Shikimate dehydrogenase - Methanocaldococcus jannaschii

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Reviewed, UniProtKB/Swiss-Prot Q58484 (AROE_METJA)

Last modified February 9, 2010. Version 74. 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:	MJ1084

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

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Protein attributes

Sequence length	282 AA.
Sequence status	Complete.
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 phosphoenolpyruvate: step 4/7. HAMAP MF_00222
Subunit structure	Homodimer. 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 – 282

282

Shikimate dehydrogenase HAMAP MF_00222

PRO_0000136060

Regions

Nucleotide binding

130 – 134

NADP HAMAP MF_00222

Nucleotide binding

152 – 157

NADP HAMAP MF_00222

Nucleotide binding

247 – 251

NADP By similarity

Sites

Active site

Proton acceptor Potential

Binding site

106

Substrate By similarity

Binding site

196

NADP; via carbonyl oxygen HAMAP MF_00222

Binding site

200

NADP HAMAP MF_00222

Binding site

224

NADP; via carbonyl oxygen HAMAP MF_00222

Secondary structure

282

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

Q58484-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: E7398E5D642F7BD1
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FASTA

282

30,877

        10         20         30         40         50         60 
MINAKTKVIG LIGHPVEHSF SPIMHNAAFK DKGLNYVYVA FDVLPENLKY VIDGAKALGI 

        70         80         90        100        110        120 
VGFNVTIPHK IEIMKYLDEI DKDAQLIGAV NTIKIEDGKA IGYNTDGIGA RMALEEEIGR 

       130        140        150        160        170        180 
VKDKNIVIYG AGGAARAVAF ELAKDNNIII ANRTVEKAEA LAKEIAEKLN KKFGEEVKFS 

       190        200        210        220        230        240 
GLDVDLDGVD IIINATPIGM YPNIDVEPIV KAEKLREDMV VMDLIYNPLE TVLLKEAKKV 

       250        260        270        280 
NAKTINGLGM LIYQGAVAFK IWTGVEPNIE VMKNAIIDKI TK

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution." Padyana A.K., Burley S.K. Structure 11:1005-1013(2003) [PubMed: 12906831] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L77117 Genomic DNA. Translation: AAB99086.1.

PIR

C64435.

RefSeq

NP_248077.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NVT	X-ray	2.35	A/B	1-282	[»]

ModBase

Search...

Genome annotation databases

GeneID

1451980.

GenomeReviews

Gene locus MJ1084 in contig L77117_GR.

KEGG

mja:MJ1084.

NMPDR

fig|243232.1.peg.1114.

TIGR

MJ1084.

Phylogenomic databases

HOGENOM

HBG553408.

OMA

FRLWTGV.

Enzyme and pathway databases

BRENDA

1.1.1.25. 256362.

Family and domain databases

HAMAP

MF_00222. Shikimate_DH_AroE.
[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_METJA

Accession

Primary (citable) accession number: Q58484

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	February 9, 2010
This is version 74 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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