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Protein

Glucose-6-phosphate isomerase B

Gene

pgiB

Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-glucose 6-phosphate = D-fructose 6-phosphate.

Pathwayi: glycolysis

This protein is involved in step 2 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase B (pgiB), Glucose-6-phosphate isomerase A (pgiA), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgiB)
  3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA)
  4. Fructose-bisphosphate aldolase (fba)
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 D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei285Proton donorBy similarity1
Active sitei306By similarity1
Active sitei420By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Gluconeogenesis, Glycolysis

Enzyme and pathway databases

BRENDAi5.3.1.9. 623.
SABIO-RKP13376.
UniPathwayiUPA00109; UER00181.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-6-phosphate isomerase B (EC:5.3.1.9)
Short name:
GPI B
Alternative name(s):
Phosphoglucose isomerase B
Short name:
PGI-B
Phosphohexose isomerase B
Short name:
PHI-B
Gene namesi
Name:pgiB
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001805921 – 445Glucose-6-phosphate isomerase BAdd BLAST445

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1445
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi8 – 10Combined sources3
Turni11 – 13Combined sources3
Helixi16 – 21Combined sources6
Helixi23 – 34Combined sources12
Helixi41 – 43Combined sources3
Turni45 – 48Combined sources4
Helixi49 – 52Combined sources4
Helixi55 – 71Combined sources17
Beta strandi73 – 78Combined sources6
Helixi81 – 83Combined sources3
Helixi85 – 94Combined sources10
Helixi99 – 101Combined sources3
Beta strandi102 – 105Combined sources4
Beta strandi107 – 114Combined sources8
Helixi117 – 127Combined sources11
Beta strandi132 – 137Combined sources6
Beta strandi139 – 141Combined sources3
Helixi144 – 161Combined sources18
Helixi163 – 166Combined sources4
Helixi167 – 169Combined sources3
Beta strandi170 – 174Combined sources5
Helixi180 – 188Combined sources9
Beta strandi191 – 194Combined sources4
Turni207 – 210Combined sources4
Helixi211 – 217Combined sources7
Helixi221 – 235Combined sources15
Helixi240 – 242Combined sources3
Helixi244 – 257Combined sources14
Beta strandi262 – 269Combined sources8
Helixi270 – 272Combined sources3
Helixi273 – 287Combined sources15
Beta strandi295 – 300Combined sources6
Helixi303 – 306Combined sources4
Helixi309 – 314Combined sources6
Beta strandi319 – 328Combined sources10
Turni346 – 350Combined sources5
Helixi353 – 370Combined sources18
Beta strandi375 – 382Combined sources8
Helixi385 – 406Combined sources22
Helixi416 – 426Combined sources11
Turni430 – 432Combined sources3
Helixi433 – 441Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0ZX-ray2.30A1-445[»]
1C7QX-ray2.30A1-445[»]
1C7RX-ray2.50A1-445[»]
2PGIX-ray2.30A1-445[»]
ProteinModelPortaliP13376.
SMRiP13376.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13376.

Family & Domainsi

Sequence similaritiesi

Belongs to the GPI family.Curated

Family and domain databases

HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13376-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAISFDYSNA LPFMQENELD YLSEFVKAAH HMLHERKGPG SDFLGWVDWP
60 70 80 90 100
IRYDKNEFSR IKQAAERIRN HSDALVVIGI GGSYLGARAA IEALSHTFHN
110 120 130 140 150
QMNDTTQIYF AGQNISSTYI SHLLDVLEGK DLSINVISKS GTTTEPAIAF
160 170 180 190 200
RIFRDYMEKK YGKEEARKRI YVTTDRTKGA LKKLADQEGY ETFVIPDNIG
210 220 230 240 250
GRYSVLTAVG LLPIAVAGLN IDRMMEGAAS AYHKYNNPDL LTNESYQYAA
260 270 280 290 300
VRNILYRKGK AIELLVNYEP SLHYVSEWWK QLFGESEGKD QKGLFPASVD
310 320 330 340 350
FTTDLHSMGQ YVQEGRRNLI ETVLHVKKPQ IELTIQEDPE NIDGLNFLAG
360 370 380 390 400
KTLDEVNKKA FQGTLLAHVD GGVPNLIVEL DEMNEYTFGE MVYFFEKACG
410 420 430 440
ISGHLLGVNP FDQPGVEAYK KNMFALLGKP GFEDEKAALM KRLSK
Length:445
Mass (Da):50,141
Last modified:January 1, 1990 - v1
Checksum:i078AD337669D1AE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16640 Genomic DNA. Translation: CAA34635.1.
PIRiS06198. NUBSS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16640 Genomic DNA. Translation: CAA34635.1.
PIRiS06198. NUBSS.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1B0ZX-ray2.30A1-445[»]
1C7QX-ray2.30A1-445[»]
1C7RX-ray2.50A1-445[»]
2PGIX-ray2.30A1-445[»]
ProteinModelPortaliP13376.
SMRiP13376.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00109; UER00181.
BRENDAi5.3.1.9. 623.
SABIO-RKP13376.

Miscellaneous databases

EvolutionaryTraceiP13376.

Family and domain databases

HAMAPiMF_00473. G6P_isomerase. 1 hit.
InterProiIPR001672. G6P_Isomerase.
IPR018189. Phosphoglucose_isomerase_CS.
[Graphical view]
PANTHERiPTHR11469. PTHR11469. 1 hit.
PfamiPF00342. PGI. 1 hit.
[Graphical view]
PRINTSiPR00662. G6PISOMERASE.
PROSITEiPS00765. P_GLUCOSE_ISOMERASE_1. 1 hit.
PS00174. P_GLUCOSE_ISOMERASE_2. 1 hit.
PS51463. P_GLUCOSE_ISOMERASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiG6PIB_GEOSE
AccessioniPrimary (citable) accession number: P13376
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: November 2, 2016
This is version 99 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

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.