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Protein
Submitted name:

2-dehydro-3-deoxyphosphoheptonate aldolase

Gene

PF1690

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311ManganeseCombined sources
Metal bindingi201 – 2011Manganese; via tele nitrogenCombined sources
Metal bindingi227 – 2271ManganeseCombined sources
Metal bindingi238 – 2381ManganeseCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

TransferaseImported

Keywords - Ligandi

ManganeseCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi2.5.1.54. 5243.

Names & Taxonomyi

Protein namesi
Submitted name:
2-dehydro-3-deoxyphosphoheptonate aldolaseImported (EC:2.5.1.54Imported)
Gene namesi
Ordered Locus Names:PF1690Imported
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)Imported
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013 Componenti: Chromosome

PTM / Processingi

Proteomic databases

PRIDEiQ8U0A9.

Interactioni

Protein-protein interaction databases

STRINGi186497.PF1690.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCOX-ray2.25A/B1-262[»]
4C1KX-ray2.15A/B/C/D/E/F1-262[»]
4C1LX-ray1.80A/B1-262[»]
4GRSX-ray3.00A/B/C/D33-262[»]
ProteinModelPortaliQ8U0A9.
SMRiQ8U0A9. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8U0A9.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2876.
HOGENOMiHOG000023020.
KOiK03856.
OMAiPCTLESY.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01361. DAHP_synth_Bsub. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8U0A9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKYSKEYKEK TVVKINDVKF GEGFTIIAGP CSIESRDQIM KVAEFLAEVG
60 70 80 90 100
IKVLRGGAFK PRTSPYSFQG YGEKALRWMR EAADEYGLVT VTEVMDTRHV
110 120 130 140 150
ELVAKYSDIL QIGARNSQNF ELLKEVGKVE NPVLLKRGMG NTIQELLYSA
160 170 180 190 200
EYIMAQGNEN VILCERGIRT FETATRFTLD ISAVPVVKEL SHLPIIVDPS
210 220 230 240 250
HPAGRRSLVI PLAKAAYAIG ADGIMVEVHP EPEKALSDSQ QQLTFDDFLQ
260
LLKELEALGW KG
Length:262
Mass (Da):29,225
Last modified:June 1, 2002 - v1
Checksum:iED84D28FD5DEADC2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81814.1.
RefSeqiNP_579419.1. NC_003413.1.
WP_011012836.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81814; AAL81814; PF1690.
GeneIDi1469567.
KEGGipfu:PF1690.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009950 Genomic DNA. Translation: AAL81814.1.
RefSeqiNP_579419.1. NC_003413.1.
WP_011012836.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZCOX-ray2.25A/B1-262[»]
4C1KX-ray2.15A/B/C/D/E/F1-262[»]
4C1LX-ray1.80A/B1-262[»]
4GRSX-ray3.00A/B/C/D33-262[»]
ProteinModelPortaliQ8U0A9.
SMRiQ8U0A9. Positions 1-262.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1690.

Proteomic databases

PRIDEiQ8U0A9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81814; AAL81814; PF1690.
GeneIDi1469567.
KEGGipfu:PF1690.

Phylogenomic databases

eggNOGiCOG2876.
HOGENOMiHOG000023020.
KOiK03856.
OMAiPCTLESY.

Enzyme and pathway databases

BRENDAi2.5.1.54. 5243.

Miscellaneous databases

EvolutionaryTraceiQ8U0A9.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR006218. DAHP1/KDSA.
IPR006268. DAHP_syn_2.
[Graphical view]
PfamiPF00793. DAHP_synth_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01361. DAHP_synth_Bsub. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1Imported.
  2. "Substrate ambiguity and crystal structure of Pyrococcus furiosus 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase: an ancestral 3-deoxyald-2-ulosonate-phosphate synthase?"
    Schofield L.R., Anderson B.F., Patchett M.L., Norris G.E., Jameson G.B., Parker E.J.
    Biochemistry 44:11950-11962(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH MANGANESE.
  3. "Engineering allosteric control to an unregulated enzyme by transfer of a regulatory domain."
    Cross P.J., Allison T.M., Dobson R.C., Jameson G.B., Parker E.J.
    Proc. Natl. Acad. Sci. U.S.A. 110:2111-2116(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 33-262.
  4. "Destabilization of the homotetrameric assembly of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from the hyperthermophile Pyrococcus furiosus enhances enzymatic activity."
    Nazmi A.R., Schofield L.R., Dobson R.C., Jameson G.B., Parker E.J.
    J. Mol. Biol. 426:656-673(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH MANGANESE.

Entry informationi

Entry nameiQ8U0A9_PYRFU
AccessioniPrimary (citable) accession number: Q8U0A9
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2002
Last sequence update: June 1, 2002
Last modified: May 27, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.