Fructose-1,6-bisphosphate aldolase

Preferred order of sections

Names and origin

Protein names	Submitted name: Fructose-1,6-bisphosphate aldolase EMBL AAF22441.1 EC=4.1.2.13 EMBL AAF22441.1
Organism	Thermus aquaticus EMBL AAF22441.1
Taxonomic identifier	271 [NCBI]
Taxonomic lineage	Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus

Protein attributes

Sequence length	305 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Zinc SAAS SAAS000771
Molecular function	Lyase SAAS SAAS000771 EMBL AAF22441.1
Technical term	3D-structure PDB 1RV8 PDB 1RVG
Gene Ontology (GO)
Biological process	fructose 1,6-bisphosphate metabolic process Inferred from electronic annotation. Source: InterPro glycolysis Inferred from electronic annotation. Source: InterPro
Molecular function	fructose-bisphosphate aldolase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

81

1

Cobalt; via tele nitrogen PDB 1RV8 PDB 1RVG

Metal binding

132

1

Cobalt PDB 1RV8 PDB 1RVG

Metal binding

178

1

Cobalt; via tele nitrogen PDB 1RV8 PDB 1RVG

Metal binding

208

1

Cobalt; via pros nitrogen PDB 1RV8 PDB 1RVG

Sequences

Sequence

Length

Mass (Da)

Tools

Q9RHA2 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6A150BE84785D003
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FASTA

305

33,093

        10         20         30         40         50         60 
MLVTGLEILK KAREEGYGVG AFNVNNMEFL QAVLEAAEEQ RSPVILALSE GAMKYGGRAL 

        70         80         90        100        110        120 
TLMAVELAKE ARVPVAVHLD HGSSYESVLR ALRAGFTSVM IDKSHEDFET NVRETRRVVE 

       130        140        150        160        170        180 
AAHAVGVTVE AELGRLAGIE EHVAVDEKDA LLTNPEEARI FMERTGADYL AVAIGTSHGA 

       190        200        210        220        230        240 
YKGKGRPFID HARLERIARL VPAPLVLHGA SAVPPELVER FRASGGEIGE AAGIHPEDIK 

       250        260        270        280        290        300 
KAISLGIAKI NTDTDLRLAF TALIREALNK NPKEFDPRKY LGPAREAVKE VVKSRMELFG 


SVGRA

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References

[1]	Sauve V., Sygusch J. Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: YT-1 EMBL AAF22441.1.
[2]	"Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase." Izard T., Sygusch J. J. Biol. Chem. 279:11825-11833(2004) [PubMed: 14699122] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF052204 Genomic DNA. Translation: AAF22441.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RV8	X-ray	2.30	A/B/C/D	1-305	[»]
1RVG	X-ray	2.00	A/B/C/D	1-305	[»]

ProteinModelPortal

Q9RHA2.

SMR

Q9RHA2. Positions 1-305.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

4.1.2.13. 118.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01116. F_bP_aldolase. 1 hit.
[Graphical view]

PIRSF

PIRSF001359. F_bP_aldolase_II. 1 hit.

TIGRFAMs

TIGR00167. CbbA. 1 hit.
TIGR01859. Fruc_bis_ald_. 1 hit.

ProtoNet

Search...

Entry information

Entry name

Q9RHA2_THEAQ

Accession

Primary (citable) accession number: Q9RHA2

Entry history

Integrated into UniProtKB/TrEMBL:	May 1, 2000
Last sequence update:	May 1, 2000
Last modified:	July 27, 2011
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)