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C7MSY8 (C7MSY8_SACVD) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 31. 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
Ordered Locus Names:Svir_02670 EMBL ACU95349.1
OrganismSaccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101) [Complete proteome] [HAMAP] EMBL ACU95349.1
Taxonomic identifier471857 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharomonospora

Protein attributes

Sequence length249 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 ACU95349.1
   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

Region24 – 2522-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region90 – 9342-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039
Region117 – 11822-phospho-D-glycerate binding By similarity HAMAP-Rule MF_01039

Sites

Active site121Tele-phosphohistidine intermediate By similarity HAMAP-Rule MF_01039
Active site1841 By similarity HAMAP-Rule MF_01039
Binding site1812-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site6312-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site10112-phospho-D-glycerate By similarity HAMAP-Rule MF_01039
Binding site18612-phospho-D-glycerate By similarity HAMAP-Rule MF_01039

Sequences

Sequence LengthMass (Da)Tools
C7MSY8 [UniParc].

Last modified October 13, 2009. Version 1.
Checksum: E875F3CE2A1917E3

FASTA24927,566
        10         20         30         40         50         60 
MAELGTLVLL RHGQSTWNAE NLFTGWVDVP LSEQGEAEAR RGGELLAEAG LLPDVVHTSL 

        70         80         90        100        110        120 
LRRAISTANI ALDVADRHWI DVRRDWRLNE RHYGALQGKN KKETLEQFGE EQFMLWRRSY 

       130        140        150        160        170        180 
DTPPPPIEPG SQYSQDGDVR YADLGDKLPT TECLKDVVER LLPYWESAIV PDLRAGKTVL 

       190        200        210        220        230        240 
IAAHGNSLRA LVKHLDGISD EDIVGLNIPT GIPLRYDLDE NLKPTNPGGT YLDPEAAEKA 


AAAVASQGR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001683 Genomic DNA. Translation: ACU95349.1.
RefSeqYP_003132176.1. NC_013159.1.

3D structure databases

ProteinModelPortalC7MSY8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471857.Svir_02670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACU95349; ACU95349; Svir_02670.
GeneID8385605.
KEGGsvi:Svir_02670.
PATRIC23390910. VBISacVir111818_0265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0588.
HOGENOMHOG000221682.
KOK01834.
OMASYYLGDQ.
OrthoDBEOG6C8N1H.
ProtClustDBCLSK2536836.

Enzyme and pathway databases

BioCycSVIR471857:GHAV-267-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 nameC7MSY8_SACVD
AccessionPrimary (citable) accession number: C7MSY8
Entry history
Integrated into UniProtKB/TrEMBL: October 13, 2009
Last sequence update: October 13, 2009
Last modified: February 19, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)