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P94453

- ALF_GEOSE

UniProt

P94453 - ALF_GEOSE

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Protein
Fructose-bisphosphate aldolase
Gene
fba
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis By similarity.

Catalytic activityi

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

Cofactori

Binds 2 zinc ions per subunit. One is catalytic and the other provides a structural contribution By similarity.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Glyceraldehyde 3-phosphate By similarity
Active sitei85 – 851Proton donor By similarity
Metal bindingi86 – 861Zinc 1; catalytic By similarity
Metal bindingi107 – 1071Zinc 2 By similarity
Metal bindingi137 – 1371Zinc 2 By similarity
Metal bindingi181 – 1811Zinc 1; catalytic By similarity
Binding sitei182 – 1821Dihydroxyacetone phosphate; via amide nitrogen By similarity
Metal bindingi209 – 2091Zinc 1; catalytic By similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. fructose 1,6-bisphosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:fba
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287Fructose-bisphosphate aldolase
PRO_0000178704Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei212 – 2121Phosphothreonine By similarity
Modified residuei234 – 2341Phosphothreonine By similarity

Keywords - PTMi

Phosphoprotein

Structurei

3D structure databases

ProteinModelPortaliP94453.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2123Dihydroxyacetone phosphate binding By similarity
Regioni231 – 2344Dihydroxyacetone phosphate binding By similarity

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFiPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsiTIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94453-1 [UniParc]FASTAAdd to Basket

« Hide

MSLVSMKEML NEALRGKYAV GQFNINNLEW TQAILAAAEE EKSPVILGVS    50
EGAARYMGGF KTVVNMVKGL MEDMNITVPV AIHLDHGSSF EKCKAAIDAG 100
FTSVMIDASH HPFEENVRIT SQVVEYAHAR GVSVEAELGI VGGQEDDVVG 150
EGVIYADPKE CEELVKRTGI DCLAPALGSV HGPYKGEPKL GFAEMEKIRD 200
LTGIPLVLHG GTGIPTEQIQ RAISLGTSKI NVNTENQIAF TKAVRELLAK 250
DPNVYDPRKI IGPGRDAIKA TVIGKMREFG SSGKAAQ 287
Length:287
Mass (Da):30,818
Last modified:July 15, 1999 - v3
Checksum:i7D9831D2CEDD07C3
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11135 Genomic DNA. Translation: CAA72018.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y11135 Genomic DNA. Translation: CAA72018.1 .

3D structure databases

ProteinModelPortali P94453.
ModBasei Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view ]
Pfami PF01116. F_bP_aldolase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsi TIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Desai S.Y., Littlechild J.A.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiALF_GEOSE
AccessioniPrimary (citable) accession number: P94453
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: June 11, 2014
This is version 69 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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