ID   Q67S06_SYMTH            Unreviewed;       406 AA.
AC   Q67S06;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Phosphopentomutase {ECO:0000313|EMBL:BAD39537.1};
GN   OrderedLocusNames=STH552 {ECO:0000313|EMBL:BAD39537.1};
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459 {ECO:0000313|EMBL:BAD39537.1, ECO:0000313|Proteomes:UP000000417};
RN   [1] {ECO:0000313|EMBL:BAD39537.1, ECO:0000313|Proteomes:UP000000417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863 {ECO:0000313|Proteomes:UP000000417};
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SIMILARITY: Belongs to the phosphopentomutase family.
CC       {ECO:0000256|ARBA:ARBA00010373}.
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DR   EMBL; AP006840; BAD39537.1; -; Genomic_DNA.
DR   RefSeq; WP_011194686.1; NC_006177.1.
DR   AlphaFoldDB; Q67S06; -.
DR   STRING; 292459.STH552; -.
DR   KEGG; sth:STH552; -.
DR   eggNOG; COG1015; Bacteria.
DR   HOGENOM; CLU_053861_1_0_9; -.
DR   OrthoDB; 9769930at2; -.
DR   Proteomes; UP000000417; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0008973; F:phosphopentomutase activity; IEA:InterPro.
DR   GO; GO:0043094; P:cellular metabolic compound salvage; IEA:InterPro.
DR   GO; GO:0009117; P:nucleotide metabolic process; IEA:InterPro.
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   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR010045; DeoB.
DR   InterPro; IPR006124; Metalloenzyme.
DR   InterPro; IPR024052; Phosphopentomutase_DeoB_cap_sf.
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.
PE   3: Inferred from homology;
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000417}.
FT   DOMAIN          3..390
FT                   /note="Metalloenzyme"
FT                   /evidence="ECO:0000259|Pfam:PF01676"
SQ   SEQUENCE   406 AA;  43320 MW;  AD8CE6701FC0FA57 CRC64;
     MAKRAIVLVL DGFGVGAMAD VEQVQPRDAG AHTLASLVRS QGALRIPSLV RLGLPHIAPE
     AGLEPAGPPL AAWGRCNLAH WGADTFAGHN EIQGNRPLRP VISLFSTVAG QVRAHLEQAG
     HRVEDALPGG SALLVDGQIL VGDNLETDPG RIYNVTGPLD TVPFERILEV GRRVRQVVQV
     SRVIALGGVG ITVEDILAHT RITPAGQTGV VTPELHIYNE HYRVRHLGYG IDPAVQAPEL
     VASTGLPVAM IGKMADVVEC PSARWRDPVV DTEAVLEQVL EQLEQMPDGG YIAATVQETD
     LMGHEQDPVR YAEVLARADR GIARLLDRLR PGDLLIILAD HGNDPLIGHS LHTREQVPLL
     AFGPGFRPAA LGVRDTMADV AATVCEHLGA PAPEFGTSFL GLLTEK
//