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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Pelagibacter ubique (strain HTCC1062)
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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei9 – 91Tele-phosphohistidine intermediateUniRule annotation
Binding sitei15 – 1512-phospho-D-glycerateUniRule annotation
Binding sitei60 – 6012-phospho-D-glycerateUniRule annotation
Binding sitei97 – 9712-phospho-D-glycerateUniRule annotation
Active sitei181 – 1811UniRule annotation
Binding sitei183 – 18312-phospho-D-glycerateUniRule annotation

GO - Molecular functioni

  1. 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. glycolytic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BioCyciCPEL335992:GH3Z-193-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:SAR11_0193
OrganismiPelagibacter ubique (strain HTCC1062)
Taxonomic identifieri335992 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaSAR11 clusterCandidatus Pelagibacter
ProteomesiUP000002528 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2382382,3-bisphosphoglycerate-dependent phosphoglycerate mutasePRO_0000229134Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi335992.SAR11_0193.

Structurei

3D structure databases

ProteinModelPortaliQ4FP74.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate bindingUniRule annotation
Regioni86 – 8942-phospho-D-glycerate bindingUniRule annotation
Regioni113 – 11422-phospho-D-glycerate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiEANIYTG.
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.

Q4FP74-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTHLILVRHG QSEWNLEKRF TGWVDVDLTG QGKLEACKAG EYIKETKIDI
60 70 80 90 100
DYFYSSFQLR AINTLKFIQD TLRDKREPVK AWQLNERHYG ALTGLNKDEM
110 120 130 140 150
KEKLGEDKIH AFRRSWDIKP DPLNRNNPYH PLNIEVYKSI PKENIPDTES
160 170 180 190 200
LKDTYDRVMK FYIDEIQMKL KNDKNILISA HGNSIRALCK FLFKLDNQRI
210 220 230
TLLEIPTGNP LLINLDSKQN IKECTYLDQD RAKDLLVF
Length:238
Mass (Da):28,001
Last modified:August 30, 2005 - v1
Checksum:i49AD3CA9E07B6358
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000084 Genomic DNA. Translation: AAZ21015.1.
RefSeqiWP_011281538.1. NC_007205.1.
YP_265618.1. NC_007205.1.

Genome annotation databases

EnsemblBacteriaiAAZ21015; AAZ21015; SAR11_0193.
KEGGipub:SAR11_0193.
PATRICi31989843. VBICanPel5618_0192.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000084 Genomic DNA. Translation: AAZ21015.1.
RefSeqiWP_011281538.1. NC_007205.1.
YP_265618.1. NC_007205.1.

3D structure databases

ProteinModelPortaliQ4FP74.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi335992.SAR11_0193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAZ21015; AAZ21015; SAR11_0193.
KEGGipub:SAR11_0193.
PATRICi31989843. VBICanPel5618_0192.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiEANIYTG.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciCPEL335992:GH3Z-193-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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HTCC1062.

Entry informationi

Entry nameiGPMA_PELUB
AccessioniPrimary (citable) accession number: Q4FP74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: August 30, 2005
Last modified: April 29, 2015
This is version 65 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, Reference 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.