Reviewed, UniProtKB/Swiss-Prot P58315 (ALF1_THETE)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase class 1
    EC=4.1.2.13
Alternative name(s):
    Fructose-biphosphate aldolase class I
      Short name=FBP aldolase

Gene names

Name:

fba

Organism

Thermoproteus tenax

Taxonomic identifier

2271 [NCBI]

Taxonomic lineage

Archaea › Crenarchaeota › Thermoprotei › Thermoproteales › Thermoproteaceae › Thermoproteus

Protein attributes

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

General annotation (Comments)

Catalytic activity	D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
Enzyme regulation	Activated by citrate.
Subunit structure	Homooligomer.
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
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

Sites

Active site

177

1

Schiff-base intermediate with dihydroxyacetone-P By similarity

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 – 35

5

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 – 178

5

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)
	P58315-1 [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

[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: 11387336] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: Kra 1 / DSM 2078.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ310483 Genomic DNA. Translation: CAC48235.1.

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	[»]
1W8R	X-ray	1.93	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	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.1.2.13. 191220.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR002915. DeoC/AroFGH_arch.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01791. DeoC. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALF1_THETE

Accession

Primary (citable) accession number: P58315

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	October 18, 2001
Last modified:	June 16, 2009
This is version 41 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)