PGM2L_MOUSE
ID PGM2L_MOUSE Reviewed; 621 AA.
AC Q8CAA7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
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 {ECO:0000312|MGI:MGI:1918224};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 142-150 AND 600-613, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=17804405; DOI=10.1074/jbc.m706818200;
RA Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Molecular identification of mammalian phosphopentomutase and glucose-1,6-
RT bisphosphate synthase, two members of the alpha-D-phosphohexomutase
RT family.";
RL J. Biol. Chem. 282:31844-31851(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: Expressed at highest levels in the brain and
CC testis, at intermediate levels in thymus, spleen, lung and skeletal
CC muscle, and at lowest levels in kidney, liver and heart.
CC {ECO:0000269|PubMed:17804405}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AK039189; BAC30270.1; -; mRNA.
DR EMBL; BC076571; AAH76571.1; -; mRNA.
DR CCDS; CCDS40035.1; -.
DR RefSeq; NP_081905.1; NM_027629.3.
DR RefSeq; XP_006508267.1; XM_006508204.1.
DR RefSeq; XP_006508268.1; XM_006508205.1.
DR AlphaFoldDB; Q8CAA7; -.
DR SMR; Q8CAA7; -.
DR IntAct; Q8CAA7; 1.
DR STRING; 10090.ENSMUSP00000081998; -.
DR iPTMnet; Q8CAA7; -.
DR PhosphoSitePlus; Q8CAA7; -.
DR EPD; Q8CAA7; -.
DR jPOST; Q8CAA7; -.
DR MaxQB; Q8CAA7; -.
DR PaxDb; Q8CAA7; -.
DR PeptideAtlas; Q8CAA7; -.
DR PRIDE; Q8CAA7; -.
DR ProteomicsDB; 289477; -.
DR Antibodypedia; 31067; 145 antibodies from 19 providers.
DR Ensembl; ENSMUST00000054436; ENSMUSP00000054782; ENSMUSG00000030729.
DR Ensembl; ENSMUST00000084935; ENSMUSP00000081998; ENSMUSG00000030729.
DR GeneID; 70974; -.
DR KEGG; mmu:70974; -.
DR UCSC; uc012fqa.1; mouse.
DR CTD; 283209; -.
DR MGI; MGI:1918224; Pgm2l1.
DR VEuPathDB; HostDB:ENSMUSG00000030729; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000158353; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q8CAA7; -.
DR OMA; PQDNGYK; -.
DR OrthoDB; 1041556at2759; -.
DR PhylomeDB; Q8CAA7; -.
DR TreeFam; TF300692; -.
DR Reactome; R-MMU-3322077; Glycogen synthesis.
DR Reactome; R-MMU-70171; Glycolysis.
DR Reactome; R-MMU-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-MMU-70370; Galactose catabolism.
DR SABIO-RK; Q8CAA7; -.
DR BioGRID-ORCS; 70974; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Pgm2l1; mouse.
DR PRO; PR:Q8CAA7; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8CAA7; protein.
DR Bgee; ENSMUSG00000030729; Expressed in otolith organ and 229 other tissues.
DR ExpressionAtlas; Q8CAA7; baseline and differential.
DR Genevisible; Q8CAA7; MM.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Direct protein sequencing;
KW Glucose metabolism; Isomerase; Magnesium; Metal-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..621
FT /note="Glucose 1,6-bisphosphate synthase"
FT /id="PRO_0000147785"
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 433
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 435
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 447
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:0007744|PubMed:21183079"
SQ SEQUENCE 621 AA; 70279 MW; 976F86C1FECD52CA CRC64;
MAENADDDLN SNLLHAPYLT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
VTSSCSSQRL AKLTAAVLLA KDIPVYLFSR YVPTPFVPYA VQELKAVAGV MITASHNRKE
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNDSWNDN LVDTSPLKKD PLQDICKKYM
EDLKKICFYR DLNSKTTLKF VHTSFHGVGH DYVQLAFQVF GFKPPIPVPE QKDPDPDFST
VKCPNPEEGE SVLELSLRLA EKENARIVLA TDPDADRLAV AELQENGRWK VFTGNELAAL
FGWWMFDCWK KNKPNADVKN VYMLATTVSS KILKAIALKE GFHFEETLPG FKWIGSRIKD
LLGNGKEVLF AFEESIGFLC GTSVLDKDGV SAAAVVAEMA SFLDTRKVTL MEQLTKVYEI
YGYHMSKTSY FLCYDPPTIK TIFERIRNFE SPKEYPKFCG AFAILHVRDI TTGYDSSQPN
KKSVLPVSKN SQMITFTFQN GCVATLRTSG TEPKIKYYAE MCASPGQSDT TFLEEELKKL
IDALIENFLE PSKNALVWRS V
