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Protein

2,3-bisphosphoglycerate-dependent phosphoglycerate mutase

Gene

gpmA

Organism
Nitratiruptor sp. (strain SB155-2)
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 annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Tele-phosphohistidine intermediateUniRule annotation
Binding sitei14 – 1412-phospho-D-glycerateUniRule annotation
Binding sitei59 – 5912-phospho-D-glycerateUniRule annotation
Binding sitei97 – 9712-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

BioCyciNSP387092:GHA5-959-MONOMER.

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:NIS_0920Imported
OrganismiNitratiruptor sp. (strain SB155-2)Imported
Taxonomic identifieri387092 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor
ProteomesiUP000001118 Componenti: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi387092.NIS_0920.

Structurei

3D structure databases

ProteinModelPortaliA6Q3H2.
SMRiA6Q3H2. Positions 1-222.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 2122-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.
OMAiDRVLPYW.
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.

A6Q3H2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLVLIRHGQ SVWNAKNLFT GWIDVELSEK GKAEAKKAGE LLKEANIYPN
60 70 80 90 100
ICYTSYLKRA IHTAQIALNE LGWEHIDVIR SWKLNERHYG DWQGKNKEEV
110 120 130 140 150
KAKYGEELFM AVRRGYDTPP PPIEESEPDY AKRYPLDPKY EDIGYHPKSE
160 170 180 190 200
SLKDTRERVV EYFYEEIVPA LLAYDTVMIA AHGNSLRALI MYLESIAPEN
210 220 230
VSKIEIPTGT PIVYDLTKEL VIYNKTTYNH
Length:230
Mass (Da):26,623
Last modified:August 21, 2007 - v1
Checksum:i120E7CB8462E76DA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70031.1.
RefSeqiWP_012082294.1. NC_009662.1.
YP_001356388.1. NC_009662.1.

Genome annotation databases

EnsemblBacteriaiBAF70031; BAF70031; NIS_0920.
KEGGinis:NIS_0920.
PATRICi22683914. VBINitSp82229_0961.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP009178 Genomic DNA. Translation: BAF70031.1.
RefSeqiWP_012082294.1. NC_009662.1.
YP_001356388.1. NC_009662.1.

3D structure databases

ProteinModelPortaliA6Q3H2.
SMRiA6Q3H2. Positions 1-222.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi387092.NIS_0920.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAF70031; BAF70031; NIS_0920.
KEGGinis:NIS_0920.
PATRICi22683914. VBINitSp82229_0961.

Phylogenomic databases

eggNOGiCOG0588.
HOGENOMiHOG000221682.
KOiK01834.
OMAiDRVLPYW.
OrthoDBiEOG6C8N1H.

Enzyme and pathway databases

BioCyciNSP387092:GHA5-959-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. "Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
    Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
    Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SB155-2Imported.

Entry informationi

Entry nameiA6Q3H2_NITSB
AccessioniPrimary (citable) accession number: A6Q3H2
Entry historyi
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: April 1, 2015
This is version 60 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.