O24246 (PMGI_PRUDU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase Short name=BPG-independent PGAM Short name=Phosphoglyceromutase EC=5.4.2.1 Alternative name(s): PGAM-I
Organism	Prunus dulcis (Almond) (Prunus amygdalus)
Taxonomic identifier	3755 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Amygdaloideae › Amygdaleae › Prunus

Protein attributes

Sequence length	488 AA.
Sequence status	Fragment.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity.
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Pathway	Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the BPG-independent phosphoglycerate mutase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Manganese Metal-binding
Molecular function	Isomerase
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	manganese ion binding Inferred from electronic annotation. Source: InterPro phosphoglycerate mutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 488	›488	2,3-bisphosphoglycerate-independent phosphoglycerate mutase		PRO_0000212112
Sites
	Active site	10	1	Phosphoserine intermediate By similarity
	Metal binding	10	1	Manganese 2 By similarity
	Metal binding	359	1	Manganese 1 By similarity
	Metal binding	363	1	Manganese 1 By similarity
	Metal binding	400	1	Manganese 2 By similarity
	Metal binding	401	1	Manganese 2 By similarity
	Metal binding	430	1	Manganese 1 By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	O24246 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: F103633B8FCD2D2A	FASTA	488	53,395
	10 20 30 40 50 60 LPTEDDMGNS EVGHNALGAG RIFAQGAKLV DSALETGKLY EGEGFKYIKE SFPTNTLHLI 70 80 90 100 110 120 GLLSDGGVHS RLDQLLLLVK GASERGAKRI RVHILTDGRD VLDGSSVGFA ETLENYLAQL 130 140 150 160 170 180 REKGVDAQIA SGGGRMYVTM DRYENDWGVV KRGWDAQVLG EAPHKFKNAV EAIKTLRQEP 190 200 210 220 230 240 NTSDQYLPPF VIVDENGKPV GPIVDGDAVV TFNFRADRMV MIAKALEYAD FDKFDRVRFP 250 260 270 280 290 300 KIRYAGMLQY DGELKLPSKY LVEPPEIDRT SGEYLTYNGV RTFACSETVK FGHVTFFWNG 310 320 330 340 350 360 NRSGYFNPQM EEYVEIPSDS GITFNVQPKM KAVEIAEKGR GAILSKKFEQ VRVNLPNSDM 370 380 390 400 410 420 VGHTSSIEAT VVACKAADEA VKIIIDAIEQ VGGIYVVTAD HGNAEDMVKR NKKGQPLLDK 430 440 450 460 470 480 NGNIQILTSH TLQPVPIAIG GPGLAPGVQF RKDVPNGGLA NVAATVMNLH GFEAPADYET TLIEVVDN

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75020 mRNA. Translation: CAA52928.1.
PIR	T09138.
3D structure databases
ProteinModelPortal	O24246.
ModBase	Search...
Proteomic databases
PRIDE	O24246.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00109; UER00186.
Family and domain databases
Gene3D	3.40.1450.10. 1 hit. 3.40.720.10. 2 hits.
InterPro	IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR011258. BPG-indep_PGM_N. IPR006124. Metalloenzyme. IPR005995. Pgm_bpd_ind. [Graphical view]
Pfam	PF06415. iPGM_N. 1 hit. PF01676. Metalloenzyme. 1 hit. [Graphical view]
PIRSF	PIRSF001492. IPGAM. 1 hit.
SUPFAM	SSF53649. Alkaline_phosphatase_core. 1 hit. SSF64158. BPG-indep_PGM_N. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PMGI_PRUDU

Accession

Primary (citable) accession number: O24246

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	April 3, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program