NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
"Complete sequence of Anabaena variabilis ATCC 29413.";
Submitted (SEP-2005) 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

CP000117; ABA22714.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_323609.1; -.

3D structure databases

ModBase

Q3M8H2.

Enzyme and pathway databases

BioCyc

AVAR240292:AVA_3106-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).
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

IPR011342; Quinate/shikimate_5-DHase.
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.

TIGR00507; aroE; 1.

Genome annotation databases

GeneID

3680852; -.

GenomeReviews

CP000117_GR; Ava_3106.

KEGG

ava:Ava_3106; -.

NMPDR

fig|240292.3.peg.2535; -.

Phylogenomic databases

HOGENOM

Q3M8H2; -.

Genome annotation databases

CMR

Q3M8H2; Ava_3106.

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`	`1 289`	`289`	`Shikimate dehydrogenase.`	`PRO_1000021255`
`NP_BIND`	`131 135`	`5`	`NADP (By similarity).`
`ACT_SITE`	`70 70`		`Proton acceptor (Potential).`

Sequence information

Length: 289 AA [This is the length of the unprocessed precursor]

Molecular weight: 31410 Da [This is the MW of the unprocessed precursor]

CRC64: 36AE4B36C538BE0A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MITGKTKLLG VIGHPVEHSL SPVMHNAAIA QLGLDYVYLP FPIAPDNLEA AIALLATIGV 

        70         80         90        100        110        120 
VGFSVTIPHK QAIIPLLAEI SPVAQAIGAV NTVTRQNNQW VGTNTDIEGF IAPLQTTYKR 

       130        140        150        160        170        180 
DWSQQIAVIL GNGGAARAVV AGCYQLGFAE IHVVGRNVQR LEEFRHSWDN SPIAENLQVH 

       190        200        210        220        230        240 
TWDYLAKLVP QANLLVNTTP IGMYPQVDES PLSTEELANL QTGAIAYDLI YIPKPTQFLQ 

       250        260        270        280 
KAQQQGAIAI DGLEMLVQQG VAALKIWLQQ DDIPVDVMRQ ALQKHLGLV

Q3M8H2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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