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P58315

- ALF1_THETK

UniProt

P58315 - ALF1_THETK

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Protein

Fructose-bisphosphate aldolase class 1

Gene

fba

Organism
Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate
Binding sitei33 – 331Substrate
Binding sitei144 – 1441Substrate
Active sitei146 – 1461Proton donor
Binding sitei148 – 1481Substrate
Active sitei177 – 1771Schiff-base intermediate with dihydroxyacetone-P

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciTTEN768679:GJSY-1253-MONOMER.
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
ProteomesiUP000002654: Chromosome

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi144 – 1441W → E: Loss of FBP aldolase activity; when associated with F-146. 1 Publication
Mutagenesisi146 – 1461Y → 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 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 263263Fructose-bisphosphate aldolase class 1PRO_0000138952Add
BLAST

Interactioni

Subunit structurei

Homodecamer (dimer of pentamers).3 Publications

Structurei

Secondary structure

1
263
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 129Combined sources
Beta strandi16 – 227Combined sources
Helixi25 – 284Combined sources
Helixi31 – 344Combined sources
Beta strandi35 – 373Combined sources
Helixi38 – 414Combined sources
Helixi43 – 5311Combined sources
Beta strandi56 – 605Combined sources
Helixi62 – 687Combined sources
Beta strandi71 – 733Combined sources
Beta strandi75 – 784Combined sources
Beta strandi93 – 964Combined sources
Helixi98 – 1036Combined sources
Beta strandi107 – 1137Combined sources
Helixi120 – 13718Combined sources
Beta strandi141 – 1455Combined sources
Helixi158 – 17114Combined sources
Beta strandi174 – 1796Combined sources
Helixi184 – 19310Combined sources
Turni194 – 1963Combined sources
Beta strandi199 – 2024Combined sources
Helixi210 – 22213Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 2354Combined sources
Helixi240 – 25112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-255.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP58315.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 252Substrate binding
Regioni177 – 1793Substrate binding
Regioni202 – 2043Substrate binding
Regioni231 – 2322Substrate binding

Sequence similaritiesi

Belongs to the DeoC/FbaB aldolase family.Curated

Phylogenomic databases

KOiK11645.
OMAiEWKMFEE.

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.

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.
YP_004892990.1. 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 .
RefSeqi WP_014127167.1. NC_016070.1.
YP_004892990.1. NC_016070.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OJX X-ray 1.90 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
1OK4 X-ray 2.10 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
1OK6 X-ray 2.40 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
1W8S X-ray 1.85 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
2YCE X-ray 1.93 A/B/C/D/E/F/G/H/I/J 1-263 [» ]
ProteinModelPortali P58315.
SMRi P58315. Positions 2-255.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CCC81912 ; CCC81912 ; TTX_1278 .
GeneIDi 11262157.
KEGGi ttn:TTX_1278.

Phylogenomic databases

KOi K11645.
OMAi EWKMFEE.

Enzyme and pathway databases

BioCyci TTEN768679:GJSY-1253-MONOMER.
SABIO-RK P58315.

Miscellaneous databases

EvolutionaryTracei P58315.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view ]
Pfami PF01791. DeoC. 1 hit.
[Graphical view ]
PIRSFi PIRSF038992. Aldolase_Ia. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Archaeal fructose-1,6-bisphosphate aldolases constitute a new family of archaeal type class I aldolases."
    Siebers B., Brinkmann H., Doerr C., Tjaden B., Lilie H., van der Oost J., Verhees C.H.
    J. Biol. Chem. 276:28710-28718(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, ENZYME REGULATION, SUBUNIT.
    Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1.
  3. "Crystal structure of an archaeal class I aldolase and the evolution of (betaalpha)8 barrel proteins."
    Lorentzen E., Pohl E., Zwart P., Stark A., Russell R.B., Knura T., Hensel R., Siebers B.
    J. Biol. Chem. 278:47253-47260(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, SUBUNIT.
  4. "Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates."
    Lorentzen E., Siebers B., Hensel R., Pohl E.
    Biochemistry 44:4222-4229(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT GLU-144 AND PHE-146 IN COMPLEX WITH SUBSTRATE ANALOGS, MUTAGENESIS OF TRP-144 AND TYR-146, REACTION MECHANISM, SUBUNIT.

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: October 29, 2014
This is version 62 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

External Data

Dasty 3