Phosphoglycerate mutase 1 - Rattus norvegicus (Rat)

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Reviewed, UniProtKB/Swiss-Prot P25113 (PGAM1_RAT)

Last modified June 16, 2009. Version 89. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phosphoglycerate mutase 1
    EC=5.4.2.1
    EC=5.4.2.4
    EC=3.1.3.13
Alternative name(s):
    Phosphoglycerate mutase isozyme B
      Short name=PGAM-B
    BPG-dependent PGAM 1

Gene names

Name:

Pgam1

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
Catalytic activity	2-phospho-D-glycerate = 3-phospho-D-glycerate. 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. 2,3-bisphospho-D-glycerate + H₂O = 3-phospho-D-glycerate + phosphate.
Subunit structure	Homodimer.
Tissue specificity	In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

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Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Hydrolase Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: RGD
Molecular function	2,3-bisphospho-D-glycerate 2-phosphohydrolase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC phosphoglycerate mutase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 254

253

Phosphoglycerate mutase 1

PRO_0000179828

Regions

Compositional bias

122 – 131

Pro-rich

Sites

Active site

Tele-phosphohistidine intermediate

Active site

186

Site

Interaction with carboxyl group of phosphoglycerates

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine Ref.5

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

118

Phosphoserine By similarity

Experimental info

Sequence conflict

C → V in AAA41834. Ref.1

Sequence conflict

N → K in AAB19888. Ref.2

Sequence conflict

180

R → G in AAA41834. Ref.1

Sequence conflict

184

A → P in AAA41834. Ref.1

Sequence conflict

190 – 191

LR → YG in AAA41834. Ref.1

Sequence conflict

232

F → S in AAA41834. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P25113-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 6DC09A3BEBB22409
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FASTA

254

28,832

        10         20         30         40         50         60 
MAAYKLVLIR HGESAWNLEN RFSGWYDADL SPAGHEEAKR GGQALRDAGY EFDICFTSVQ 

        70         80         90        100        110        120 
KRAIRTLWTV LDAIDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEA QVKIWRRSYD 

       130        140        150        160        170        180 
VPPPPMEPDH PFYSNISKDR RYADLTEDQL PSCESLKDTI ARALPFWNEE IVPQIKEGKR 

       190        200        210        220        230        240 
VLIAAHGNSL RGIVKHLEGL SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR 

       250 
KAMEAVAAQG KVKK

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and sequencing of a cDNA encoding the B isozyme of rat phosphoglycerate mutase." Urena J.M., Grana X., de Lecea L., Ruiz P., Castella J., Carreras J., Pons G., Climent F. Gene 113:281-282(1992) [PubMed: 1533381] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA encoding type B subunit of rat phosphoglycerate mutase: its isolation and nucleotide sequence." Uchida K. Arch. Biochem. Biophys. 288:558-561(1991) [PubMed: 1832843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Prostate.
[4]	Lubec G., Diao W., Afjehi-Sadat L., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 11-39; 47-62; 163-176 AND 222-240, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus and Spinal cord.
[5]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY. Tissue: Kidney.

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Cross-references

Sequence databases
	M76591 mRNA. Translation: AAA41834.1. S63233 mRNA. Translation: AAB19888.2. BC065582 mRNA. Translation: AAH65582.1.
IPI	IPI00421428.
RefSeq	NP_445742.1.
UniGene	Rn.1383 Rn.154337
3D structure databases
HSSP	HSSP built from PDB template 1E58 based on UniProtKB P31217.
SMR	P25113. Positions 2-246.
ModBase	Search...
PTM databases
PhosphoSite	P25113.
Proteomic databases
PRIDE	P25113.
Genome annotation databases
GeneID	24642.
KEGG	rno:24642.
Organism-specific databases
RGD	3312. Pgam1.
Phylogenomic databases
HOVERGEN	P25113.
Enzyme and pathway databases
BRENDA	3.1.3.13. 248. 5.4.2.1. 248. 5.4.2.4. 248.
Family and domain databases
InterPro	IPR001345. PG/BPGM_mutase. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	603944.

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Entry information

Entry name

PGAM1_RAT

Accession

Primary (citable) accession number: P25113
Secondary accession number(s): Q6P0K6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 89 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents