Reviewed, UniProtKB/Swiss-Prot P44480 (ALKH_HAEIN)

Names and origin

Protein names

Recommended name:
    Putative KHG/KDPG aldolase
Including the following 2 domains:
    1- Recommended name:
            4-hydroxy-2-oxoglutarate aldolase
              EC=4.1.3.16
        Alternative name(s):
            2-keto-4-hydroxyglutarate aldolase
              Short name=KHG-aldolase
    2- Recommended name:
            2-dehydro-3-deoxy-phosphogluconate aldolase
              EC=4.1.2.14
        Alternative name(s):
            Phospho-2-dehydro-3-deoxygluconate aldolase
            Phospho-2-keto-3-deoxygluconate aldolase
            2-keto-3-deoxy-6-phosphogluconate aldolase
              Short name=KDPG-aldolase

Gene names

Name:	eda
Ordered Locus Names:	HI0047

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	212 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate. 2-dehydro-3-deoxy-D-gluconate 6-phosphate = 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 component	Cytoplasm
Ligand	Schiff base
Molecular function	Lyase
Technical term	3D-structure Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	2-dehydro-3-deoxy-phosphogluconate aldolase activity Inferred from electronic annotation. Source: EC 4-hydroxy-2-oxoglutarate aldolase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 212

212

Putative KHG/KDPG aldolase

PRO_0000201041

Sites

Active site

45

1

By similarity

Active site

49

1

By similarity

Active site

133

1

Schiff-base intermediate with KHG or pyruvate By similarity

Secondary structure

1

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212

Helix Strand Turn

Details...

Helix

5 – 15

11

Beta strand

17 – 21

5

Helix

26 – 28

3

Helix

29 – 38

10

Beta strand

43 – 47

5

Helix

53 – 63

11

Beta strand

68 – 73

6

Helix

77 – 86

10

Beta strand

89 – 92

4

Helix

98 – 106

9

Helix

118 – 126

9

Beta strand

131 – 134

4

Turn

135 – 141

7

Helix

142 – 150

9

Turn

151 – 155

5

Beta strand

157 – 163

7

Turn

166 – 168

3

Helix

169 – 173

5

Beta strand

181 – 183

3

Helix

185 – 187

3

Helix

189 – 193

5

Helix

197 – 211

15

Sequences

	Sequence		Length	Mass (Da)
	P44480-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 1D920F34AB4C14E3	FASTA	212	22,861
	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

References

	« Hide 'large scale' referencesShow '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. , 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: 7542800] [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. , 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: 16021622] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-212.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L42023 Genomic DNA. Translation: AAC21725.1.

PIR

A64045.

RefSeq

NP_438220.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VHC	X-ray	1.89	A/B/C/D/E/F	2-212	[»]

ModBase

Search...

Genome annotation databases

GeneID

950945.

GenomeReviews

Gene locus HI0047 in contig L42023_GR.

KEGG

hin:HI0047.

NMPDR

fig|71421.1.peg.46.

TIGR

HI0047.

Phylogenomic databases

HOGENOM

P44480.

OMA

AKNWDEI

Enzyme and pathway databases

BioCyc

HINF71421:HI_0047-MON.

BRENDA

4.1.2.14. 109.
4.1.3.16. 109.

Family and domain databases

InterPro

IPR000887. Aldlse_KDPG_KHG.
IPR013785. Aldolase_TIM.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

Pfam

PF01081. Aldolase. 1 hit.
[Graphical view]

TIGRFAMs

TIGR01182. eda. 1 hit.

PROSITE

PS00159. ALDOLASE_KDPG_KHG_1. 1 hit.
PS00160. ALDOLASE_KDPG_KHG_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ALKH_HAEIN

Accession

Primary (citable) accession number: P44480

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)