ID   PGM2_PONAB              Reviewed;         612 AA.
AC   Q5RFI8;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Phosphopentomutase {ECO:0000305};
DE            EC=5.4.2.7 {ECO:0000250|UniProtKB:Q96G03};
DE   AltName: Full=Glucose phosphomutase 2;
DE   AltName: Full=Phosphodeoxyribomutase;
DE   AltName: Full=Phosphoglucomutase-2 {ECO:0000305};
DE            Short=PGM 2;
DE            EC=5.4.2.2 {ECO:0000250|UniProtKB:Q96G03};
GN   Name=PGM2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the conversion of the nucleoside breakdown products
CC       ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-
CC       phosphopentoses. Catalyzes the interconversion of glucose-1-phosphate
CC       into glucose-6-phosphate but with a lower catalytic efficiency. In
CC       vitro, has also a low glucose 1,6-bisphosphate synthase activity which
CC       is most probably not physiologically relevant.
CC       {ECO:0000250|UniProtKB:Q96G03}.
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:0000250|UniProtKB:Q96G03};
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;
CC         Evidence={ECO:0000250|UniProtKB:Q96G03};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC         Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC         EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:Q96G03};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P00949};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P00949};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q96G03}.
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR   EMBL; CR857168; CAH89469.1; -; mRNA.
DR   RefSeq; NP_001128996.1; NM_001135524.2.
DR   AlphaFoldDB; Q5RFI8; -.
DR   SMR; Q5RFI8; -.
DR   STRING; 9601.ENSPPYP00000016381; -.
DR   GeneID; 100190836; -.
DR   KEGG; pon:100190836; -.
DR   CTD; 55276; -.
DR   eggNOG; KOG1220; Eukaryota.
DR   InParanoid; Q5RFI8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0004614; F:phosphoglucomutase activity; ISS:UniProtKB.
DR   GO; GO:0008973; F:phosphopentomutase activity; ISS:UniProtKB.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR   InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR   InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR   InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR   InterPro; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   SUPFAM; SSF53738; SSF53738; 3.
DR   SUPFAM; SSF55957; SSF55957; 1.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Carbohydrate metabolism; Cytoplasm; Glucose metabolism;
KW   Isomerase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G03"
FT   CHAIN           2..612
FT                   /note="Phosphopentomutase"
FT                   /id="PRO_0000147783"
FT   ACT_SITE        165
FT                   /note="Phosphoserine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         63
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         165
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         165
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /note="via phosphate group"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         322
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         324
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         326
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         326
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         327
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         400
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         424
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   BINDING         438
FT                   /ligand="alpha-D-glucose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58392"
FT                   /evidence="ECO:0000250|UniProtKB:P00949"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G03"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G03"
SQ   SEQUENCE   612 AA;  68270 MW;  DD968C06E018FDB1 CRC64;
     MAAPEGSGLG EDARLDQETA QWLHWDKNSL TLEAVKRLIA EGNEEELRKC FGARMEFGTA
     GLRAAMGPGI SRMNDLTIIQ TTQGFCRYLE KQFSDLKQKG IVISFDARAH PSSGGSSRRF
     ARLAATTFIS QGIPVYLFSD ITPTPFVPFT VSRLKLCAGI MITASHNPKQ DNGYKVYWDN
     GAQIISPHDK GISQAIEENL EPWPQAWDDS LIDSSPLLHN PSASINNDYF EDLKKYCFHR
     SVNRETKVKF VHTSVHGVGH SFVQSAFKAF DLVPPEAVPE QKDPDPEFPT VKYPNPEEGK
     GVLTLSFALA DKTKARIVLA NDPDADRLAV AEKQDSGEWR VFSGNELGAL LGWWLFTSWK
     EKNQDRSALK DTYMLSSTVS SKILRAIALK EGFHFEETLT GFKWMGNRAK QLIDQGKTVL
     FAFEEAIGYM CCPFVLDKDG VSAAVISAEL ASFLATKNLS LSQQLKAIYV EYGYHITKAS
     YFICHDQDTI KKLFENLRSY DGKNNYPKAC GKFEISAIRD LTTGYDDNQP DKKAVLPTSK
     SSQMITFTFA NGGVATMRTS GTEPKIKYYA ELCAPPGNSD PEQLKKELNE LVSAIEEHFF
     QPQKYNLQPK AD