Q5RFB8 (PGAM1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglycerate mutase 1
EC=3.1.3.13
EC=5.4.2.1
EC=5.4.2.4

Alternative name(s):
BPG-dependent PGAM 1
Phosphoglycerate mutase isozyme B
Short name=PGAM-B

Gene names

Name:

PGAM1

Organism

Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Ponginae › Pongo

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 transcript level

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	2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. 2-phospho-D-glycerate = 3-phospho-D-glycerate. 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate.
Subunit structure	Homodimer By similarity.
Tissue specificity	In mammalian tissues there are two types of phosphoglycerate mutase isozymes: type-M in muscles and type-B in other tissues.
Post-translational modification	Acetylated at Lys-253, Lys-253 and Lys-254 under high glucose condition. Acetylation increases catalytic activity. Under glucose restriction SIRT1 levels dramatically increase and it deacetylates the enzyme By similarity.
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Hydrolase Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	bisphosphoglycerate 2-phosphatase activity Inferred from electronic annotation. Source: EC bisphosphoglycerate mutase activity Inferred from electronic annotation. Source: EC 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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 254	253	Phosphoglycerate mutase 1		PRO_0000179827
Regions
	Compositional bias	122 – 131	10	Pro-rich
Sites
	Active site	11	1	Tele-phosphohistidine intermediate By similarity
	Active site	186	1	By similarity
	Site	62	1	Interaction with carboxyl group of phosphoglycerates By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	14	1	Phosphoserine By similarity
	Modified residue	26	1	Phosphotyrosine By similarity
	Modified residue	31	1	Phosphoserine By similarity
	Modified residue	92	1	Phosphotyrosine By similarity
	Modified residue	118	1	Phosphoserine By similarity
	Modified residue	251	1	N6-acetyllysine By similarity
	Modified residue	253	1	N6-acetyllysine By similarity
	Modified residue	254	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5RFB8 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E650852BEBB23AF8	FASTA	254	28,778
	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 DKNSKPIKPM QFLGDEETVR 250 KAMEAVAAQG KAKK

References

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

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR857242 mRNA. Translation: CAH89539.1.
RefSeq	NP_001127164.1. NM_001133692.2.
UniGene	Pab.4825.
3D structure databases
ProteinModelPortal	Q5RFB8.
SMR	Q5RFB8. Positions 2-246.
ModBase	Search...
Proteomic databases
PRIDE	Q5RFB8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100174215.
KEGG	pon:100174215.
Organism-specific databases
CTD	5223.
Phylogenomic databases
HOVERGEN	HBG027528.
InParanoid	Q5RFB8.
KO	K01834.
Family and domain databases
InterPro	IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. PTHR11931. 1 hit.
Pfam	PF00300. His_Phos_1. 1 hit. [Graphical view]
SMART	SM00855. PGAM. 1 hit. [Graphical view]
TIGRFAMs	TIGR01258. pgm_1. 1 hit.
PROSITE	PS00175. PG_MUTASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGAM1_PONAB

Accession

Primary (citable) accession number: Q5RFB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	January 23, 2007
Last modified:	October 31, 2012
This is version 55 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program