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P13243 (ALF_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 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:fbaA
Synonyms:fba, fba1, tsr
Ordered Locus Names:BSU37120
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length285 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.

Post-translational modification

Phosphorylated during sporulation. Ref.5

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 285285Probable fructose-bisphosphate aldolase
PRO_0000178705

Regions

Region210 – 2123Dihydroxyacetone phosphate binding By similarity
Region231 – 2344Dihydroxyacetone phosphate binding By similarity

Sites

Active site851Proton donor By similarity
Metal binding861Zinc 1; catalytic By similarity
Metal binding1071Zinc 2 By similarity
Metal binding1371Zinc 2 By similarity
Metal binding1811Zinc 1; catalytic By similarity
Metal binding2091Zinc 1; catalytic By similarity
Binding site501Glyceraldehyde 3-phosphate By similarity
Binding site1821Dihydroxyacetone phosphate; via amide nitrogen By similarity

Amino acid modifications

Modified residue2121Phosphothreonine Ref.6
Modified residue2341Phosphothreonine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P13243 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: 482D3CE048583BCF

FASTA28530,401
        10         20         30         40         50         60 
MPLVSMTEML NTAKEKGYAV GQFNLNNLEF TQAILQAAEE EKSPVILGVS EGAGRYMGGF 

        70         80         90        100        110        120 
KTVVAMVKAL MEEYKVTVPV AIHLDHGSSF ESCAKAIHAG FTSVMIDASH HPFEENVATT 

       130        140        150        160        170        180 
AKVVELAHFH GVSVEAELGT VGGQEDDVIA EGVIYADPKE CQELVERTGI DCLAPALGSV 

       190        200        210        220        230        240 
HGPYKGEPNL GFKEMEEIGK STGLPLVLHG GTGIPTADIK KSISLGTAKI NVNTENQISS 

       250        260        270        280 
AKAVRETLAA KPDEYDPRKY LGPAREAIKE TVIGKMREFG SSNQA

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and transcriptional analysis of the spo0F region of the Bacillus subtilis chromosome."
Trach K., Chapman J.W., Piggot P.J., Lecoq D., Hoch J.A.
J. Bacteriol. 170:4194-4208(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[2]"The amino acid sequence of a Bacillus subtilis phosphoprotein that matches an orfY-tsr coding sequence."
Mitchell C., Morris P.W., Lum L., Spiegelman G., Vary J.C.
Mol. Microbiol. 6:1345-1349(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26, SEQUENCE REVISION.
Strain: 168 / JH642.
[3]"The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
Microbiology 143:3313-3328(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Identification of proteins phosphorylated by ATP during sporulation of Bacillus subtilis."
Mitchell C., Morris P.W., Vary J.C.
J. Bacteriol. 174:2474-2477(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-16, PHOSPHORYLATION.
[6]"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-212 AND THR-234, MASS SPECTROMETRY.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M22039 Unassigned DNA. Translation: AAA16803.1.
S42590 Genomic DNA. Translation: AAB22716.1.
Z49782 Genomic DNA. Translation: CAA89873.1.
AL009126 Genomic DNA. Translation: CAB15729.1.
PIRD32354. S55426.
RefSeqNP_391593.1. NC_000964.3.

3D structure databases

ProteinModelPortalP13243.
SMRP13243. Positions 1-285.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU37120.

PTM databases

PhosSiteP0802211.

Proteomic databases

PaxDbP13243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15729; CAB15729; BSU37120.
GeneID937040.
KEGGbsu:BSU37120.
PATRIC18979460. VBIBacSub10457_3892.

Organism-specific databases

GenoListBSU37120. [Micado]

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227793.
KOK01624.
OMAAIKETVI.
ProtClustDBPRK08610.

Enzyme and pathway databases

BioCycBSUB:BSU37120-MONOMER.
SABIO-RKP13243.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
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.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF_BACSU
AccessionPrimary (citable) accession number: P13243
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents