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P44480 (ALKH_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative KHG/KDPG aldolase

Including the following 2 domains:

  1. 4-hydroxy-2-oxoglutarate aldolase
    EC=4.1.3.16
    Alternative name(s):
    2-keto-4-hydroxyglutarate aldolase
    Short name=KHG-aldolase
  2. 2-dehydro-3-deoxy-phosphogluconate aldolase
    EC=4.1.2.14
    Alternative name(s):
    2-keto-3-deoxy-6-phosphogluconate aldolase
    Short name=KDPG-aldolase
    Phospho-2-dehydro-3-deoxygluconate aldolase
    Phospho-2-keto-3-deoxygluconate aldolase
Gene names
Name:eda
Ordered Locus Names:HI_0047
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP]
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length212 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.

2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate.

Pathway

Carbohydrate acid metabolism; 2-dehydro-3-deoxy-D-gluconate degradation; D-glyceraldehyde 3-phosphate and pyruvate from 2-dehydro-3-deoxy-D-gluconate: step 2/2.

Carbohydrate metabolism; glyoxylate and dicarboxylate metabolism.

Subunit structure

Homotrimer.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the KHG/KDPG aldolase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function2-dehydro-3-deoxy-phosphogluconate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

4-hydroxy-2-oxoglutarate aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 212212Putative KHG/KDPG aldolase
PRO_0000201041

Sites

Active site451 By similarity
Active site491 By similarity
Active site1331Schiff-base intermediate with KHG or pyruvate By similarity

Secondary structure

........................................ 212
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P44480 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 1D920F34AB4C14E3

FASTA21222,861
        10         20         30         40         50         60 
MSYTTQQIIE KLRELKIVPV IALDNADDIL PLADTLAKNG LSVAEITFRS EAAADAIRLL 

        70         80         90        100        110        120 
RANRPDFLIA AGTVLTAEQV VLAKSSGADF VVTPGLNPKI VKLCQDLNFP ITPGVNNPMA 

       130        140        150        160        170        180 
IEIALEMGIS AVKFFPAEAS GGVKMIKALL GPYAQLQIMP TGGIGLHNIR DYLAIPNIVA 

       190        200        210 
CGGSWFVEKK LIQSNNWDEI GRLVREVIDI IK 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Structural analysis of a set of proteins resulting from a bacterial genomics project."
Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., Gajiwala K.S., Gao X., He D., Hendle J. expand/collapse author list , Huber A., Hoda K., Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., Wright T.A., Wu L., Xu J., Harris T.J.R.
Proteins 60:787-796(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-212.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42023 Genomic DNA. Translation: AAC21725.1.
PIRA64045.
RefSeqNP_438220.1. NC_000907.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VHCX-ray1.89A/B/C/D/E/F2-212[»]
ProteinModelPortalP44480.
SMRP44480. Positions 2-212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING71421.HI0047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC21725; AAC21725; HI_0047.
GeneID950945.
KEGGhin:HI0047.
PATRIC20188547. VBIHaeInf48452_0047.

Phylogenomic databases

eggNOGCOG0800.
KOK01625.
OMAYCQELNI.
OrthoDBEOG67DPKT.
PhylomeDBP44480.

Enzyme and pathway databases

UniPathwayUPA00227.
UPA00856; UER00829.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]
PfamPF01081. Aldolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01182. eda. 1 hit.
PROSITEPS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP44480.

Entry information

Entry nameALKH_HAEIN
AccessionPrimary (citable) accession number: P44480
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names