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Reviewed, UniProtKB/Swiss-Prot Q5ZLN1 (PGAM1_CHICK)

Last modified February 9, 2010. Version 37. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length254 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P18669
Chain2 – 254253Phosphoglycerate mutase 1
PRO_0000223502

Regions

Compositional bias122 – 1254Poly-Pro

Sites

Active site111Tele-phosphohistidine intermediate By similarity UniProtKB P18669
Active site1861 By similarity UniProtKB P18669
Site621Interaction with carboxyl group of phosphoglycerates By similarity UniProtKB P18669

Amino acid modifications

Modified residue21N-acetylalanine By similarity UniProtKB P18669
Modified residue261Phosphotyrosine By similarity UniProtKB P18669

Sequences

Sequence LengthMass (Da)Tools
Q5ZLN1-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E96705B2E5F7F227

FASTA25428,898
        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 

« Hide

References

« Hide '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.
IPIIPI00585486.
RefSeqNP_001026727.1.
UniGeneGga.6033

3D structure databases

SMRQ5ZLN1. Positions 2-246.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5ZLN1.

Genome annotation databases

EnsemblENSGALT00000012301; ENSGALP00000012287; ENSGALG00000007606; Gallus gallus. [Genome view]
ENSGALT00000039466; ENSGALP00000038677; ENSGALG00000007606; Gallus gallus. [Genome view]
GeneID428969.
KEGGgga:428969.

Organism-specific databases

CTD428969.

Phylogenomic databases

eggNOGveNOG12777.
HOGENOMHBG658938.
HOVERGENQ5ZLN1.
InParanoidQ5ZLN1.
PhylomeDBQ5ZLN1.

Enzyme and pathway databases

BRENDA3.1.3.13. 4.
5.4.2.1. 4.
5.4.2.4. 4.

Family and domain databases

InterProIPR001345. PG/BPGM_mutase_AS.
IPR013078. PG_mutase.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. PGAM. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGAM1_CHICK
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

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