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P99117 (ALF1_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase class 1

EC=4.1.2.13
Alternative name(s):
Fructose-bisphosphate aldolase class I
Short name=FBP aldolase
Gene names
Name:fda
Ordered Locus Names:SA2399
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. HAMAP-Rule MF_00729

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. HAMAP-Rule MF_00729

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 296295Fructose-bisphosphate aldolase class 1 HAMAP-Rule MF_00729
PRO_0000216905

Sites

Active site1751Proton acceptor By similarity
Active site2121Schiff-base intermediate with dihydroxyacetone-P By similarity

Sequences

Sequence LengthMass (Da)Tools
P99117 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: D63B1A3C7646725B

FASTA29633,042
        10         20         30         40         50         60 
MNKEQLEKMK NGKGFIAALD QSGGSTPKAL KEYGVNEDQY SNEDEMFQLV HDMRTRVVTS 

        70         80         90        100        110        120 
PSFSPDKILG AILFEQTMDR EVEGKYTADY LADKGVVPFL KVDKGLAEEQ NGVQLMKPID 

       130        140        150        160        170        180 
NLDSLLDRAN ERHIFGTKMR SNILELNEQG IKDVVEQQFE VAKQIIAKGL VPIIEPEVNI 

       190        200        210        220        230        240 
NAKDKAEIEK VLKAELKKGL DSLNADQLVM LKLTIPTEPN LYKELAEHPN VVRVVVLSGG 

       250        260        270        280        290 
YSREKANELL KDNDELIASF SRALASDLRA DQSKEEFDKA LGDAVESIYD ASVNKN 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB43704.1.
PIRF90067.
RefSeqNP_375725.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99117.
SMRP99117. Positions 1-293.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA2399.

PTM databases

PhosSiteP0909757.

2D gel databases

SWISS-2DPAGEP99117.

Proteomic databases

PRIDEP99117.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB43704; BAB43704; BAB43704.
GeneID1125328.
KEGGsau:SA2399.
PATRIC19577364. VBIStaAur116463_2600.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3588.
HOGENOMHOG000073502.
KOK01623.
OMAYTGDYLA.
OrthoDBEOG6M6JJT.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-2562-MONOMER.
UniPathwayUPA00109; UER00183.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00729. FBP_aldolase_1.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
IPR023014. FBP_aldolase_I_bac.
[Graphical view]
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameALF1_STAAN
AccessionPrimary (citable) accession number: P99117
Secondary accession number(s): Q99R31
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways