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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Herbaspirillum seropedicae (strain SmR1)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

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

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotationSAAS 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 sitei98 – 9812-phospho-D-glycerateUniRule annotation
Active sitei182 – 1821UniRule annotation
Binding sitei184 – 18412-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

IsomeraseUniRule annotationSAAS annotation

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotation

Enzyme and pathway databases

BioCyciHSER757424:GCTT-163-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 annotationImported
Ordered Locus Names:Hsero_0163Imported
OrganismiHerbaspirillum seropedicae (strain SmR1)Imported
Taxonomic identifieri757424 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesOxalobacteraceaeHerbaspirillum
ProteomesiUP000000329 Componenti: Chromosome

Structurei

3D structure databases

ProteinModelPortaliD8IUX0.
SMRiD8IUX0. Positions 3-236.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 2222-phospho-D-glycerate bindingUniRule annotation
Regioni87 – 9042-phospho-D-glycerate bindingUniRule annotation
Regioni114 – 11522-phospho-D-glycerate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
HAMAPiMF_01039. PGAM_GpmA.
InterProiIPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
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.

Sequencei

Sequence statusi: Complete.

D8IUX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYKIVFMRHG ESTWNLANRF TGWVDVDLTE KGVAEARQAG KLLKEAGFTF
60 70 80 90 100
DLAYTSVLKR AIRTLWTTLD EMDQMYIPIK NDWRLNERHY GALQGLNKAE
110 120 130 140 150
TAAQYGDEQV LVWRRSYDTP PNPLTPGEER DAFGDPRYAG LSREQVPLTE
160 170 180 190 200
CLKDTVARVL PAWNDAIAPA IRAGKQIIIS AHGNSLRALI KYLDGISDND
210 220 230 240
IVGLNIPNGQ PLVYELDADL KPIKSYYLGD QSAIEAALKA VANQGKSK
Length:248
Mass (Da):27,726
Last modified:October 5, 2010 - v1
Checksum:i386510D4E2F880BC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002039 Genomic DNA. Translation: ADJ61689.1.
RefSeqiYP_003773597.1. NC_014323.1.

Genome annotation databases

EnsemblBacteriaiADJ61689; ADJ61689; Hsero_0163.
KEGGihse:Hsero_0163.
PATRICi42358983. VBIHerSer153339_0166.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002039 Genomic DNA. Translation: ADJ61689.1.
RefSeqiYP_003773597.1. NC_014323.1.

3D structure databases

ProteinModelPortaliD8IUX0.
SMRiD8IUX0. Positions 3-236.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADJ61689; ADJ61689; Hsero_0163.
KEGGihse:Hsero_0163.
PATRICi42358983. VBIHerSer153339_0166.

Phylogenomic databases

HOGENOMiHOG000221682.
KOiK01834.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BioCyciHSER757424:GCTT-163-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.
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.
ProtoNetiSearch...

Publicationsi

  1. "The genome of Herbaspirillum seropedicae SmR1, an endophytic, nitrogen-fixing, plant-growth promoting beta-Proteobacteria."
    Pedrosa F.O., Monteiro R.A., Wassem R., Cruz L.M., Ayub R.A., Colauto N.B., Fernandez M.A., Fungaro M.H.P., Grisard E.C., Hungria M., Madeira H.M.F., Nodari R.O., Osaku C.A., Petzl-Erler M.L., Terenzi H., Vieira L.G.E., Almeida M.I.M., Alves L.R.
    , Arantes O.M.N., Balsanelli E., Barcellos F.G., Baura V.A., Binde D.R., Campo R.J., Chubatsu L.S., Chueire L.M.O., Ciferri R.R., Correa L.C., da Conceicao Silva J.L., Dabul A.N.G., Dambros B.P., Faoro H., Favetti A., Friedermann G., Furlaneto M.C., Gasques L.S., Gimenes C.C.T., Gioppo N.M.R., Glienke-Blanco C., Godoy L.P., Guerra M.P., Karp S., Kava-Cordeiro V., Margarido V.P., Mathioni S.M., Menck-Soares M.A., Murace N.K., Nicolas M.F., Oliveira C.E.C., Pagnan N.A.B., Pamphile J.A., Patussi E.V., Pereira L.F.P., Pereira-Ferrari L., Pinto F.G.S., Precoma C., Prioli A.J., Prioli S.M.A.P., Raittz R.T., Ramos H.J.O., Ribeiro E.M.S.F., Rigo L.U., Rocha C.L.M.S.C., Rocha S.N., Santos K., Satori D., Silva A.G., Simao R.C.G., Soares M.A.M., Souza E.M., Steffens M.B.R., Steindel M., Tadra-Sfeir M.Z., Takahashi E.K., Torres R.A., Valle J.S., Vernal J.I., Vilas-Boas L.A., Watanabe M.A.E., Weiss V.A., Yates M.A., Souza E.M.
    Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SmR1Imported.

Entry informationi

Entry nameiD8IUX0_HERSS
AccessioniPrimary (citable) accession number: D8IUX0
Entry historyi
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: April 29, 2015
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

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.