Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase class 1

Gene

fba

Organism
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.1 Publication

Enzyme regulationi

Activated by citrate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei29Substrate1
Binding sitei33Substrate1
Binding sitei144Substrate1
Active sitei146Proton donor1
Binding sitei148Substrate1
Active sitei177Schiff-base intermediate with dihydroxyacetone-P1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BRENDAi4.1.2.13. 6329.
SABIO-RKP58315.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase class 1 (EC:4.1.2.13)
Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name:
FBP aldolase
Short name:
FBPA
Gene namesi
Name:fba
Ordered Locus Names:TTX_1278
OrganismiThermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Taxonomic identifieri768679 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaeThermoproteus
Proteomesi
  • UP000002654 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi144W → E: Loss of FBP aldolase activity; when associated with F-146. 1 Publication1
Mutagenesisi146Y → F: The catalytic activity is at least 3-fold lower than for the wild-type. Loss of FBP aldolase activity; when associated with E-144. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001389521 – 263Fructose-bisphosphate aldolase class 1Add BLAST263

Interactioni

Subunit structurei

Homodecamer (dimer of pentamers).3 Publications

Protein-protein interaction databases

STRINGi768679.TTX_1278.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 12Combined sources9
Beta strandi16 – 22Combined sources7
Helixi25 – 28Combined sources4
Helixi31 – 34Combined sources4
Beta strandi35 – 37Combined sources3
Helixi38 – 41Combined sources4
Helixi43 – 53Combined sources11
Beta strandi56 – 60Combined sources5
Helixi62 – 68Combined sources7
Beta strandi71 – 73Combined sources3
Beta strandi75 – 78Combined sources4
Beta strandi93 – 96Combined sources4
Helixi98 – 103Combined sources6
Beta strandi107 – 113Combined sources7
Helixi120 – 137Combined sources18
Beta strandi141 – 145Combined sources5
Helixi158 – 171Combined sources14
Beta strandi174 – 179Combined sources6
Helixi184 – 193Combined sources10
Turni194 – 196Combined sources3
Beta strandi199 – 202Combined sources4
Helixi210 – 222Combined sources13
Beta strandi227 – 231Combined sources5
Helixi232 – 235Combined sources4
Helixi240 – 251Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OJXX-ray1.90A/B/C/D/E/F/G/H/I/J1-263[»]
1OK4X-ray2.10A/B/C/D/E/F/G/H/I/J1-263[»]
1OK6X-ray2.40A/B/C/D/E/F/G/H/I/J1-263[»]
1W8SX-ray1.85A/B/C/D/E/F/G/H/I/J1-263[»]
2YCEX-ray1.93A/B/C/D/E/F/G/H/I/J1-263[»]
ProteinModelPortaliP58315.
SMRiP58315.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58315.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 25Substrate binding2
Regioni177 – 179Substrate binding3
Regioni202 – 204Substrate binding3
Regioni231 – 232Substrate binding2

Sequence similaritiesi

Belongs to the DeoC/FbaB aldolase family.Curated

Phylogenomic databases

eggNOGiarCOG04044. Archaea.
COG1830. LUCA.
KOiK11645.
OMAiYDHGIEH.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P58315-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANLTEKFLR IFARRGKSII LAYDHGIEHG PADFMDNPDS ADPEYILRLA
60 70 80 90 100
RDAGFDGVVF QRGIAEKYYD GSVPLILKLN GKTTLYNGEP VSVANCSVEE
110 120 130 140 150
AVSLGASAVG YTIYPGSGFE WKMFEELARI KRDAVKFDLP LVVWSYPRGG
160 170 180 190 200
KVVNETAPEI VAYAARIALE LGADAMKIKY TGDPKTFSWA VKVAGKVPVL
210 220 230 240 250
MSGGPKTKTE EDFLKQVEGV LEAGALGIAV GRNVWQRRDA LKFARALAEL
260
VYGGKKLAEP LNV
Length:263
Mass (Da):28,705
Last modified:October 18, 2001 - v1
Checksum:i1399A6D0CF4F0D9E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310483 Genomic DNA. Translation: CAC48235.1.
FN869859 Genomic DNA. Translation: CCC81912.1.
RefSeqiWP_014127167.1. NC_016070.1.

Genome annotation databases

EnsemblBacteriaiCCC81912; CCC81912; TTX_1278.
GeneIDi11262157.
KEGGittn:TTX_1278.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ310483 Genomic DNA. Translation: CAC48235.1.
FN869859 Genomic DNA. Translation: CCC81912.1.
RefSeqiWP_014127167.1. NC_016070.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OJXX-ray1.90A/B/C/D/E/F/G/H/I/J1-263[»]
1OK4X-ray2.10A/B/C/D/E/F/G/H/I/J1-263[»]
1OK6X-ray2.40A/B/C/D/E/F/G/H/I/J1-263[»]
1W8SX-ray1.85A/B/C/D/E/F/G/H/I/J1-263[»]
2YCEX-ray1.93A/B/C/D/E/F/G/H/I/J1-263[»]
ProteinModelPortaliP58315.
SMRiP58315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi768679.TTX_1278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCC81912; CCC81912; TTX_1278.
GeneIDi11262157.
KEGGittn:TTX_1278.

Phylogenomic databases

eggNOGiarCOG04044. Archaea.
COG1830. LUCA.
KOiK11645.
OMAiYDHGIEH.

Enzyme and pathway databases

BRENDAi4.1.2.13. 6329.
SABIO-RKP58315.

Miscellaneous databases

EvolutionaryTraceiP58315.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]
PfamiPF01791. DeoC. 1 hit.
[Graphical view]
PIRSFiPIRSF038992. Aldolase_Ia. 1 hit.
SMARTiSM01133. DeoC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALF1_THETK
AccessioniPrimary (citable) accession number: P58315
Secondary accession number(s): G4RK17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: November 2, 2016
This is version 73 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.