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Protein

2,3-bisphosphoglycerate-independent phosphoglycerate mutase

Gene

apgM

Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi: glycolysis

This protein is involved in step 3 of the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate.UniRule annotation
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Glyceraldehyde-3-phosphate dehydrogenase (gap)
  2. Phosphoglycerate kinase (pgk)
  3. 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (apgM), 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (Ta1347)
  4. Enolase (eno)
  5. Pyruvate kinase (Ta0896)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyruvate from D-glyceraldehyde 3-phosphate, the pathway glycolysis and in Carbohydrate degradation.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Glycolysis

Enzyme and pathway databases

BRENDAi5.4.2.12. 6324.
UniPathwayiUPA00109; UER00186.

Names & Taxonomyi

Protein namesi
Recommended name:
2,3-bisphosphoglycerate-independent phosphoglycerate mutaseUniRule annotation (EC:5.4.2.12UniRule annotation)
Short name:
BPG-independent PGAMUniRule annotation
Short name:
PhosphoglyceromutaseUniRule annotation
Short name:
aPGAMUniRule annotation
Gene namesi
Name:apgMUniRule annotation
Ordered Locus Names:Ta0413
OrganismiThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Taxonomic identifieri273075 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma
Proteomesi
  • UP000001024 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4044042,3-bisphosphoglycerate-independent phosphoglycerate mutasePRO_0000138150Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi273075.Ta0413.

Structurei

Secondary structure

1
404
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Turni19 – 224Combined sources
Helixi26 – 294Combined sources
Helixi33 – 408Combined sources
Beta strandi42 – 487Combined sources
Helixi62 – 654Combined sources
Helixi70 – 734Combined sources
Helixi77 – 848Combined sources
Beta strandi94 – 11017Combined sources
Helixi113 – 1153Combined sources
Helixi120 – 1267Combined sources
Beta strandi129 – 1313Combined sources
Beta strandi134 – 1407Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi176 – 1783Combined sources
Helixi179 – 1813Combined sources
Helixi182 – 20019Combined sources
Helixi203 – 2108Combined sources
Beta strandi218 – 2269Combined sources
Helixi233 – 2375Combined sources
Beta strandi241 – 2444Combined sources
Helixi248 – 2569Combined sources
Beta strandi260 – 2623Combined sources
Helixi275 – 28511Combined sources
Turni286 – 2883Combined sources
Beta strandi290 – 2978Combined sources
Helixi308 – 32013Combined sources
Helixi321 – 3266Combined sources
Turni329 – 3313Combined sources
Beta strandi332 – 3398Combined sources
Beta strandi354 – 3607Combined sources
Turni373 – 3753Combined sources
Helixi376 – 3783Combined sources
Beta strandi379 – 3846Combined sources
Helixi385 – 3873Combined sources
Helixi388 – 3947Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDDX-ray2.80A/B1-404[»]
3KD8X-ray2.60A/B2-397[»]
ProteinModelPortaliQ9HL27.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HL27.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiarCOG01696. Archaea.
COG3635. LUCA.
HOGENOMiHOG000004785.
KOiK15635.
OMAiKDHSADP.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
HAMAPiMF_01402_A. ApgM_A. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR023665. ApgAM_prokaryotes.
IPR006124. Metalloenzyme.
IPR004456. Phosphoglycerate_mutase_apgM.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFiPIRSF006392. IPGAM_arch. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR00306. apgM. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9HL27-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMKSIILIVL DGLGDRPGSD LQNRTPLQAA FRPNLNWLAS HGINGIMHPI
60 70 80 90 100
SPGIRCGSDT SHMSLLGYDP KVYYPGRGPF EALGLGMDIR PGDLAFRANF
110 120 130 140 150
ATNRDGVIVD RRAGRENKGN EELADAISLD MGEYSFRVKS GVEHRAALVV
160 170 180 190 200
SGPDLSDMIG DSDPHREGLP PEKIRPTDPS GDRTAEVMNA YLEEARRILS
210 220 230 240 250
DHRVNKERVK NGRLPGNELL VRSAGKVPAI PSFTEKNRMK GACVVGSPWL
260 270 280 290 300
KGLCRLLRMD VFDVPGATGT VGSNYRGKIE KAVDLTSSHD FVLVNIKATD
310 320 330 340 350
VAGHDGNYPL KRDVIEDIDR AMEPLKSIGD HAVICVTGDH STPCSFKDHS
360 370 380 390 400
GDPVPIVFYT DGVMNDGVHL FDELSSASGS LRITSYNVMD ILMQLAGRSD

KFGS
Length:404
Mass (Da):43,933
Last modified:March 1, 2001 - v1
Checksum:i06C0306580FE8BDF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11555.1.
RefSeqiWP_010900840.1. NC_002578.1.

Genome annotation databases

EnsemblBacteriaiCAC11555; CAC11555; CAC11555.
GeneIDi1456023.
KEGGitac:Ta0413.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL445064 Genomic DNA. Translation: CAC11555.1.
RefSeqiWP_010900840.1. NC_002578.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IDDX-ray2.80A/B1-404[»]
3KD8X-ray2.60A/B2-397[»]
ProteinModelPortaliQ9HL27.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273075.Ta0413.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC11555; CAC11555; CAC11555.
GeneIDi1456023.
KEGGitac:Ta0413.

Phylogenomic databases

eggNOGiarCOG01696. Archaea.
COG3635. LUCA.
HOGENOMiHOG000004785.
KOiK15635.
OMAiKDHSADP.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00186.
BRENDAi5.4.2.12. 6324.

Miscellaneous databases

EvolutionaryTraceiQ9HL27.

Family and domain databases

Gene3Di3.40.720.10. 2 hits.
HAMAPiMF_01402_A. ApgM_A. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR017850. Alkaline_phosphatase_core.
IPR023665. ApgAM_prokaryotes.
IPR006124. Metalloenzyme.
IPR004456. Phosphoglycerate_mutase_apgM.
[Graphical view]
PfamiPF01676. Metalloenzyme. 1 hit.
PF10143. PhosphMutase. 1 hit.
[Graphical view]
PIRSFiPIRSF006392. IPGAM_arch. 1 hit.
SUPFAMiSSF53649. SSF53649. 2 hits.
TIGRFAMsiTIGR00306. apgM. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiAPGM_THEAC
AccessioniPrimary (citable) accession number: Q9HL27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: September 7, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.