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H2H2H1

- H2H2H1_CORDD

UniProt

H2H2H1 - H2H2H1_CORDD

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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene
gpmA, CDCE8392_0339
Organism
Corynebacterium diphtheriae (strain CDCE 8392)
Status
Unreviewed - Annotation score: 2 out of 5 - Protein inferred from homologyi

Functioni

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

Catalytic activityi

2-phospho-D-glycerate = 3-phospho-D-glycerate.UniRule annotationSAAS annotations

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei11 – 111Tele-phosphohistidine intermediate By similarityUniRule annotation
Binding sitei17 – 1712-phospho-D-glycerate By similarityUniRule annotation
Binding sitei62 – 6212-phospho-D-glycerate By similarityUniRule annotation
Binding sitei100 – 10012-phospho-D-glycerate By similarityUniRule annotation
Active sitei182 – 1821 By similarityUniRule annotation
Binding sitei184 – 18412-phospho-D-glycerate By similarityUniRule 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 annotationsImported

Keywords - Biological processi

GlycolysisUniRule annotationSAAS annotations

Enzyme and pathway databases

BioCyciCDIP698965:GHJP-353-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:CDCE8392_0339Imported
OrganismiCorynebacterium diphtheriae (strain CDCE 8392)Imported
Taxonomic identifieri698965 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium
ProteomesiUP000007156: Chromosome

Structurei

3D structure databases

ProteinModelPortaliH2H2H1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni23 – 2422-phospho-D-glycerate binding By similarityUniRule annotation
Regioni89 – 9242-phospho-D-glycerate binding By similarityUniRule annotation
Regioni116 – 11722-phospho-D-glycerate binding By similarityUniRule annotation

Sequence similaritiesi

Phylogenomic databases

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.
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.

H2H2H1-1 [UniParc]FASTAAdd to Basket

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MTTGKLILLR HGQSEWNASN QFTGWVDVNL TEKGEAEAKR GGELLKAQGV    50
LPSVVYTSLL RRAIRTANIA LNAADRHWIP VVRDWRLNER HYGALQGLNK 100
AETKEKYGDE QFMAWRRSYG TPPPELEDSS EFSQANDPRY ANLDVVPRTE 150
CLKDVVERFV PYFKEEILPR VQNGETVLIA AHGNSLRALV KHLDNISDAD 200
IAELNIPTGI PLVYELDEAG TVLNPGGTYL DPEAAAAGAA AVAAQGTK 248
Length:248
Mass (Da):27,333
Last modified:March 21, 2012 - v1
Checksum:iFE74E05C8608052E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003211 Genomic DNA. Translation: AEX71341.1.
RefSeqiYP_005132889.1. NC_016785.1.

Genome annotation databases

EnsemblBacteriaiAEX71341; AEX71341; CDCE8392_0339.
GeneIDi11707718.
KEGGicdd:CDCE8392_0339.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP003211 Genomic DNA. Translation: AEX71341.1 .
RefSeqi YP_005132889.1. NC_016785.1.

3D structure databases

ProteinModelPortali H2H2H1.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AEX71341 ; AEX71341 ; CDCE8392_0339 .
GeneIDi 11707718.
KEGGi cdd:CDCE8392_0339.

Phylogenomic databases

KOi K01834.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00186 .
BioCyci CDIP698965:GHJP-353-MONOMER.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
HAMAPi MF_01039. PGAM_GpmA.
InterProi IPR013078. His_Pase_superF_clade-1.
IPR029033. His_PPase_superfam.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view ]
PANTHERi PTHR11931. PTHR11931. 1 hit.
Pfami PF00300. His_Phos_1. 1 hit.
[Graphical view ]
SMARTi SM00855. PGAM. 1 hit.
[Graphical view ]
SUPFAMi SSF53254. SSF53254. 1 hit.
TIGRFAMsi TIGR01258. pgm_1. 1 hit.
PROSITEi PS00175. PG_MUTASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Pangenomic Study of Corynebacterium diphtheriae That Provides Insights into the Genomic Diversity of Pathogenic Isolates from Cases of Classical Diphtheria, Endocarditis, and Pneumonia."
    Trost E., Blom J., de Castro Soares S., Huang I.H., Al-Dilaimi A., Schroder J., Jaenicke S., Dorella F.A., Rocha F.S., Miyoshi A., Azevedo V., Schneider M.P., Silva A., Camello T.C., Sabbadini P.S., Santos C.S., Santos L.S., Hirata R.Jr.
    , Mattos-Guaraldi A.L., Efstratiou A., Schmitt M.P., Ton-That H., Tauch A.
    J. Bacteriol. 194:3199-3215(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CDCE 8392Imported.

Entry informationi

Entry nameiH2H2H1_CORDD
AccessioniPrimary (citable) accession number: H2H2H1
Entry historyi
Integrated into UniProtKB/TrEMBL: March 21, 2012
Last sequence update: March 21, 2012
Last modified: June 11, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome

External Data

Dasty 3

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