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P19537 (ALF_CORGL) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. 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

Short name=FBP aldolase
Short name=FBPA
EC=4.1.2.13
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene names
Name:fba
Synonyms:fda
Ordered Locus Names:Cgl2770, cg3068
OrganismCorynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025) [Reference proteome] [HAMAP]
Taxonomic identifier196627 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Sequence similarities

Belongs to the class II fructose-bisphosphate aldolase family.

Ontologies

Keywords
   Biological processGlycolysis
   LigandMetal-binding
Zinc
   Molecular functionLyase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionfructose-bisphosphate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 344343Fructose-bisphosphate aldolase
PRO_0000178712

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

Experimental info

Sequence conflict2801Q → H in CAA35190. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P19537 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 745B189A2AC72BBF

FASTA34437,214
        10         20         30         40         50         60 
MPIATPEVYN EMLDRAKEGG FAFPAINCTS SETINAALKG FAEAESDGII QFSTGGAEFG 

        70         80         90        100        110        120 
SGLAVKNKVK GAVALAAFAH EAAKSYGINV ALHTDHCQKE VLDEYVRPLL AISQERVDRG 

       130        140        150        160        170        180 
ELPLFQSHMW DGSAVPIDEN LEIAQELLAK AKAANIILEV EIGVVGGEED GVEAKAGANL 

       190        200        210        220        230        240 
YTSPEDFEKT IDAIGTGEKG RYLLAATFGN VHGVYKPGNV KLRPEVLLEG QQVARKKLGL 

       250        260        270        280        290        300 
ADDALPFDFV FHGGSGSEKE KIEEALTYGV IKMNVDTDTQ YAFTRPIVSH MFENYNGVLK 

       310        320        330        340 
IDGEVGNKKA YDPRSYMKKA EQSMSERIIE SCQDLKSVGK TTSK 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, nucleotide sequence and fine-structural analysis of the Corynebacterium glutamicum fda gene: structural comparison of C. glutamicum fructose-1,6-biphosphate aldolase to class I and class II aldolases."
von der Osten C.H., Barbas C.F. III, Wong C.-H., Sinskey A.J.
Mol. Microbiol. 3:1625-1637(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
Strain: ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613.
[2]"The Corynebacterium glutamicum genome: features and impacts on biotechnological processes."
Ikeda M., Nakagawa S.
Appl. Microbiol. Biotechnol. 62:99-109(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[3]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X17313 Genomic DNA. Translation: CAA35190.1.
BA000036 Genomic DNA. Translation: BAC00164.1.
BX927156 Genomic DNA. Translation: CAF20791.1.
PIRS09283.
RefSeqNP_601964.1. NC_003450.3.
YP_227007.1. NC_006958.1.

3D structure databases

ProteinModelPortalP19537.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING196627.cg3068.

2D gel databases

World-2DPAGE0001:P19537.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC00164; BAC00164; BAC00164.
CAF20791; CAF20791; cg3068.
GeneID1020714.
KEGGcgb:cg3068.
cgl:NCgl2673.
PATRIC21497578. VBICorGlu203724_2701.

Phylogenomic databases

eggNOGCOG0191.
HOGENOMHOG000227794.
KOK01624.
OMAVDNEIND.
OrthoDBEOG69GZPB.

Enzyme and pathway databases

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...

Entry information

Entry nameALF_CORGL
AccessionPrimary (citable) accession number: P19537
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 100 of the entry and version 3 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