[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.; Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.

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 .
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

CP000728; ABS42848.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001391837.1; -.

3D structure databases

ModBase

A7GGC7.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0005488;	Molecular function: binding (inferred from electronic annotation from InterPro).
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).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_00222; -; 1.
PBIL [Tree]

InterPro

IPR013708; Shikimate_DHase-bd_N.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Pfam

PF01488; Shikimate_DH; 1.
PF08501; Shikimate_dh_N; 1.
Pfam graphical view of domain structure.

ProtoNet

A7GGC7.

Genome annotation databases

GeneID

5405239; -.

GenomeReviews

CP000728_GR; CLI_2602.

KEGG

cbf:CLI_2602; -.

CMR

A7GGC7; CLI_2602.

Other

UniRef

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

Keywords

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 258`	`258`	`Shikimate dehydrogenase.`	`PRO_1000021276`
`NP_BIND`	`125 129`	`5`	`NADP (By similarity).`
`ACT_SITE`	`65 65`		`Proton acceptor (Potential).`

Sequence information

Length: 258 AA [This is the length of the unprocessed precursor]

Molecular weight: 29726 Da [This is the MW of the unprocessed precursor]

CRC64: EFBF67F83F9CDAB2 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYTTGLIGKN INYSESPEIH NNYYKKNNIP FFYKIFNLKQ DQIDDFIKNL HKNNIKGFNV 

        70         80         90        100        110        120 
TIPYKETILQ YLNDIVYPAD KIGAVNTVAV QEDKLIGYNT DYIGFIKSLQ YYNIQVKNFK 

       130        140        150        160        170        180 
CLIIGSGGSA KCIYYALKEL NARDICIVSR NPEKARLKFE EKVKILNIKD ENKLDRYDLI 

       190        200        210        220        230        240 
VNCTPIGGPN FKEQKPIELK EIKKNCVVYD LNYTPKRSKL LKEAKENGAF IINGEKMLIF 

       250 
QAYSAIGLWC LNGIKGGR

A7GGC7 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