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Protein

Fructose-bisphosphate aldolase

Gene

cbbA

Organism
Xanthobacter flavus
Status
Reviewed-Annotation score: -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.1 Publication

Catalytic activityi

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

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit. One is catalytic and the other provides a structural contribution.By similarity

Enzyme regulationi

Activity is stimulated by Fe2+ in autotrophically grown cells.1 Publication

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Pathwayi: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.By similarity
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Fructose-bisphosphate aldolase (cbbA)
This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei50Glyceraldehyde 3-phosphateBy similarity1
Active sitei83Proton donorBy similarity1
Metal bindingi84Zinc 1; catalyticBy similarity1
Metal bindingi105Zinc 2By similarity1
Metal bindingi142Zinc 2By similarity1
Metal bindingi198Zinc 1; catalyticBy similarity1
Binding sitei199Dihydroxyacetone phosphate; via amide nitrogenBy similarity1
Metal bindingi232Zinc 1; catalyticBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionLyase
Biological processCalvin cycle, Glycolysis
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183
UPA00116

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase1 Publication (EC:4.1.2.131 Publication)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Gene namesi
Name:cbbA1 Publication
OrganismiXanthobacter flavus
Taxonomic identifieri281 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeXanthobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001787551 – 354Fructose-bisphosphate aldolaseAdd BLAST354

Proteomic databases

PRIDEiQ56815

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ56815
SMRiQ56815
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 235Dihydroxyacetone phosphate bindingBy similarity3
Regioni275 – 278Dihydroxyacetone phosphate bindingBy similarity4

Sequence similaritiesi

Family and domain databases

CDDicd00947 TBP_aldolase_IIB, 1 hit
Gene3Di3.20.20.70, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000771 FBA_II
IPR006412 Fruct_bisP_Calv
PfamiView protein in Pfam
PF01116 F_bP_aldolase, 1 hit
PIRSFiPIRSF001359 F_bP_aldolase_II, 1 hit
TIGRFAMsiTIGR00167 cbbA, 1 hit
TIGR01521 FruBisAldo_II_B, 1 hit
PROSITEiView protein in PROSITE
PS00602 ALDOLASE_CLASS_II_1, 1 hit
PS00806 ALDOLASE_CLASS_II_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q56815-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALVSMRQLL DHAADDSYGL PAFNVNNMEQ VKAIMDAARA TSSPVILQGS
60 70 80 90 100
AGARKYAGEP FLRHLIAAAV EAYPEIPVVM HQDHGASPAV CMGAIKSGFS
110 120 130 140 150
SVMMDGSLKE DGKTPADYDY NVSVTAKVVE LAHAVGVSVE GELGCLGSLE
160 170 180 190 200
TGKGEAEDGH GAEEALDHSK LLTDPDEAAQ FVKATQCDAL AIAIGTSHGA
210 220 230 240 250
YKFTRKPTGD ILAIDRIKAI HQRIPTTHLV MHGSSSVPQE LLEEIRTYGG
260 270 280 290 300
DIKETYGVPV EEIQEGIRYG VRKVNIDTDI RLAMTAAIRR VGAKNKSEFD
310 320 330 340 350
PRKFMAAAME EAKKVCIARF EAFGSAGKAE KIRAIELDEM AKRYASGELA

QVVH
Length:354
Mass (Da):37,982
Last modified:November 1, 1996 - v1
Checksum:iDDF44661B527E4B7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U29134 Genomic DNA Translation: AAA96742.1

Similar proteinsi

Entry informationi

Entry nameiALF_XANFL
AccessioniPrimary (citable) accession number: Q56815
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 70 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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