Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Glucose 1,6-bisphosphate synthase

Gene

Pgm2l1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Glucose 1,6-bisphosphate synthase using 1,3-bisphosphoglycerate as a phosphate donor and a series of 1-phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1-phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5-bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities (By similarity).By similarity

Catalytic activityi

3-phospho-D-glyceroyl phosphate + alpha-D-glucose 1-phosphate = 3-phospho-D-glycerate + alpha-D-glucose 1,6-bisphosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei69 – 691SubstrateBy similarity
Binding sitei73 – 731SubstrateBy similarity
Active sitei175 – 1751Phosphoserine intermediateBy similarity
Metal bindingi175 – 1751Magnesium; via phosphate groupBy similarity
Metal bindingi332 – 3321MagnesiumBy similarity
Metal bindingi334 – 3341MagnesiumBy similarity
Metal bindingi336 – 3361MagnesiumBy similarity
Binding sitei447 – 4471SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

SABIO-RKQ8CAA7.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose 1,6-bisphosphate synthase (EC:2.7.1.106)
Alternative name(s):
Phosphoglucomutase-2-like 1
Gene namesi
Name:Pgm2l1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1918224. Pgm2l1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 621621Glucose 1,6-bisphosphate synthasePRO_0000147785Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei175 – 1751PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8CAA7.
MaxQBiQ8CAA7.
PaxDbiQ8CAA7.
PRIDEiQ8CAA7.

PTM databases

iPTMnetiQ8CAA7.
PhosphoSiteiQ8CAA7.

Expressioni

Tissue specificityi

Expressed at highest levels in the brain and testis, at intermediate levels in thymus, spleen, lung and skeletal muscle, and at lowest levels in kidney, liver and heart.1 Publication

Gene expression databases

BgeeiQ8CAA7.
CleanExiMM_PGM2L1.
ExpressionAtlasiQ8CAA7. baseline and differential.
GenevisibleiQ8CAA7. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8CAA7. 1 interaction.
STRINGi10090.ENSMUSP00000054782.

Structurei

3D structure databases

ProteinModelPortaliQ8CAA7.
SMRiQ8CAA7. Positions 67-348.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni175 – 1762Substrate bindingBy similarity
Regioni336 – 3372Substrate bindingBy similarity
Regioni433 – 4353Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ8CAA7.
KOiK11809.
OMAiSVLICEM.
OrthoDBiEOG715Q3R.
PhylomeDBiQ8CAA7.
TreeFamiTF300692.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8CAA7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAENADDDLN SNLLHAPYLT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR
60 70 80 90 100
NGMNKELRDR LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE
110 120 130 140 150
RCFSDFKQRG FVVGYDTRGQ VTSSCSSQRL AKLTAAVLLA KDIPVYLFSR
160 170 180 190 200
YVPTPFVPYA VQELKAVAGV MITASHNRKE DNGYKVYWET GAQITSPHDK
210 220 230 240 250
EILKCIEECV EPWNDSWNDN LVDTSPLKKD PLQDICKKYM EDLKKICFYR
260 270 280 290 300
DLNSKTTLKF VHTSFHGVGH DYVQLAFQVF GFKPPIPVPE QKDPDPDFST
310 320 330 340 350
VKCPNPEEGE SVLELSLRLA EKENARIVLA TDPDADRLAV AELQENGRWK
360 370 380 390 400
VFTGNELAAL FGWWMFDCWK KNKPNADVKN VYMLATTVSS KILKAIALKE
410 420 430 440 450
GFHFEETLPG FKWIGSRIKD LLGNGKEVLF AFEESIGFLC GTSVLDKDGV
460 470 480 490 500
SAAAVVAEMA SFLDTRKVTL MEQLTKVYEI YGYHMSKTSY FLCYDPPTIK
510 520 530 540 550
TIFERIRNFE SPKEYPKFCG AFAILHVRDI TTGYDSSQPN KKSVLPVSKN
560 570 580 590 600
SQMITFTFQN GCVATLRTSG TEPKIKYYAE MCASPGQSDT TFLEEELKKL
610 620
IDALIENFLE PSKNALVWRS V
Length:621
Mass (Da):70,279
Last modified:March 1, 2003 - v1
Checksum:i976F86C1FECD52CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039189 mRNA. Translation: BAC30270.1.
BC076571 mRNA. Translation: AAH76571.1.
CCDSiCCDS40035.1.
RefSeqiNP_081905.1. NM_027629.3.
XP_006508267.1. XM_006508204.1.
XP_006508268.1. XM_006508205.1.
UniGeneiMm.440524.

Genome annotation databases

EnsembliENSMUST00000054436; ENSMUSP00000054782; ENSMUSG00000030729.
ENSMUST00000084935; ENSMUSP00000081998; ENSMUSG00000030729.
GeneIDi70974.
KEGGimmu:70974.
UCSCiuc012fqa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK039189 mRNA. Translation: BAC30270.1.
BC076571 mRNA. Translation: AAH76571.1.
CCDSiCCDS40035.1.
RefSeqiNP_081905.1. NM_027629.3.
XP_006508267.1. XM_006508204.1.
XP_006508268.1. XM_006508205.1.
UniGeneiMm.440524.

3D structure databases

ProteinModelPortaliQ8CAA7.
SMRiQ8CAA7. Positions 67-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CAA7. 1 interaction.
STRINGi10090.ENSMUSP00000054782.

PTM databases

iPTMnetiQ8CAA7.
PhosphoSiteiQ8CAA7.

Proteomic databases

EPDiQ8CAA7.
MaxQBiQ8CAA7.
PaxDbiQ8CAA7.
PRIDEiQ8CAA7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054436; ENSMUSP00000054782; ENSMUSG00000030729.
ENSMUST00000084935; ENSMUSP00000081998; ENSMUSG00000030729.
GeneIDi70974.
KEGGimmu:70974.
UCSCiuc012fqa.1. mouse.

Organism-specific databases

CTDi283209.
MGIiMGI:1918224. Pgm2l1.

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ8CAA7.
KOiK11809.
OMAiSVLICEM.
OrthoDBiEOG715Q3R.
PhylomeDBiQ8CAA7.
TreeFamiTF300692.

Enzyme and pathway databases

SABIO-RKQ8CAA7.

Miscellaneous databases

NextBioi332727.
PROiQ8CAA7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CAA7.
CleanExiMM_PGM2L1.
ExpressionAtlasiQ8CAA7. baseline and differential.
GenevisibleiQ8CAA7. MM.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. A-D-PHexomutase_a/b/a-I.
IPR016055. A-D-PHexomutase_a/b/a-I/II/III.
IPR005845. A-D-PHexomutase_a/b/a-II.
IPR005846. A-D-PHexomutase_a/b/a-III.
IPR005843. A-D-PHexomutase_C.
[Graphical view]
PfamiPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Hypothalamus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 142-150 AND 600-613, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Molecular identification of mammalian phosphopentomutase and glucose-1,6-bisphosphate synthase, two members of the alpha-D-phosphohexomutase family."
    Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M., Van Schaftingen E.
    J. Biol. Chem. 282:31844-31851(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen and Testis.

Entry informationi

Entry nameiPGM2L_MOUSE
AccessioniPrimary (citable) accession number: Q8CAA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 1, 2003
Last modified: May 11, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.