[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 13059 / LMG 3658 / NCIB 10332 / AS019 / 613; Joy J., O'Donohue M., Dunican L.K.; "The cloning and phylogenetic analysis of the 3-dehydroquinase gene from Corynebacterium glutamicum."; Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; Nakagawa S.; "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025; DOI=10.1016/S0168-1656(03)00154-8; PubMed=12948626 [NCBI, ExPASy, EBI, Israel, Japan] Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.; "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."; J. Biotechnol. 104:5-25(2003).
[4]	X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND SUBUNIT. Schoepe J., Niefind K., Schomburg D.; "Crystal structure of the quinate dehydrogenase from Corynebacterium glutamicum."; Submitted (NOV-2006) to the PDB data bank.

Comments

CATALYTIC ACTIVITY: Shikimate + NADP⁺ = 3-dehydroshikimate + NADPH.
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 4/7 .
PATHWAY: Context: Aromatic amino acids biosynthesis .
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the shikimate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF124518; AAD30993.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BA000036; BAB97817.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX927149; CAF19140.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_599671.1; -.
YP_224726.1; -.

3D structure databases

PDB

2NLO; X-ray; 1.64 A; A=1-283.

[ExPASy / RCSB / EBI]

PDBsum

2NLO; -.

ModBase

Q9X5C9.

Enzyme and pathway databases

BioCyc

CGLU196627-1:CG0504-MON; -.

Ontologies

GO:0004764;	Molecular function: shikimate 5-dehydrogenase activity (inferred from electronic annotation from HAMAP).
GO:0009073;	Biological process: aromatic amino acid family biosynthetic process (inferred from electronic annotation from HAMAP).
QuickGo view.

Family and domain databases

HAMAP

MF_00222; -; 1.
PBIL [Tree]

InterPro

IPR016040; NAD(P)-bd.
IPR013708; Shikimate_DHase-bd_N.
IPR000594; ThiF_NAD_FAD_bd.
Graphical view of domain structure.

Gene3D

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

Pfam

PF08501; Shikimate_dh_N; 1.
PF00899; ThiF; 1.
Pfam graphical view of domain structure.

BLOCKS

Q9X5C9.

Genome annotation databases

GeneID

1021203; -.
3343183; -.

GenomeReviews

BX927147_GR; cg0504.
BA000036_GR; Cgl0424.

KEGG

cgb:cg0504; -.
cgl:NCgl0409; -.

Phylogenomic databases

HOGENOM

Q9X5C9; -.

Genome annotation databases

CMR

Q9X5C9; Cgl0424.

Other

ProtoNet

Q9X5C9.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; NADP; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 283`	`283`	`Shikimate dehydrogenase.`	`PRO_0000136001`
`NP_BIND`	`134 138`	`5`	`NADP (By similarity).`
`NP_BIND`	`158 163`	`6`	`NADP (Potential).`
`NP_BIND`	`251 255`	`5`	`NADP (By similarity).`
`BINDING`	`110 110`		`Substrate (By similarity).`
`CONFLICT`	`29 29`		`A -> P (in Ref. 1; AAD30993).`
`CONFLICT`	`135 143`		`AGGVGNAVA -> RRRRKRSR (in Ref. 1; AAD30993).`
`CONFLICT`	`211 211`		`Missing (in Ref. 1; AAD30993).`
`CONFLICT`	`272 273`		`DV -> T (in Ref. 1; AAD30993).`
`STRAND`	`5 13`	`9`
`HELIX`	`19 29`	`11`
`STRAND`	`34 40`	`7`
`TURN`	`44 48`	`5`
`HELIX`	`51 60`	`10`
`STRAND`	`65 68`	`4`
`TURN`	`73 76`	`4`
`HELIX`	`77 79`	`3`
`STRAND`	`80 83`	`4`
`HELIX`	`85 90`	`6`
`STRAND`	`95 98`	`4`
`STRAND`	`104 107`	`4`
`HELIX`	`109 121`	`13`
`STRAND`	`128 133`	`6`
`HELIX`	`139 148`	`10`
`STRAND`	`152 160`	`9`
`HELIX`	`161 175`	`15`
`STRAND`	`180 185`	`6`
`HELIX`	`188 194`	`7`
`STRAND`	`195 200`	`6`
`HELIX`	`216 218`	`3`
`STRAND`	`224 228`	`5`
`STRAND`	`231 234`	`4`
`HELIX`	`236 244`	`9`
`STRAND`	`247 249`	`3`
`HELIX`	`252 267`	`16`
`HELIX`	`273 281`	`9`

Sequence information

Length: 283 AA [This is the length of the unprocessed precursor]

Molecular weight: 29697 Da [This is the MW of the unprocessed precursor]

CRC64: 2DBCE25D186DAF74 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD LKTLLDAALY 

        70         80         90        100        110        120 
LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA TGHTTGHNTD VSGFGRGMEE 

       130        140        150        160        170        180 
GLPNAKLDSV VQVGAGGVGN AVAYALVTHG VQKLQVADLD TSRAQALADV INNAVGREAV 

       190        200        210        220        230        240 
VGVDARGIED VIAAADGVVN ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA 

       250        260        270        280 
ARALGCETLD GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL

Q9X5C9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools