Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Staphylococcus haemolyticus (strain JCSC1435)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate.UniRule annotation

Catalytic activityi

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

Pathway:iglycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (gpmA), 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (gpmI)
  4. Enolase (eno)
  5. Pyruvate kinase (pyk)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei60 – 601SubstrateUniRule annotation
Binding sitei98 – 981SubstrateUniRule annotation
Active sitei182 – 1821UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciSHAE279808:GJX7-638-MONOMER.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.11UniRule annotation)
Short name:
BPG-dependent PGAMUniRule annotation
Short name:
PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
dPGMUniRule annotation
Gene namesi
Name:gpmAUniRule annotation
Ordered Locus Names:SH0636
OrganismiStaphylococcus haemolyticus (strain JCSC1435)
Taxonomic identifieri279808 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000543 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2282282,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_0000179918Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi279808.SH0636.

Structurei

3D structure databases

ProteinModelPortaliQ4L8T0.
SMRiQ4L8T0. Positions 3-228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 158Substrate bindingUniRule annotation
Regioni21 – 222Substrate bindingUniRule annotation
Regioni87 – 904Substrate bindingUniRule annotation
Regioni114 – 1152Substrate bindingUniRule annotation
Regioni183 – 1842Substrate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiPIKRYYL.
OrthoDBiEOG6C8N1H.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4L8T0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPKLILCRHG QSEWNAKNLF TGWEDVQLSE QGRNEAITSG RKLKENGIEI
60 70 80 90 100
DVAFTSLLTR ALETTQFLLA ESDQEWIPVH KSWRLNERHY GKLQGLNKDE
110 120 130 140 150
ARKEFGEEQV HQWRRSYDVK PPAQTEEQRE SYLKDRRYRH LDHRMMPYSE
160 170 180 190 200
SLKTTLERVV PIWTDKISQH LLDGETVLVA AHGNSIRALI KYLDNVSDED
210 220
IIGYEIKTGA PLIYELDDNL NVIDHYYL
Length:228
Mass (Da):26,735
Last modified:August 2, 2005 - v1
Checksum:i0C65EFA7A78A02F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE03945.1.
RefSeqiWP_011274961.1. NC_007168.1.

Genome annotation databases

EnsemblBacteriaiBAE03945; BAE03945; SH0636.
GeneIDi24247001.
KEGGisha:SH0636.
PATRICi19617295. VBIStaHae67511_0624.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP006716 Genomic DNA. Translation: BAE03945.1.
RefSeqiWP_011274961.1. NC_007168.1.

3D structure databases

ProteinModelPortaliQ4L8T0.
SMRiQ4L8T0. Positions 3-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi279808.SH0636.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAE03945; BAE03945; SH0636.
GeneIDi24247001.
KEGGisha:SH0636.
PATRICi19617295. VBIStaHae67511_0624.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiPIKRYYL.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciSHAE279808:GJX7-638-MONOMER.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERiPTHR11931. PTHR11931. 1 hit.
PfamiPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTiSM00855. PGAM. 1 hit.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
TIGRFAMsiTIGR01258. pgm_1. 1 hit.
PROSITEiPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the extreme plasticity of its genome and the evolution of human-colonizing staphylococcal species."
    Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y., Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C., Hiramatsu K.
    J. Bacteriol. 187:7292-7308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: JCSC1435.

Entry informationi

Entry nameiGPMA_STAHJ
AccessioniPrimary (citable) accession number: Q4L8T0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: August 2, 2005
Last modified: July 22, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.