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P67475 (ALF_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase
Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Ordered Locus Names:Rv0363c, MT0379
ORF Names:MTCY13E10.25c
OrganismMycobacterium tuberculosis [Reference proteome] [HAMAP]
Taxonomic identifier1773 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Cofactor

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

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Miscellaneous

Was identified as a high-confidence drug target.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Fructose-bisphosphate aldolase
PRO_0000178722

Regions

Region253 – 2553Dihydroxyacetone phosphate binding By similarity
Region274 – 2774Dihydroxyacetone phosphate binding By similarity

Sites

Active site951Proton donor By similarity
Metal binding961Zinc 1; catalytic By similarity
Metal binding1311Zinc 2 By similarity
Metal binding1611Zinc 2 By similarity
Metal binding2121Zinc 1; catalytic By similarity
Metal binding2521Zinc 1; catalytic By similarity
Binding site531Glyceraldehyde 3-phosphate By similarity
Binding site2131Dihydroxyacetone phosphate; via amide nitrogen By similarity

Secondary structure

1 .......................................................... 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67475 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 04FA3E1123F72FB1

FASTA34436,544
        10         20         30         40         50         60 
MPIATPEVYA EMLGQAKQNS YAFPAINCTS SETVNAAIKG FADAGSDGII QFSTGGAEFG 

        70         80         90        100        110        120 
SGLGVKDMVT GAVALAEFTH VIAAKYPVNV ALHTDHCPKD KLDSYVRPLL AISAQRVSKG 

       130        140        150        160        170        180 
GNPLFQSHMW DGSAVPIDEN LAIAQELLKA AAAAKIILEI EIGVVGGEED GVANEINEKL 

       190        200        210        220        230        240 
YTSPEDFEKT IEALGAGEHG KYLLAATFGN VHGVYKPGNV KLRPDILAQG QQVAAAKLGL 

       250        260        270        280        290        300 
PADAKPFDFV FHGGSGSLKS EIEEALRYGV VKMNVDTDTQ YAFTRPIAGH MFTNYDGVLK 

       310        320        330        340 
VDGEVGVKKV YDPRSYLKKA EASMSQRVVQ ACNDLHCAGK SLTH

« Hide

References

[1]"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence."
Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. expand/collapse author list , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G.
Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25618 / H37Rv.
[2]"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains."
Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. expand/collapse author list , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.
J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 1551 / Oshkosh.
[3]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX842573 Genomic DNA. Translation: CAB08571.1.
AE000516 Genomic DNA. Translation: AAK44600.1.
AL123456 Genomic DNA. Translation: CCP43093.1.
PIRD70576.
RefSeqNP_214877.1. NC_000962.3.
NP_334786.1. NC_002755.2.
YP_006513689.1. NC_018143.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP67475.
SMRP67475. Positions 2-344.
ModBaseSearch...

Protein-protein interaction databases

STRING83332.Rv0363c.

Proteomic databases

PaxDbP67475.
PRIDEP67475.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK44600; AAK44600; MT0379.
GeneID13318230.
886474.
923567.
KEGGmtc:MT0379.
mtu:Rv0363c.
mtv:RVBD_0363c.
PATRIC18122544. VBIMycTub22151_0406.

Organism-specific databases

TubercuListRv0363c.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAREGEKTM.
ProtClustDBPRK09197.

Enzyme and pathway databases

BRENDA4.1.2.13. 3445.
SABIO-RKP67475.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR006411. Fruct_bisP_bact.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamPF01116. F_bP_aldolase. 1 hit.
[Graphical view]
PIRSFPIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsTIGR00167. cbbA. 1 hit.
TIGR01520. FruBisAldo_II_A. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP67475.
ChEMBLCHEMBL1287620.
EvolutionaryTraceP67475.

Entry information

Entry nameALF_MYCTU
AccessionPrimary (citable) accession number: P67475
Secondary accession number(s): L0T684, O06313
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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