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P27995

- ALF1_RHOSH

UniProt

P27995 - ALF1_RHOSH

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Protein
Fructose-bisphosphate aldolase 1
Gene
cfxA
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

UniPathwayiUPA00109; UER00183.
UPA00116.

Names & Taxonomyi

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 359359Fructose-bisphosphate aldolase 1
PRO_0000178731Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

3D structure databases

ProteinModelPortaliP27995.

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.

P27995-1 [UniParc]FASTAAdd to Basket

« Hide

MALITLRQLL DHAAERLQGY GVPAFNINNM EQGLAILAAA RACDAPVIAS    50
RGARSYAGDI MLRHIVEALA EMYPQIPICL HQDHGNNEAT CLSAIRHGFT 100
SVMMDGSLQA DMKTVASYDY NVDITRRVTD AAHWVGASVE GELGVLGSLE 150
KGEAEAEDGS GAEGKLDHSQ MLTDPDQAVE FVQATRVDAL AIAMGTSHGA 200
YKFSRKPDGE ILAMRVIEEI HARLPATHLV MHGSSSVAAR LQDLINAHGA 250
DMPQTYGVPV EEIERGIRHG VRKVNIDTDC RMALTGQFRK VAMESPKEFD 300
ARKFMIPAMK EMEALVRDRF ERFGTAGNAS KITVIPMDDM AKRYASGALD 350
PAVATAKAA 359
Length:359
Mass (Da):38,872
Last modified:August 1, 1992 - v1
Checksum:i6A898301D5A2F1ED
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64624 Genomic DNA. Translation: AAA26114.1.
PIRiB40767. ADRFAS.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64624 Genomic DNA. Translation: AAA26114.1 .
PIRi B40767. ADRFAS.

3D structure databases

ProteinModelPortali P27995.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
UPA00116 .

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. "Nucleotide sequence, transcriptional analysis, and expression of genes encoded within the form I CO2 fixation operon of Rhodobacter sphaeroides."
    Gibson J.L., Falcone D.L., Tabita F.R.
    J. Biol. Chem. 266:14646-14653(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiALF1_RHOSH
AccessioniPrimary (citable) accession number: P27995
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 11, 2014
This is version 68 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 I ribulose-bisphosphate carboxylase operon, which predominates when carbon dioxide is limiting.

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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