Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Mycobacterium leprae (strain TN)
Status
Reviewed-Annotation score: 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

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Pathway: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase (pfkA)
  4. Fructose-bisphosphate aldolase (fba)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Glyceraldehyde 3-phosphateBy similarity
Active sitei95 – 951Proton donorBy similarity
Metal bindingi96 – 961Zinc 1; catalyticBy similarity
Metal bindingi131 – 1311Zinc 2By similarity
Metal bindingi161 – 1611Zinc 2By similarity
Metal bindingi212 – 2121Zinc 1; catalyticBy similarity
Binding sitei213 – 2131Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi252 – 2521Zinc 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

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
Ordered Locus Names:ML0286
ORF Names:MLCB4.29c
OrganismiMycobacterium leprae (strain TN)
Taxonomic identifieri272631 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacterium
ProteomesiUP000000806 Componenti: Chromosome

Organism-specific databases

LepromaiML0286.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345Fructose-bisphosphate aldolasePRO_0000178721Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi272631.ML0286.

Structurei

3D structure databases

ProteinModelPortaliO69600.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni253 – 2553Dihydroxyacetone phosphate bindingBy similarity
Regioni274 – 2774Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG69GZPB.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
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.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O69600-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIATPEIYA EMLRRAKENS YAFPAINCTS SETVNAAIKG FADAGSDGII
60 70 80 90 100
QFSTGGAEFA SGLGVKDMVT GAVALAKFTH TIAAKYPINV ALHTDHCPKD
110 120 130 140 150
KLDSYVRPLL AISARRVATG KDPLFGSHMW DGSAIPIDEN LAIAQDLLKD
160 170 180 190 200
AAAAKIILEV EIGVVGGEED GVAGEINEKL YTTPKDFVKT IDALGAGEHG
210 220 230 240 250
KYLLAATFGN VHGVYKPGNV KLRPDILAEG QKVAAAKLSQ SEGSKPFDFV
260 270 280 290 300
FHGGSGSEKS EIEEALRYGV VKMNVDTDTQ YAFTRPVSGH MFTNYDGVLK
310 320 330 340
VDGDVGNKKV YDPRSYLKKA EASMTERVLE ACNDLRCAGK SVAAS
Length:345
Mass (Da):36,741
Last modified:August 1, 1998 - v1
Checksum:i29FE8474C41D00C7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL023514 Genomic DNA. Translation: CAA18950.1.
AL583918 Genomic DNA. Translation: CAC29794.1.
PIRiF86944.
RefSeqiNP_301326.1. NC_002677.1.
WP_010907650.1. NC_002677.1.

Genome annotation databases

EnsemblBacteriaiCAC29794; CAC29794; CAC29794.
GeneIDi908824.
KEGGimle:ML0286.
PATRICi18051002. VBIMycLep78757_0450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL023514 Genomic DNA. Translation: CAA18950.1.
AL583918 Genomic DNA. Translation: CAC29794.1.
PIRiF86944.
RefSeqiNP_301326.1. NC_002677.1.
WP_010907650.1. NC_002677.1.

3D structure databases

ProteinModelPortaliO69600.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272631.ML0286.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC29794; CAC29794; CAC29794.
GeneIDi908824.
KEGGimle:ML0286.
PATRICi18051002. VBIMycLep78757_0450.

Organism-specific databases

LepromaiML0286.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227794.
KOiK01624.
OMAiRMSKMGM.
OrthoDBiEOG69GZPB.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
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.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: TN.

Entry informationi

Entry nameiALF_MYCLE
AccessioniPrimary (citable) accession number: O69600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 93 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.