PGM2L_PONAB
ID PGM2L_PONAB Reviewed; 622 AA.
AC Q5R979; Q5RAD8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glucose 1,6-bisphosphate synthase {ECO:0000305};
DE EC=2.7.1.106 {ECO:0000250|UniProtKB:Q6PCE3};
DE AltName: Full=Phosphoglucomutase-2-like 1;
GN Name=PGM2L1;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-
CC bisphosphoglycerate as a phosphate donor and a series of 1-phosphate
CC sugars, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-
CC phosphate and deoxyribose 1-phosphate, as acceptors. In vitro, also
CC exhibits very low phosphopentomutase and phosphoglucomutase activity
CC which are most probably not physiologically relevant.
CC {ECO:0000250|UniProtKB:Q6PCE3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16769, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:58392,
CC ChEBI:CHEBI:58601; EC=2.7.1.106;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16770;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 6-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70911, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58225, ChEBI:CHEBI:58272,
CC ChEBI:CHEBI:58392; Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70912;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-ribose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-ribose 1,5-bisphosphate
CC + H(+); Xref=Rhea:RHEA:70899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57720, ChEBI:CHEBI:58272, ChEBI:CHEBI:68688;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70900;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + 2-deoxy-alpha-D-ribose 1-
CC phosphate = (2R)-3-phosphoglycerate + 2-deoxy-alpha-D-ribose 1,5-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70903, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272,
CC ChEBI:CHEBI:190126; Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70904;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-mannose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-mannose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70907, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:58409,
CC ChEBI:CHEBI:190127; Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70908;
CC Evidence={ECO:0000250|UniProtKB:Q6PCE3};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6PCE3}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; CR859079; CAH91272.1; -; mRNA.
DR EMBL; CR859513; CAH91681.1; -; mRNA.
DR RefSeq; NP_001125984.1; NM_001132512.1.
DR AlphaFoldDB; Q5R979; -.
DR SMR; Q5R979; -.
DR STRING; 9601.ENSPPYP00000004199; -.
DR PRIDE; Q5R979; -.
DR Ensembl; ENSPPYT00000004370; ENSPPYP00000004199; ENSPPYG00000003674.
DR GeneID; 100172923; -.
DR KEGG; pon:100172923; -.
DR CTD; 283209; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000158353; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q5R979; -.
DR OMA; PQDNGYK; -.
DR OrthoDB; 1041556at2759; -.
DR TreeFam; TF300692; -.
DR Proteomes; UP000001595; Chromosome 11.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; ISS:UniProtKB.
DR GO; GO:0016868; F:intramolecular transferase activity, phosphotransferases; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..622
FT /note="Glucose 1,6-bisphosphate synthase"
FT /id="PRO_0000147786"
FT ACT_SITE 175
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 73
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 175
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 336
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 336
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 337
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 434
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 436
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 448
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6PCE3"
FT CONFLICT 598
FT /note="L -> P (in Ref. 1; CAH91272)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70456 MW; 994B941D5AC78225 CRC64;
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM
EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL
FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII
DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE
KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD ITTGYDSSQP
NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK
LIDALIENFL QPSKNGLIWR SV
