71640.1, 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; ABD71640.1; -; Genomic_DNA. DR RefSeq; WP_011466202.1; NC_007908.1. DR AlphaFoldDB; Q21RG3; -. DR STRING; 338969.Rfer_3941; -. DR KEGG; rfr:Rfer_3941; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_4_1_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 NCBIfam; NF033484; Stp1_PP2C_phos; 1. 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 4..245 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 261 AA; 28074 MW; 3D9BFC2543D52584 CRC64; MNYTFCTQTD PGRVRENNED SVAFDAATNL GVLADGMGGY NAGEIASGMA TAYIKSELAR WLSEASPQAN AGEVRRAIEI CVDNANRSIF AASCSNRHYA GMGTTLVVGV FLDNRLLLGH VGDSRCYRWR GNTLLQITKD HSLLQEQIDA GLLTPEQAAT APNKNLVTRA LGVDNVVSLE LNEHRVEPGD IYLMCSDGLS DMMPDAAIAE VLQHGISLLP MVQELVTLAN QNGGRDNITV LLIQASASPD KRGLMARLLG K //