Shikimate dehydrogenase - Haemophilus influenzae

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Reviewed, UniProtKB/Swiss-Prot P43876 (AROE_HAEIN)

Last modified June 16, 2009. Version 70. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
Shikimate dehydrogenase
EC=1.1.1.25

Gene names

Name:	aroE
Ordered Locus Names:	HI0655

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

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Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Shikimate + NADP⁺ = 3-dehydroshikimate + NADPH. HAMAP MF_00222
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 4/7. HAMAP MF_00222
Subunit structure	Monomer. Ref.2
Sequence similarities	Belongs to the shikimate dehydrogenase family.

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Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: HAMAP oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	NADP or NADPH binding Inferred from electronic annotation. Source: InterPro shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 272

272

Shikimate dehydrogenase HAMAP MF_00222

PRO_0000136006

Regions

Nucleotide binding

126 – 130

NADP HAMAP MF_00222

Nucleotide binding

149 – 154

NADP HAMAP MF_00222

Nucleotide binding

238 – 242

NADP By similarity

Sites

Active site

Proton acceptor Potential

Binding site

102

Substrate By similarity

Binding site

189

NADP; via amide nitrogen HAMAP MF_00222

Binding site

190

NADP; via amide nitrogen HAMAP MF_00222

Secondary structure

272

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P43876-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 3B7A92AF22D4470B
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FASTA

272

29,760

        10         20         30         40         50         60 
MDLYAVWGNP IAQSKSPLIQ NKLAAQTHQT MEYIAKLGDL DAFEQQLLAF FEEGAKGCNI 

        70         80         90        100        110        120 
TSPFKERAYQ LADEYSQRAK LAEACNTLKK LDDGKLYADN TDGIGLVTDL QRLNWLRPNQ 

       130        140        150        160        170        180 
HVLILGAGGA TKGVLLPLLQ AQQNIVLANR TFSKTKELAE RFQPYGNIQA VSMDSIPLQT 

       190        200        210        220        230        240 
YDLVINATSA GLSGGTASVD AEILKLGSAF YDMQYAKGTD TPFIALCKSL GLTNVSDGFG 

       250        260        270 
MLVAQAAHSF HLWRGVMPDF VSVYEQLKKA ML

« Hide

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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. 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]	"The crystal structure of shikimate dehydrogenase (AroE) reveals a unique NADPH binding mode." Ye S., Von Delft F., Brooun A., Knuth M.W., Swanson R.V., McRee D.E. J. Bacteriol. 185:4144-4151(2003) [PubMed: 12837789] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

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Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC22314.1.

PIR

H64084.

RefSeq

NP_438815.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P74	X-ray	2.40	A/B	1-272	[»]
1P77	X-ray	1.95	A	1-272	[»]

ModBase

Search...

Genome annotation databases

GeneID

949697.

GenomeReviews

Gene locus HI0655 in contig L42023_GR.

KEGG

hin:HI0655.

NMPDR

fig|71421.1.peg.625.

TIGR

HI0655.

Phylogenomic databases

HOGENOM

P43876.

OMA

P43876. YDMMYGR.

Enzyme and pathway databases

BioCyc

HINF71421:HI_0655-MON.

BRENDA

1.1.1.25. 109.

Family and domain databases

HAMAP

MF_00222.
[Tree]

InterPro

IPR016040. NAD(P)-bd_dom.
IPR011342. Quinate/shikimate_5-DH.
IPR013708. Shikimate_DH-bd_N.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]

Gene3D

G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.

Pfam

PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00507. aroE. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

AROE_HAEIN

Accession

Primary (citable) accession number: P43876

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 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)

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