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Protein

Fructose-bisphosphate aldolase

Gene

cbbA

Organism
Sinorhizobium medicae (strain WSM419) (Ensifer medicae)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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

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

Pathway: 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.

Pathway: glycolysis

This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. Glucose-6-phosphate isomerase (pgi), Glucose-6-phosphate isomerase (pgiA)
  3. Pyrophosphate--fructose 6-phosphate 1-phosphotransferase (pfp)
  4. Fructose-bisphosphate aldolase (cbbA), Fructose-bisphosphate aldolase (Smed_2654)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Glyceraldehyde 3-phosphateBy similarity
Active sitei83 – 831Proton donorBy similarity
Metal bindingi84 – 841Zinc 1; catalyticBy similarity
Metal bindingi105 – 1051Zinc 2By similarity
Metal bindingi142 – 1421Zinc 2By similarity
Metal bindingi198 – 1981Zinc 1; catalyticBy similarity
Binding sitei199 – 1991Dihydroxyacetone phosphate; via amide nitrogenBy similarity
Metal bindingi232 – 2321Zinc 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Calvin cycle, Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSMED366394:GJAL-3984-MONOMER.
UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
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:cbbA
Ordered Locus Names:Smed_3923
Encoded oniPlasmid pSMED010 Publication
OrganismiSinorhizobium medicae (strain WSM419) (Ensifer medicae)
Taxonomic identifieri366394 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
ProteomesiUP000001108 Componenti: Plasmid pSMED01

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Fructose-bisphosphate aldolasePRO_0000178730Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP56888.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni233 – 2353Dihydroxyacetone phosphate bindingBy similarity
Regioni275 – 2784Dihydroxyacetone phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiYIAAMTR.
OrthoDBiEOG6HXJ7B.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARITLRQLL DHAAERSYGV PAFNINNMEQ GLAIMEAARA CDAPVILQVS
60 70 80 90 100
RGARSYANDI MLAKMMEALE VMYPDIPLCI HQDHGNNVAT CLTAIQHGFT
110 120 130 140 150
SVMMDGSLKE DAKTPADYAY NAMITTEVSR LAHMVGASVE GELGCLGSLE
160 170 180 190 200
TGHGEAEDGH GFEGALDRSQ LLTDPDEAAR FVAETGVDAL AVAIGTSHGA
210 220 230 240 250
YKFTRKPTGE VLAMDVIEKI HERLPDTHIV MHGSSSVPQE WQDVFNAHGG
260 270 280 290 300
EMRETYGVPV EEIVRGIRFG VRKVNIDTDL RLAAAAAFRR VADTSRTEFD
310 320 330 340 350
PRKFLKPAMD AMSAVCKARF EAFGTAGNAS RIKVVPMAEM ARRYASGSLK

PQAKRAEAA
Length:359
Mass (Da):38,925
Last modified:November 13, 2007 - v2
Checksum:i00D2342753333700
GO

Sequence cautioni

The sequence AAF25378.1 differs from that shown. Reason: Frameshift at positions 100 and 120. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 902AT → PN in AAF25378 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF211846 Genomic DNA. Translation: AAF25378.1. Frameshift.
CP000739 Genomic DNA. Translation: ABR62733.1.
RefSeqiWP_011969555.1. NC_009620.1.
YP_001312666.1. NC_009620.1.

Genome annotation databases

EnsemblBacteriaiABR62733; ABR62733; Smed_3923.
GeneIDi5318708.
KEGGismd:Smed_3923.
PATRICi23613392. VBISinMed134228_0369.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF211846 Genomic DNA. Translation: AAF25378.1. Frameshift.
CP000739 Genomic DNA. Translation: ABR62733.1.
RefSeqiWP_011969555.1. NC_009620.1.
YP_001312666.1. NC_009620.1.

3D structure databases

ProteinModelPortaliP56888.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABR62733; ABR62733; Smed_3923.
GeneIDi5318708.
KEGGismd:Smed_3923.
PATRICi23613392. VBISinMed134228_0369.

Phylogenomic databases

eggNOGiCOG0191.
HOGENOMiHOG000227792.
KOiK01624.
OMAiYIAAMTR.
OrthoDBiEOG6HXJ7B.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
UPA00116.
BioCyciSMED366394:GJAL-3984-MONOMER.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEiPS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genetic regulation of C1 metabolism in Sinorhizobium meliloti."
    Fenner B.J., Tiwari R.P., Dilworth M.J.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete sequence of Sinorhizobium medicae WSM419 plasmid pSMED01."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G., Richardson P.
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: WSM419.

Entry informationi

Entry nameiALF_SINMW
AccessioniPrimary (citable) accession number: P56888
Secondary accession number(s): A6UGF3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2007
Last modified: June 24, 2015
This is version 84 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, Plasmid

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.