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A6Q3H2 (A6Q3H2_NITSB) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase HAMAP-Rule MF_01039

Short name=BPG-dependent PGAM HAMAP-Rule MF_01039
Short name=PGAM HAMAP-Rule MF_01039
Short name=Phosphoglyceromutase HAMAP-Rule MF_01039
Short name=dPGM HAMAP-Rule MF_01039
EC=5.4.2.11 HAMAP-Rule MF_01039
Gene names
Name:gpmA HAMAP-Rule MF_01039 EMBL BAF70031.1
Ordered Locus Names:NIS_0920 EMBL BAF70031.1
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP] EMBL BAF70031.1
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01039 RuleBase RU004512

Catalytic activity

2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01039 RuleBase RU004512 SAAS SAAS001345

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01039 RuleBase RU004512

Sequence similarities

Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP-Rule MF_01039

Ontologies

Keywords
   Biological processGlycolysis HAMAP-Rule MF_01039 SAAS SAAS001345
   Molecular functionIsomerase HAMAP-Rule MF_01039 SAAS SAAS001345 EMBL BAF70031.1
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_function2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region20 – 2122-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region86 – 8942-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region113 – 11422-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site81Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1821 By similarity HAMAP-Rule MF_01039
Binding site1412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site5912-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site9712-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18412-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
A6Q3H2 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 120E7CB8462E76DA

FASTA23026,623
        10         20         30         40         50         60 
MKLVLIRHGQ SVWNAKNLFT GWIDVELSEK GKAEAKKAGE LLKEANIYPN ICYTSYLKRA 

        70         80         90        100        110        120 
IHTAQIALNE LGWEHIDVIR SWKLNERHYG DWQGKNKEEV KAKYGEELFM AVRRGYDTPP 

       130        140        150        160        170        180 
PPIEESEPDY AKRYPLDPKY EDIGYHPKSE SLKDTRERVV EYFYEEIVPA LLAYDTVMIA 

       190        200        210        220        230 
AHGNSLRALI MYLESIAPEN VSKIEIPTGT PIVYDLTKEL VIYNKTTYNH 

« Hide

References

[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(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB155-2 EMBL BAF70031.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF70031.1.
RefSeqYP_001356388.1. NC_009662.1.

3D structure databases

ProteinModelPortalA6Q3H2.
SMRA6Q3H2. Positions 1-222.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_0920.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF70031; BAF70031; NIS_0920.
GeneID5360429.
KEGGnis:NIS_0920.
PATRIC22683914. VBINitSp82229_0961.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBCLSK977629.

Enzyme and pathway databases

BioCycNSP387092:GHA5-959-MONOMER.
UniPathwayUPA00109; UER00186.

Family and domain databases

HAMAPMF_01039. PGAM_GpmA.
InterProIPR013078. His_Pase_superF_clade-1.
IPR001345. PG/BPGM_mutase_AS.
IPR005952. Phosphogly_mut1.
[Graphical view]
PANTHERPTHR11931. PTHR11931. 1 hit.
PfamPF00300. His_Phos_1. 1 hit.
[Graphical view]
SMARTSM00855. PGAM. 1 hit.
[Graphical view]
TIGRFAMsTIGR01258. pgm_1. 1 hit.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameA6Q3H2_NITSB
AccessionPrimary (citable) accession number: A6Q3H2
Entry history
Integrated into UniProtKB/TrEMBL: August 21, 2007
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)