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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene
N/A
Organism
Prunus dulcis (Almond) (Amygdalus dulcis)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.By similarity

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei10Phosphoserine intermediateBy similarity1
Metal bindingi10Manganese 2By similarity1
Binding sitei69SubstrateBy similarity1
Binding sitei135SubstrateBy similarity1
Binding sitei142SubstrateBy similarity1
Binding sitei290SubstrateBy similarity1
Metal bindingi359Manganese 1By similarity1
Metal bindingi363Manganese 1By similarity1
Metal bindingi400Manganese 2By similarity1
Metal bindingi401Manganese 2By similarity1
Metal bindingi430Manganese 1By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionIsomerase
Biological processGlycolysis
LigandManganese, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutase (EC:5.4.2.12)
Short name:
BPG-independent PGAM
Short name:
Phosphoglyceromutase
Alternative name(s):
PGAM-I
OrganismiPrunus dulcis (Almond) (Amygdalus dulcis)
Taxonomic identifieri3755 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsRosalesRosaceaeMaloideaeAmygdaleaePrunus

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000212112‹1 – 4882,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST›488

Proteomic databases

PRIDEiO24246.

Interactioni

Subunit structurei

Monomer.By similarity

Structurei

3D structure databases

ProteinModelPortaliO24246.
SMRiO24246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni99 – 100Substrate bindingBy similarity2
Regioni215 – 218Substrate bindingBy similarity4

Sequence similaritiesi

Family and domain databases

CDDicd16010. iPGM. 1 hit.
Gene3Di3.40.720.10. 1 hit.
InterProiView protein in InterPro
IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
PfamiView protein in Pfam
PF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.

Sequencei

Sequence statusi: Fragment.

O24246-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
LPTEDDMGNS EVGHNALGAG RIFAQGAKLV DSALETGKLY EGEGFKYIKE
60 70 80 90 100
SFPTNTLHLI GLLSDGGVHS RLDQLLLLVK GASERGAKRI RVHILTDGRD
110 120 130 140 150
VLDGSSVGFA ETLENYLAQL REKGVDAQIA SGGGRMYVTM DRYENDWGVV
160 170 180 190 200
KRGWDAQVLG EAPHKFKNAV EAIKTLRQEP NTSDQYLPPF VIVDENGKPV
210 220 230 240 250
GPIVDGDAVV TFNFRADRMV MIAKALEYAD FDKFDRVRFP KIRYAGMLQY
260 270 280 290 300
DGELKLPSKY LVEPPEIDRT SGEYLTYNGV RTFACSETVK FGHVTFFWNG
310 320 330 340 350
NRSGYFNPQM EEYVEIPSDS GITFNVQPKM KAVEIAEKGR GAILSKKFEQ
360 370 380 390 400
VRVNLPNSDM VGHTSSIEAT VVACKAADEA VKIIIDAIEQ VGGIYVVTAD
410 420 430 440 450
HGNAEDMVKR NKKGQPLLDK NGNIQILTSH TLQPVPIAIG GPGLAPGVQF
460 470 480
RKDVPNGGLA NVAATVMNLH GFEAPADYET TLIEVVDN
Length:488
Mass (Da):53,395
Last modified:January 1, 1998 - v1
Checksum:iF103633B8FCD2D2A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-terminal residuei11

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75020 mRNA. Translation: CAA52928.1.
PIRiT09138.

Similar proteinsi

Entry informationi

Entry nameiPMGI_PRUDU
AccessioniPrimary (citable) accession number: O24246
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: August 30, 2017
This is version 87 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families