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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)DescriptionActionsGraphical viewLength
ChainiPRO_00001381501 – 4042,3-bisphosphoglycerate-independent phosphoglycerate mutaseAdd BLAST404

Interactioni

Protein-protein interaction databases

STRINGi273075.Ta0413.

Structurei

Secondary structure

1404
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Turni19 – 22Combined sources4
Helixi26 – 29Combined sources4
Helixi33 – 40Combined sources8
Beta strandi42 – 48Combined sources7
Helixi62 – 65Combined sources4
Helixi70 – 73Combined sources4
Helixi77 – 84Combined sources8
Beta strandi94 – 110Combined sources17
Helixi113 – 115Combined sources3
Helixi120 – 126Combined sources7
Beta strandi129 – 131Combined sources3
Beta strandi134 – 140Combined sources7
Beta strandi145 – 152Combined sources8
Beta strandi176 – 178Combined sources3
Helixi179 – 181Combined sources3
Helixi182 – 200Combined sources19
Helixi203 – 210Combined sources8
Beta strandi218 – 226Combined sources9
Helixi233 – 237Combined sources5
Beta strandi241 – 244Combined sources4
Helixi248 – 256Combined sources9
Beta strandi260 – 262Combined sources3
Helixi275 – 285Combined sources11
Turni286 – 288Combined sources3
Beta strandi290 – 297Combined sources8
Helixi308 – 320Combined sources13
Helixi321 – 326Combined sources6
Turni329 – 331Combined sources3
Beta strandi332 – 339Combined sources8
Beta strandi354 – 360Combined sources7
Turni373 – 375Combined sources3
Helixi376 – 378Combined sources3
Beta strandi379 – 384Combined sources6
Helixi385 – 387Combined sources3
Helixi388 – 394Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IDDX-ray2.80A/B1-404[»]
3KD8X-ray2.60A/B2-397[»]
ProteinModelPortaliQ9HL27.
SMRiQ9HL27.
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. Pglycerate_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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3IDDX-ray2.80A/B1-404[»]
3KD8X-ray2.60A/B2-397[»]
ProteinModelPortaliQ9HL27.
SMRiQ9HL27.
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. Pglycerate_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: November 30, 2016
This is version 94 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.