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Q12326 (PMG3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglycerate mutase 3

Short name=PGAM 3
EC=5.4.2.1
Alternative name(s):
BPG-dependent PGAM 3
MPGM 3
Phosphoglyceromutase 3
Gene names
Name:GPM3
Ordered Locus Names:YOL056W
ORF Names:O1236
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could be non-functional.

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.

Miscellaneous

Present with 3730 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   Molecular functionIsomerase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionphosphoglycerate mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Phosphoglycerate mutase 3
PRO_0000179841

Sites

Active site141Tele-phosphohistidine intermediate By similarity
Active site2351 By similarity
Site701Interaction with carboxyl group of phosphoglycerates By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12326 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 29C3FF3D28560914

FASTA30334,863
        10         20         30         40         50         60 
MTVTDTFKLF ILRHGQSELN SENIFCGWID AQLTEKGKSQ ARHSAKLIKQ FCDSNNISLP 

        70         80         90        100        110        120 
QIGYTSRLIR TQQTMDVILE ELGLKHTNYV ITTNTNIKEE LQDTRFEGSM PVLQTWRLNE 

       130        140        150        160        170        180 
RHYGAWQGQR KPDILKEYGK EKYMYIRRDY NGKPPKVNLN LEMVQEENDQ GSSTGYDFKE 

       190        200        210        220        230        240 
PNRHLKYGPE EKANERLPES ESLCEVVVRL KPFLNNVVLS TANKISQESC VIVGHGSSVR 

       250        260        270        280        290        300 
SLLKVLEGIS DEDIKDVDIP NGIPLVIELD RDNYSFVRKF YLDPESAKVN AQMVRDEGFE 


KNP 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a 26 kb region on the left arm of yeast chromosome XV."
Mannhaupt G., Vetter I., Schwarzlose C., Mitzel S., Feldmann H.
Yeast 12:67-76(1996) [PubMed: 8789261] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 90843 / S288c / FY73.
[2]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D. expand/collapse author list , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
Nature 387:98-102(1997) [PubMed: 9169874] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Investigation of two yeast genes encoding putative isoenzymes of phosphoglycerate mutase."
Heinisch J.J., Mueller S., Schlueter E., Jacoby J., Rodicio R.
Yeast 14:203-213(1998) [PubMed: 9544241] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X91067 Genomic DNA. Translation: CAA62530.1.
Z74798 Genomic DNA. Translation: CAA99064.1.
BK006948 Genomic DNA. Translation: DAA10727.1.
PIRS61723.
RefSeqNP_014585.1. NM_001183311.1.

3D structure databases

ProteinModelPortalQ12326.
SMRQ12326. Positions 7-294.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4234N.
IntActQ12326. 5 interactions.
MINTMINT-520340.
STRINGQ12326.

Proteomic databases

PeptideAtlasQ12326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYOL056W; YOL056W; YOL056W.
GeneID854098.
KEGGsce:YOL056W.
NMPDRfig|4932.3.peg.5677.

Organism-specific databases

CYGDYOL056w.
SGDS000005417. GPM3.

Phylogenomic databases

eggNOGfuNOG04978.
GeneTreeEFGT00070000008776.
HOGENOMHBG658938.
OMANVARERW.
OrthoDBEOG44F9K8.

Gene expression databases

ArrayExpressQ12326.
GenevestigatorQ12326.
GermOnlineYOL056W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
KOK01834.
PANTHERPTHR11931. Phosphogly_mut1. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. Pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio975767.

Entry information

Entry namePMG3_YEAST
AccessionPrimary (citable) accession number: Q12326
Secondary accession number(s): D6W211
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families