Reviewed, UniProtKB/Swiss-Prot Q5ZLN1 (PGAM1_CHICK)

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):
    BPG-dependent PGAM 1

Gene names

Name:	PGAM1
ORF Names:	RCJMB04_5g20

Organism

Gallus gallus (Chicken)

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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.

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. UniProtKB P18669 3-phospho-D-glyceroyl phosphate = 2,3-bisphospho-D-glycerate. UniProtKB P18669 2,3-bisphospho-D-glycerate + H2O = 3-phospho-D-glycerate + phosphate. UniProtKB P18669
Subunit structure	Homodimer By similarity. UniProtKB P18669
Sequence similarities	Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Mass spectrometry	Molecular mass is 28769±1 Da from positions 2 - 254. Determined by MALDI. Ref.2

Ontologies

Keywords
Biological process	Glycolysis
Molecular function	Hydrolase Isomerase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
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 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 UniProtKB P18669
	Chain	2 – 254	253	Phosphoglycerate mutase 1		PRO_0000223502
Regions
	Compositional bias	122 – 125	4	Poly-Pro
Sites
	Active site	11	1	Tele-phosphohistidine intermediate By similarity UniProtKB P18669
	Active site	186	1	By similarity UniProtKB P18669
	Site	62	1	Interaction with carboxyl group of phosphoglycerates By similarity UniProtKB P18669
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity UniProtKB P18669
	Modified residue	26	1	Phosphotyrosine By similarity UniProtKB P18669

Sequences

	Sequence		Length	Mass (Da)
	Q5ZLN1-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E96705B2E5F7F227	FASTA	254	28,898
	10 20 30 40 50 60 MAAYRLVLVR HGESAWNLEN RFCGWYDADL SPAGQQEARR GGEALRDAGY EFDICFTSVQ 70 80 90 100 110 120 KRAIRTLWNV LDAIDQMWLP VVRTWRLNER HYGALTGLNK AETAAKHGEA QVKIWRRSFD 130 140 150 160 170 180 IPPPPMQSDH PFFSTISKDR RYADLTEDQL PTCESLKDTI ARALPFWNEE IVPQIKEGKR 190 200 210 220 230 240 VLIAAHGNSL RGIVKHLEGM SEEAIMELNL PTGIPIVYEL DKNLKPIKPM QFLGDEETVR 250 KAMEAVAAQG KVKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene function analysis." Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M. Genome Biol. 6:R6.1-R6.9(2005) [PubMed: 15642098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: CB. Tissue: Bursa of Fabricius.
[2]	"Proteomic analysis of the Gallus gallus embryo at stage-29 of development." Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J., Schneider J., Palomar M.A., Linares R. Proteomics 5:4946-4957(2005) [PubMed: 16287166] [Abstract] Cited for: IDENTIFICATION, MASS SPECTROMETRY. Tissue: Embryo.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ719703 mRNA. Translation: CAG31362.1.
IPI	IPI00585486.
RefSeq	NP_001026727.1.
UniGene	Gga.6033
3D structure databases
SMR	Q5ZLN1. Positions 2-246.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5ZLN1.
Genome annotation databases
Ensembl	ENSGALT00000012301; ENSGALP00000012287; ENSGALG00000007606; Gallus gallus. [Genome view] ENSGALT00000039466; ENSGALP00000038677; ENSGALG00000007606; Gallus gallus. [Genome view]
GeneID	428969.
KEGG	gga:428969.
Organism-specific databases
CTD	428969.
Phylogenomic databases
eggNOG	veNOG12777.
HOGENOM	HBG658938.
HOVERGEN	Q5ZLN1.
InParanoid	Q5ZLN1.
PhylomeDB	Q5ZLN1.
Enzyme and pathway databases
BRENDA	3.1.3.13. 4. 5.4.2.1. 4. 5.4.2.4. 4.
Family and domain databases
InterPro	IPR001345. PG/BPGM_mutase_AS. IPR013078. PG_mutase. IPR005952. Phosphogly_mut1. [Graphical view]
PANTHER	PTHR11931. Phosphogly_mut1. 1 hit.
Pfam	PF00300. PGAM. 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_CHICK

Accession

Primary (citable) accession number: Q5ZLN1
Secondary accession number(s): P84174

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 37 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)