SubmitCancel

Skip Header

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

P13243

- ALF_BACSU

UniProt

P13243 - ALF_BACSU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Probable fructose-bisphosphate aldolase
Gene
fbaA, fba, fba1, tsr, BSU37120
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Glyceraldehyde 3-phosphate By similarity
Active sitei85 – 851Proton donor By similarity
Metal bindingi86 – 861Zinc 1; catalytic By similarity
Metal bindingi107 – 1071Zinc 2 By similarity
Metal bindingi137 – 1371Zinc 2 By similarity
Metal bindingi181 – 1811Zinc 1; catalytic By similarity
Binding sitei182 – 1821Dihydroxyacetone phosphate; via amide nitrogen By similarity
Metal bindingi209 – 2091Zinc 1; catalytic By similarity

GO - Molecular functioni

  1. fructose-bisphosphate aldolase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. fructose 1,6-bisphosphate metabolic process Source: InterPro
  2. glycolytic process Source: UniProtKB-UniPathway
  3. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis, Sporulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU37120-MONOMER.
SABIO-RKP13243.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 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:fbaA
Synonyms:fba, fba1, tsr
Ordered Locus Names:BSU37120
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU37120. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Probable fructose-bisphosphate aldolase
PRO_0000178705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei212 – 2121Phosphothreonine1 Publication
Modified residuei234 – 2341Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated during sporulation.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP13243.

PTM databases

PhosSiteiP0802211.

Interactioni

Protein-protein interaction databases

IntActiP13243. 1 interaction.
MINTiMINT-8365567.
STRINGi224308.BSU37120.

Structurei

3D structure databases

ProteinModelPortaliP13243.
SMRiP13243. Positions 1-285.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni210 – 2123Dihydroxyacetone phosphate binding By similarity
Regioni231 – 2344Dihydroxyacetone phosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227793.
KOiK01624.
OMAiCTTRYEA.
OrthoDBiEOG6HXJ7B.
PhylomeDBiP13243.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
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.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P13243-1 [UniParc]FASTAAdd to Basket

« Hide

MPLVSMTEML NTAKEKGYAV GQFNLNNLEF TQAILQAAEE EKSPVILGVS    50
EGAGRYMGGF KTVVAMVKAL MEEYKVTVPV AIHLDHGSSF ESCAKAIHAG 100
FTSVMIDASH HPFEENVATT AKVVELAHFH GVSVEAELGT VGGQEDDVIA 150
EGVIYADPKE CQELVERTGI DCLAPALGSV HGPYKGEPNL GFKEMEEIGK 200
STGLPLVLHG GTGIPTADIK KSISLGTAKI NVNTENQISS AKAVRETLAA 250
KPDEYDPRKY LGPAREAIKE TVIGKMREFG SSNQA 285
Length:285
Mass (Da):30,401
Last modified:June 1, 1994 - v2
Checksum:i482D3CE048583BCF
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22039 Unassigned DNA. Translation: AAA16803.1.
S42590 Genomic DNA. Translation: AAB22716.1.
Z49782 Genomic DNA. Translation: CAA89873.1.
AL009126 Genomic DNA. Translation: CAB15729.1.
PIRiS55426. D32354.
RefSeqiNP_391593.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15729; CAB15729; BSU37120.
GeneIDi937040.
KEGGibsu:BSU37120.
PATRICi18979460. VBIBacSub10457_3892.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M22039 Unassigned DNA. Translation: AAA16803.1 .
S42590 Genomic DNA. Translation: AAB22716.1 .
Z49782 Genomic DNA. Translation: CAA89873.1 .
AL009126 Genomic DNA. Translation: CAB15729.1 .
PIRi S55426. D32354.
RefSeqi NP_391593.1. NC_000964.3.

3D structure databases

ProteinModelPortali P13243.
SMRi P13243. Positions 1-285.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P13243. 1 interaction.
MINTi MINT-8365567.
STRINGi 224308.BSU37120.

PTM databases

PhosSitei P0802211.

Proteomic databases

PaxDbi P13243.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15729 ; CAB15729 ; BSU37120 .
GeneIDi 937040.
KEGGi bsu:BSU37120.
PATRICi 18979460. VBIBacSub10457_3892.

Organism-specific databases

GenoListi BSU37120. [Micado ]

Phylogenomic databases

eggNOGi COG0191.
HOGENOMi HOG000227793.
KOi K01624.
OMAi CTTRYEA.
OrthoDBi EOG6HXJ7B.
PhylomeDBi P13243.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci BSUB:BSU37120-MONOMER.
SABIO-RK P13243.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR011289. Fruc_bis_ald_class-2.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view ]
Pfami PF01116. F_bP_aldolase. 1 hit.
[Graphical view ]
PIRSFi PIRSF001359. F_bP_aldolase_II. 1 hit.
TIGRFAMsi TIGR00167. cbbA. 1 hit.
TIGR01859. fruc_bis_ald_. 1 hit.
PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiALF_BACSU
AccessioniPrimary (citable) accession number: P13243
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi