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Q5R979 (PGM2L_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Glucose 1,6-bisphosphate synthase

EC=2.7.1.106
Alternative name(s):
Phosphoglucomutase-2-like 1
Gene names
Name:PGM2L1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Glucose 1,6-bisphosphate synthase
PRO_0000147786

Sites

Active site1751Phosphoserine intermediate By similarity

Amino acid modifications

Modified residue1751Phosphoserine By similarity

Experimental info

Sequence conflict5981L → P in CAH91272. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q5R979 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 994B941D5AC78225

FASTA62270,456
        10         20         30         40         50         60 
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR 

        70         80         90        100        110        120 
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ 

       130        140        150        160        170        180 
VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE 

       190        200        210        220        230        240 
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM 

       250        260        270        280        290        300 
EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST 

       310        320        330        340        350        360 
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL 

       370        380        390        400        410        420 
FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII 

       430        440        450        460        470        480 
DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE 

       490        500        510        520        530        540 
KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD ITTGYDSSQP 

       550        560        570        580        590        600 
NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK 

       610        620 
LIDALIENFL QPSKNGLIWR SV 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR859079 mRNA. Translation: CAH91272.1.
CR859513 mRNA. Translation: CAH91681.1.
RefSeqNP_001125984.1. NM_001132512.1.
UniGenePab.1510.

3D structure databases

ProteinModelPortalQ5R979.
SMRQ5R979. Positions 562-606.
ModBaseSearch...

Proteomic databases

PRIDEQ5R979.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSPPYT00000004370; ENSPPYP00000004199; ENSPPYG00000003674.
GeneID100172923.
KEGGpon:100172923.

Organism-specific databases

CTD283209.

Phylogenomic databases

HOVERGENHBG056917.
InParanoidQ5R979.
OMAIGEDVDM.

Family and domain databases

InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK11809.
PfamPF02878. 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]
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITEPS00710. PGM_PMM. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM2L_PONAB
AccessionPrimary (citable) accession number: Q5R979
Secondary accession number(s): Q5RAD8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: December 21, 2004
Last modified: November 16, 2011
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families