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P29271

- ALF2_RHOSH

UniProt

P29271 - ALF2_RHOSH

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Protein

Fructose-bisphosphate aldolase 2

Gene
cfxB
Organism
Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Status
Reviewed - Annotation score: 4 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

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 sitei83 – 831Proton donor By similarity
Metal bindingi84 – 841Zinc 1; catalytic By similarity
Metal bindingi105 – 1051Zinc 2 By similarity
Metal bindingi142 – 1421Zinc 2 By similarity
Metal bindingi198 – 1981Zinc 1; catalytic By similarity
Binding sitei199 – 1991Dihydroxyacetone phosphate; via amide nitrogen By similarity
Metal bindingi232 – 2321Zinc 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. glycolytic process Source: UniProtKB-UniPathway
  2. reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Calvin cycle, Glycolysis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-5054-MONOMER.
UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase 2 (EC:4.1.2.13)
Short name:
FBP aldolase
Short name:
FBPA
Alternative name(s):
Fructose-1,6-bisphosphate aldolase
Fructose-bisphosphate aldolase II
Gene namesi
Name:cfxB
OrganismiRhodobacter sphaeroides (Rhodopseudomonas sphaeroides)
Taxonomic identifieri1063 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRhodobacter

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Fructose-bisphosphate aldolase 2PRO_0000178733Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP29271.

Family & Domainsi

Region

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

Sequence similaritiesi

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.

P29271-1 [UniParc]FASTAAdd to Basket

« Hide

MALITLRQLL DHAAEQGYGV PAFNINNMEQ GLAIMEAARA CDAPVIIQAS    50
RGARSYANDI MLAKMIEALA AIYPEIPLCM HQDHGNNEAT CMTAIRHGFT 100
SVMMDGSLKA DAKTPADYDY NVDITARVSH MAHWVGASVE GELGVLGSLE 150
TGESEAEDGH GAEGKLDHSQ LLTDPDQAVD FVKKTQVDAL AIACGTSHGA 200
YKFSRKPDGE ILAMSVIEAI HKKLPDTHLV MHGSSSVPQE LQDIINAFGG 250
AMPQTFGVPV EEIVRGIKMG VRKVNIDTDC RMAMTGQFRR IAQQTPSEFD 300
PRKFLKPAMD AMRDLCKQRL EAFGTAGQAG KIRIIPMDDM AKRYASGALA 350
PKTA 354
Length:354
Mass (Da):38,269
Last modified:December 1, 1992 - v1
Checksum:i9F547E84FC72ACF5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M68914 Genomic DNA. Translation: AAA26157.1.
PIRiD41080.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M68914 Genomic DNA. Translation: AAA26157.1 .
PIRi D41080.

3D structure databases

ProteinModelPortali P29271.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
UPA00116 .
BioCyci RETL1328306-WGS:GSTH-5054-MONOMER.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR006412. Fruct_bisP_Calv.
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.
TIGR01521. FruBisAldo_II_B. 1 hit.
PROSITEi PS00602. ALDOLASE_CLASS_II_1. 1 hit.
PS00806. ALDOLASE_CLASS_II_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Identification, expression, and deduced primary structure of transketolase and other enzymes encoded within the form II CO2 fixation operon of Rhodobacter sphaeroides."
    Chen J.-H., Gibson J.L., McCue L.A., Tabita F.R.
    J. Biol. Chem. 266:20447-20452(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiALF2_RHOSH
AccessioniPrimary (citable) accession number: P29271
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: July 9, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is encoded within the form II ribulose-bisphosphate carboxylase operon.

Documents

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

External Data

Dasty 3

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