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Protein
Submitted name:

Fructose 1,6-bisphosphate aldolase

Gene

cbbA

Organism
Hydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Protein predictedi

Functioni

GO - Molecular functioni

  1. aldehyde-lyase activity Source: InterPro
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

LyaseSAAS annotation

Keywords - Ligandi

Metal-bindingSAAS annotation, ZincSAAS annotation

Names & Taxonomyi

Protein namesi
Submitted name:
Fructose 1,6-bisphosphate aldolaseImported
Gene namesi
Name:cbbAImported
OrganismiHydrogenophilus thermoluteolus (Pseudomonas hydrogenothermophila)Imported
Taxonomic identifieri297 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaHydrogenophilalesHydrogenophilaceaeHydrogenophilus

Structurei

3D structure databases

ProteinModelPortaliQ9ZA13.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013097. Dabb.
IPR011008. Dimeric_a/b-barrel.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF07876. Dabb. 1 hit.
PF01116. F_bP_aldolase. 1 hit.
[Graphical view]
SMARTiSM00886. Dabb. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51502. S_R_A_B_BARREL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZA13-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVAASALLQ HAVANRYAIG AYDILDTTML EGVLLGAQRA EAPVLISIAE
60 70 80 90 100
VHTDQFDEAT LLAAVVEAAA AAPGTVAIHY DHGTTLDRLV RATQLGYTSL
110 120 130 140 150
MIDGSHLEWA ENVALTRRAA ALAHAVGFPL EGEIGYVPGE EGKDAELHPG
160 170 180 190 200
AIRYTEPDEA EAFVTETGCD WLAVSIGTVH GRFRGEPQLD LERLAAIRAR
210 220 230 240 250
LPRTPLVIHG GTGLSDEQFR ALVAAGANKI NYYTALVETA AAAAIDYRRW
260 270 280 290 300
DEQRLAAREA IAAEVERTCR VWGAAGHANV VLDVAPMVTP VEHVIFHCWS
310 320 330 340 350
SDVSDVAAMQ AEGVATLGAL PGVRRIAAGV AETPNAPYPY LWAMTFATPE
360 370 380 390
ALAHFRTHPE HQRFADSRFR PFASERITID FHLTYGNGRC ATPKSSRR
Length:398
Mass (Da):42,916
Last modified:April 30, 1999 - v1
Checksum:i5B40F03B89108312
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003906 Genomic DNA. Translation: BAA75221.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003906 Genomic DNA. Translation: BAA75221.1.

3D structure databases

ProteinModelPortaliQ9ZA13.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR013097. Dabb.
IPR011008. Dimeric_a/b-barrel.
IPR000771. Ketose_bisP_aldolase_II.
[Graphical view]
PfamiPF07876. Dabb. 1 hit.
PF01116. F_bP_aldolase. 1 hit.
[Graphical view]
SMARTiSM00886. Dabb. 1 hit.
[Graphical view]
SUPFAMiSSF54909. SSF54909. 1 hit.
PROSITEiPS51502. S_R_A_B_BARREL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The novel genes, cbbQ and cbbO, located downstream from the RubisCO genes of Pseudomonas hydrogenothermophila, affect the conformational states and activity of RubisCO."
    Hayashi N.R., Arai H., Kodama T., Igarashi Y.
    Biochem. Biophys. Res. Commun. 241:565-569(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TH-1Imported.
  2. Hayashi N.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: TH-1Imported.

Entry informationi

Entry nameiQ9ZA13_HYDTE
AccessioniPrimary (citable) accession number: Q9ZA13
Entry historyi
Integrated into UniProtKB/TrEMBL: April 30, 1999
Last sequence update: April 30, 1999
Last modified: March 31, 2015
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.