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O24246

- PMGI_PRUDU

UniProt

O24246 - PMGI_PRUDU

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Protein
2,3-bisphosphoglycerate-independent phosphoglycerate mutase
Gene
N/A
Organism
Prunus dulcis (Almond) (Amygdalus dulcis)
Status
Reviewed - 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

Binds 2 manganese ions per subunit By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei10 – 101Phosphoserine intermediate By similarity
Metal bindingi10 – 101Manganese 2 By similarity
Metal bindingi359 – 3591Manganese 1 By similarity
Metal bindingi363 – 3631Manganese 1 By similarity
Metal bindingi400 – 4001Manganese 2 By similarity
Metal bindingi401 – 4011Manganese 2 By similarity
Metal bindingi430 – 4301Manganese 1 By similarity

GO - Molecular functioni

  1. manganese ion binding Source: InterPro
  2. phosphoglycerate mutase activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. glucose catabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Manganese, 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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – 488›4882,3-bisphosphoglycerate-independent phosphoglycerate mutase
PRO_0000212112Add
BLAST

Proteomic databases

PRIDEiO24246.

Interactioni

Subunit structurei

Monomer By similarity.

Structurei

3D structure databases

ProteinModelPortaliO24246.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view]
PfamiPF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view]
PIRSFiPIRSF001492. IPGAM. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.

Sequencei

Sequence statusi: Fragment.

O24246-1 [UniParc]FASTAAdd to Basket

« Hide

LPTEDDMGNS EVGHNALGAG RIFAQGAKLV DSALETGKLY EGEGFKYIKE    50
SFPTNTLHLI GLLSDGGVHS RLDQLLLLVK GASERGAKRI RVHILTDGRD 100
VLDGSSVGFA ETLENYLAQL REKGVDAQIA SGGGRMYVTM DRYENDWGVV 150
KRGWDAQVLG EAPHKFKNAV EAIKTLRQEP NTSDQYLPPF VIVDENGKPV 200
GPIVDGDAVV TFNFRADRMV MIAKALEYAD FDKFDRVRFP KIRYAGMLQY 250
DGELKLPSKY LVEPPEIDRT SGEYLTYNGV RTFACSETVK FGHVTFFWNG 300
NRSGYFNPQM EEYVEIPSDS GITFNVQPKM KAVEIAEKGR GAILSKKFEQ 350
VRVNLPNSDM VGHTSSIEAT VVACKAADEA VKIIIDAIEQ VGGIYVVTAD 400
HGNAEDMVKR NKKGQPLLDK NGNIQILTSH TLQPVPIAIG GPGLAPGVQF 450
RKDVPNGGLA NVAATVMNLH GFEAPADYET TLIEVVDN 488
Length:488
Mass (Da):53,395
Last modified:January 1, 1998 - v1
Checksum:iF103633B8FCD2D2A
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75020 mRNA. Translation: CAA52928.1.
PIRiT09138.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75020 mRNA. Translation: CAA52928.1 .
PIRi T09138.

3D structure databases

ProteinModelPortali O24246.
ModBasei Search...

Proteomic databases

PRIDEi O24246.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00186 .

Family and domain databases

Gene3Di 3.40.1450.10. 1 hit.
3.40.720.10. 2 hits.
InterProi IPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR011258. BPG-indep_PGM_N.
IPR006124. Metalloenzyme.
IPR005995. Pgm_bpd_ind.
[Graphical view ]
Pfami PF06415. iPGM_N. 1 hit.
PF01676. Metalloenzyme. 1 hit.
[Graphical view ]
PIRSFi PIRSF001492. IPGAM. 1 hit.
SUPFAMi SSF53649. SSF53649. 2 hits.
SSF64158. SSF64158. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "2,3-Bisphosphoglycerate-independent phosphoglycerate mutase is conserved among different phylogenic kingdoms."
    Grana X., Perez de la Ossa P., Broceno C., Stocker M., Garriga J., Puigdomenech P., Climent F.
    Comp. Biochem. Physiol. 112B:287-293(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: cv. Texas.
    Tissue: Root.

Entry informationi

Entry nameiPMGI_PRUDU
AccessioniPrimary (citable) accession number: O24246
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: January 1, 1998
Last modified: June 11, 2014
This is version 78 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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