P58315 (ALF1_THETK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	fba
Ordered Locus Names:	TTX_1278

Organism

Thermoproteus tenax (strain ATCC 35583 / NBRC 100435 / JCM 9277 / Kra 1) [Complete proteome] [HAMAP]

Taxonomic identifier

768679 [NCBI]

Taxonomic lineage

cellular organisms › Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Thermoproteus › Thermoproteus tenax

Protein attributes

Sequence length	263 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible cleavage of fructose 1,6-bisphosphate (FBP) to glyceraldehyde 3-phosphate (GAP) and dihydroxyacetone phosphate (DHAP).
Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.1
Enzyme regulation	Activated by citrate. Ref.1
Subunit structure	Homodecamer (dimer of pentamers). Ref.1 Ref.3 Ref.4
Subcellular location	Cytoplasm Probable.
Sequence similarities	Belongs to the DeoC/FbaB aldolase family.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 263

263

Fructose-bisphosphate aldolase class 1

PRO_0000138952

Regions

Region

24 – 25

2

Substrate binding

Region

177 – 179

3

Substrate binding

Region

202 – 204

3

Substrate binding

Region

231 – 232

2

Substrate binding

Sites

Active site

146

1

Proton donor

Active site

177

1

Schiff-base intermediate with dihydroxyacetone-P

Binding site

29

1

Substrate

Binding site

33

1

Substrate

Binding site

144

1

Substrate

Binding site

148

1

Substrate

Experimental info

Mutagenesis

144

1

W → E: Loss of FBP aldolase activity; when associated with F-146. Ref.4

Mutagenesis

146

1

Y → 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. Ref.4

Secondary structure

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263

Helix Strand Turn

Details...

Helix

4 – 12

9

Beta strand

16 – 22

7

Helix

25 – 28

4

Helix

31 – 34

4

Beta strand

35 – 37

3

Helix

38 – 41

4

Helix

43 – 53

11

Beta strand

56 – 60

5

Helix

62 – 68

7

Beta strand

71 – 73

3

Beta strand

75 – 78

4

Beta strand

93 – 96

4

Helix

98 – 103

6

Beta strand

107 – 113

7

Helix

120 – 137

18

Beta strand

141 – 145

5

Helix

158 – 171

14

Beta strand

174 – 179

6

Helix

184 – 193

10

Turn

194 – 196

3

Beta strand

199 – 202

4

Helix

210 – 222

13

Beta strand

227 – 231

5

Helix

232 – 235

4

Helix

240 – 251

12

Sequences

	Sequence		Length	Mass (Da)
	P58315 [UniParc]. Last modified October 18, 2001. Version 1. Checksum: 1399A6D0CF4F0D9E	FASTA	263	28,705
	10 20 30 40 50 60 MANLTEKFLR IFARRGKSII LAYDHGIEHG PADFMDNPDS ADPEYILRLA RDAGFDGVVF 70 80 90 100 110 120 QRGIAEKYYD GSVPLILKLN GKTTLYNGEP VSVANCSVEE AVSLGASAVG YTIYPGSGFE 130 140 150 160 170 180 WKMFEELARI KRDAVKFDLP LVVWSYPRGG KVVNETAPEI VAYAARIALE LGADAMKIKY 190 200 210 220 230 240 TGDPKTFSWA VKVAGKVPVL MSGGPKTKTE EDFLKQVEGV LEAGALGIAV GRNVWQRRDA 250 260 LKFARALAEL VYGGKKLAEP LNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The complete genome sequence of Thermoproteus tenax: a physiologically versatile member of the Crenarchaeota." Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D., Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M., Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C., Hensel R. PLoS ONE 6:E24222-E24222(2011) [PubMed] [Europe PMC] [Abstract] 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ310483 Genomic DNA. Translation: CAC48235.1.
FN869859 Genomic DNA. Translation: CCC81912.1.

RefSeq

YP_004892990.1. NC_016070.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P58315.

SMR

P58315. Positions 2-255.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CCC81912; CCC81912; TTX_1278.

GeneID

11262157.

KEGG

ttn:TTX_1278.

Organism-specific databases

CMR

Search...

Phylogenomic databases

KO

K11645.

Enzyme and pathway databases

SABIO-RK

P58315.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR013785. Aldolase_TIM.
IPR002915. DeoC/FbaB/lacD_aldolase.
[Graphical view]

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P58315.

Entry information

Entry name

ALF1_THETK

Accession

Primary (citable) accession number: P58315
Secondary accession number(s): G4RK17

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	October 18, 2001
Last modified:	April 3, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program