ID D1AIR5_SEBTE Unreviewed; 392 AA. AC D1AIR5; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 18-JUN-2025, entry version 89. DE RecName: Full=Phosphopentomutase {ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000256|NCBIfam:TIGR01696}; DE EC=5.4.2.7 {ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000256|NCBIfam:TIGR01696}; DE AltName: Full=Phosphodeoxyribomutase {ECO:0000256|HAMAP-Rule:MF_00740}; GN Name=deoB {ECO:0000256|HAMAP-Rule:MF_00740}; GN OrderedLocusNames=Sterm_1791 {ECO:0000313|EMBL:ACZ08649.1}; OS Sebaldella termitidis (strain ATCC 33386 / NCTC 11300). OC Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia; Fusobacteriales; OC Leptotrichiaceae; Sebaldella. OX NCBI_TaxID=526218 {ECO:0000313|EMBL:ACZ08649.1, ECO:0000313|Proteomes:UP000000845}; RN [1] {ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., Sims D., Meincke L., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., Hugenholtz P., RA Woyke T., Wu D., Eisen J.A.; RT "The complete chromosome of Sebaldella termitidis ATCC 33386."; RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ08649.1, ECO:0000313|Proteomes:UP000000845} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33386 / NCTC 11300 {ECO:0000313|Proteomes:UP000000845}; RX PubMed=21304705; RA Harmon-Smith M., Celia L., Chertkov O., Lapidus A., Copeland A., RA Glavina Del Rio T., Nolan M., Lucas S., Tice H., Cheng J.F., Han C., RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Pati A., Liolios K., RA Ivanova N., Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M., RA Hauser L., Chang Y.J., Jeffries C.D., Brettin T., Goker M., Beck B., RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., RA Klenk H.P., Chen F.; RT "Complete genome sequence of Sebaldella termitidis type strain RT (NCTC 11300)."; RL Stand. Genomic Sci. 2:220-227(2010). CC -!- FUNCTION: Isomerase that catalyzes the conversion of deoxy-ribose 1- CC phosphate (dRib-1-P) and ribose 1-phosphate (Rib-1-P) to deoxy-ribose CC 5-phosphate (dRib-5-P) and ribose 5-phosphate (Rib-5-P), respectively. CC {ECO:0000256|HAMAP-Rule:MF_00740}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-D-ribose 5- CC phosphate; Xref=Rhea:RHEA:27658, ChEBI:CHEBI:57259, CC ChEBI:CHEBI:62877; EC=5.4.2.7; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00740}; CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-ribose 1-phosphate = D-ribose 5-phosphate; CC Xref=Rhea:RHEA:18793, ChEBI:CHEBI:57720, ChEBI:CHEBI:78346; CC EC=5.4.2.7; Evidence={ECO:0000256|HAMAP-Rule:MF_00740}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00740}; CC Note=Binds 2 manganese ions. {ECO:0000256|HAMAP-Rule:MF_00740}; CC -!- PATHWAY: Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate CC degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2- CC deoxy-alpha-D-ribose 1-phosphate: step 1/2. {ECO:0000256|HAMAP- CC Rule:MF_00740}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740}. CC -!- SIMILARITY: Belongs to the phosphopentomutase family. CC {ECO:0000256|ARBA:ARBA00010373, ECO:0000256|HAMAP-Rule:MF_00740}. 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; CP001739; ACZ08649.1; -; Genomic_DNA. DR RefSeq; WP_012861243.1; NC_013517.1. DR AlphaFoldDB; D1AIR5; -. DR STRING; 526218.Sterm_1791; -. DR KEGG; str:Sterm_1791; -. DR eggNOG; COG1015; Bacteria. DR HOGENOM; CLU_053861_0_0_0; -. DR UniPathway; UPA00087; UER00173. DR Proteomes; UP000000845; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008973; F:phosphopentomutase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006018; P:2-deoxyribose 1-phosphate catabolic process; IEA:UniProtKB-UniRule. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0043094; P:metabolic compound salvage; IEA:UniProtKB-UniRule. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd16009; PPM; 1. DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1. DR Gene3D; 3.30.70.1250; Phosphopentomutase; 1. DR HAMAP; MF_00740; Phosphopentomut; 1. DR InterPro; IPR017850; Alkaline_phosphatase_core_sf. DR InterPro; IPR010045; DeoB. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf. DR NCBIfam; TIGR01696; deoB; 1. DR NCBIfam; NF003766; PRK05362.1; 1. DR PANTHER; PTHR21110; PHOSPHOPENTOMUTASE; 1. DR PANTHER; PTHR21110:SF0; PHOSPHOPENTOMUTASE; 1. DR Pfam; PF01676; Metalloenzyme; 1. DR PIRSF; PIRSF001491; Ppentomutase; 1. DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1. DR SUPFAM; SSF143856; DeoB insert domain-like; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00740}; KW Isomerase {ECO:0000256|HAMAP-Rule:MF_00740, ECO:0000313|EMBL:ACZ08649.1}; KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_00740}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00740}; Reference proteome {ECO:0000313|Proteomes:UP000000845}. FT DOMAIN 6..377 FT /note="Metalloenzyme" FT /evidence="ECO:0000259|Pfam:PF01676" FT BINDING 13 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" FT BINDING 287 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" FT BINDING 292 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" FT BINDING 328 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" FT BINDING 329 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" FT BINDING 340 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00740" SQ SEQUENCE 392 AA; 43051 MW; 148CEF7BB895E15A CRC64; MSKINRVTLI VLDSVGAGEL PDAKDFGDEG SNTLGNLSKA TGGLNLPNMQ KIGLGNITDI TGVAPNNNPD GAYGKAKEVS IGKDTTTGHW EMSGVILERP FPNYMKGFSE EVIKEFSEKT GRGVLWNKAA SGTVVIEDCG EEQMKTGKWI VYSSADPVFQ IAANEEIIPL EELYKACEIA LEICNAKSPV SRVIARPFVG KKKGEFKRTS NRHDFSIQPP GVTVLDKLSE AGKDVIGIGK IYDIFAGRGI TDTRKTNKDD LDGIKKTIEA LKEDTNGLIF TNLVDFDMLY GHRRDTEGYK NALELFDKWL PEIEKNLRDD EILIITADHG NDPTYKGTDH TREYIPVLVY GKHVKKGADI GTRESFTDIA STIEELLLGN KTEGSFADII LD //