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Protein

Fructose-bisphosphate aldolase

Gene

fba

Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

Pathwayi: 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), Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase (pfkA), ATP-dependent 6-phosphofructokinase (pfkA), Putative ATP-dependent 6-phosphofructokinase isozyme 2 (pfkB)
  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)DescriptionActionsGraphical viewLength
Binding sitei53Glyceraldehyde 3-phosphateBy similarity1
Active sitei95Proton donorBy similarity1
Metal bindingi96Zinc 1; catalyticBy similarity1
Metal bindingi131Zinc 2By similarity1
Metal bindingi161Zinc 2By similarity1
Metal bindingi212Zinc 1; catalyticBy similarity1
Binding sitei213Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi252Zinc 1; catalyticBy similarity1

GO - Molecular functioni

  • fructose-bisphosphate aldolase activity Source: MTBBASE
  • zinc ion binding Source: MTBBASE

GO - Biological processi

  • gluconeogenesis Source: GO_Central
  • glycolytic process Source: MTBBASE
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMTBH37RV:G185E-4487-MONOMER.
BRENDAi4.1.2.13. 3445.
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:Rv0363c
ORF Names:MTCY13E10.25c
OrganismiMycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Taxonomic identifieri83332 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex
Proteomesi
  • UP000001584 Componenti: Chromosome

Organism-specific databases

TubercuListiRv0363c.

Subcellular locationi

GO - Cellular componenti

  • cell wall Source: MTBBASE
  • cytosol Source: GO_Central
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1287620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787221 – 344Fructose-bisphosphate aldolaseAdd BLAST344

Proteomic databases

PaxDbiP9WQA3.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv0363c.

Chemistry databases

BindingDBiP9WQA3.

Structurei

Secondary structure

1344
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 18Combined sources13
Beta strandi23 – 27Combined sources5
Helixi31 – 43Combined sources13
Beta strandi48 – 52Combined sources5
Helixi54 – 61Combined sources8
Turni63 – 65Combined sources3
Helixi68 – 83Combined sources16
Beta strandi86 – 88Combined sources3
Beta strandi90 – 94Combined sources5
Helixi99 – 104Combined sources6
Helixi106 – 118Combined sources13
Beta strandi126 – 130Combined sources5
Helixi137 – 153Combined sources17
Beta strandi157 – 163Combined sources7
Beta strandi166 – 169Combined sources4
Beta strandi172 – 174Combined sources3
Helixi178 – 180Combined sources3
Helixi184 – 194Combined sources11
Turni195 – 199Combined sources5
Beta strandi202 – 206Combined sources5
Beta strandi211 – 213Combined sources3
Helixi225 – 238Combined sources14
Beta strandi249 – 251Combined sources3
Helixi259 – 267Combined sources9
Beta strandi270 – 275Combined sources6
Helixi277 – 293Combined sources17
Helixi295 – 298Combined sources4
Helixi308 – 311Combined sources4
Helixi313 – 334Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EKLX-ray1.51A1-344[»]
3EKZX-ray2.07A1-344[»]
3ELFX-ray1.31A1-344[»]
4A21X-ray2.35A/B/C/D1-344[»]
4A22X-ray1.90A/B/C/D1-344[»]
4DEFX-ray1.64A1-344[»]
4DELX-ray1.58A1-344[»]
4LV4X-ray2.08A1-344[»]
ProteinModelPortaliP9WQA3.
SMRiP9WQA3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni253 – 255Dihydroxyacetone phosphate bindingBy similarity3
Regioni274 – 277Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4107RCW. Bacteria.
COG0191. LUCA.
KOiK01624.
OMAiRMSKMGM.
PhylomeDBiP9WQA3.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR006411. Fruct_bisP_bact.
[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.

P9WQA3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPIATPEVYA EMLGQAKQNS YAFPAINCTS SETVNAAIKG FADAGSDGII
60 70 80 90 100
QFSTGGAEFG SGLGVKDMVT GAVALAEFTH VIAAKYPVNV ALHTDHCPKD
110 120 130 140 150
KLDSYVRPLL AISAQRVSKG GNPLFQSHMW DGSAVPIDEN LAIAQELLKA
160 170 180 190 200
AAAAKIILEI EIGVVGGEED GVANEINEKL YTSPEDFEKT IEALGAGEHG
210 220 230 240 250
KYLLAATFGN VHGVYKPGNV KLRPDILAQG QQVAAAKLGL PADAKPFDFV
260 270 280 290 300
FHGGSGSLKS EIEEALRYGV VKMNVDTDTQ YAFTRPIAGH MFTNYDGVLK
310 320 330 340
VDGEVGVKKV YDPRSYLKKA EASMSQRVVQ ACNDLHCAGK SLTH
Length:344
Mass (Da):36,544
Last modified:April 16, 2014 - v1
Checksum:i04FA3E1123F72FB1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43093.1.
PIRiD70576.
RefSeqiNP_214877.1. NC_000962.3.
WP_003401856.1. NZ_KK339370.1.

Genome annotation databases

EnsemblBacteriaiCCP43093; CCP43093; Rv0363c.
GeneIDi886474.
KEGGimtu:Rv0363c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL123456 Genomic DNA. Translation: CCP43093.1.
PIRiD70576.
RefSeqiNP_214877.1. NC_000962.3.
WP_003401856.1. NZ_KK339370.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3EKLX-ray1.51A1-344[»]
3EKZX-ray2.07A1-344[»]
3ELFX-ray1.31A1-344[»]
4A21X-ray2.35A/B/C/D1-344[»]
4A22X-ray1.90A/B/C/D1-344[»]
4DEFX-ray1.64A1-344[»]
4DELX-ray1.58A1-344[»]
4LV4X-ray2.08A1-344[»]
ProteinModelPortaliP9WQA3.
SMRiP9WQA3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0363c.

Chemistry databases

BindingDBiP9WQA3.
ChEMBLiCHEMBL1287620.

Proteomic databases

PaxDbiP9WQA3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCCP43093; CCP43093; Rv0363c.
GeneIDi886474.
KEGGimtu:Rv0363c.

Organism-specific databases

TubercuListiRv0363c.

Phylogenomic databases

eggNOGiENOG4107RCW. Bacteria.
COG0191. LUCA.
KOiK01624.
OMAiRMSKMGM.
PhylomeDBiP9WQA3.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciMTBH37RV:G185E-4487-MONOMER.
BRENDAi4.1.2.13. 3445.

Miscellaneous databases

PROiP9WQA3.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000771. FBA_II.
IPR006411. Fruct_bisP_bact.
[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...

Entry informationi

Entry nameiALF_MYCTU
AccessioniPrimary (citable) accession number: P9WQA3
Secondary accession number(s): L0T684, O06313, P67475
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: November 30, 2016
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Was identified as a high-confidence drug target.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh
    Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.