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 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 (LH57_05150), Glucose-6-phosphate isomerase (pgi)
  3. ATP-dependent 6-phosphofructokinase (pfkA), 6-phosphofructokinase (LH57_16435), 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)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

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

GO - Biological processi

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

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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
  • extracellular region Source: MTBBASE
  • plasma membrane Source: MTBBASE
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1287620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 344344Fructose-bisphosphate aldolasePRO_0000178722Add
BLAST

Proteomic databases

PaxDbiP9WQA3.

Interactioni

Protein-protein interaction databases

STRINGi83332.Rv0363c.

Chemistry

BindingDBiP9WQA3.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Beta strandi23 – 275Combined sources
Helixi31 – 4313Combined sources
Beta strandi48 – 525Combined sources
Helixi54 – 618Combined sources
Turni63 – 653Combined sources
Helixi68 – 8316Combined sources
Beta strandi86 – 883Combined sources
Beta strandi90 – 945Combined sources
Helixi99 – 1046Combined sources
Helixi106 – 11813Combined sources
Beta strandi126 – 1305Combined sources
Helixi137 – 15317Combined sources
Beta strandi157 – 1637Combined sources
Beta strandi166 – 1694Combined sources
Beta strandi172 – 1743Combined sources
Helixi178 – 1803Combined sources
Helixi184 – 19411Combined sources
Turni195 – 1995Combined sources
Beta strandi202 – 2065Combined sources
Beta strandi211 – 2133Combined sources
Helixi225 – 23814Combined sources
Beta strandi249 – 2513Combined sources
Helixi259 – 2679Combined sources
Beta strandi270 – 2756Combined sources
Helixi277 – 29317Combined sources
Helixi295 – 2984Combined sources
Helixi308 – 3114Combined sources
Helixi313 – 33422Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-344.
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

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

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.

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
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. Positions 2-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi83332.Rv0363c.

Chemistry

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.
BRENDAi4.1.2.13. 3445.

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: ATCC 25618 / H37Rv.
  2. "targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis."
    Raman K., Yeturu K., Chandra N.
    BMC Syst. Biol. 2:109-109(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 25618 / H37Rv.

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: December 9, 2015
This is version 17 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.