Q32GE1 (YDIB_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Quinate/shikimate dehydrogenase
EC=1.1.1.282

Alternative name(s):
NAD-dependent shikimate 5-dehydrogenase 2

Gene names

Name:	ydiB
Ordered Locus Names:	SDY_1475

Organism

Shigella dysenteriae serotype 1 (strain Sd197)

Taxonomic identifier

300267 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella

Protein attributes

Sequence length	297 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Catalytic activity	L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H. HAMAP MF_01578 Shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H. HAMAP MF_01578
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. HAMAP MF_01578
Subunit structure	Homodimer By similarity. HAMAP MF_01578
Sequence similarities	Belongs to the shikimate dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	nucleotide binding Inferred from electronic annotation. Source: InterPro quinate 3-dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC quinate 3-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC shikimate 3-dehydrogenase (NAD+) activity Inferred from electronic annotation. Source: EC shikimate 3-dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 297	297	Quinate/shikimate dehydrogenase HAMAP MF_01578		PRO_0000280776
Regions
	Nucleotide binding	140 – 144	5	NAD By similarity
	Nucleotide binding	164 – 167	4	NAD By similarity
	Nucleotide binding	264 – 268	5	NAD By similarity
Sites
	Active site	80	1	Proton acceptor Potential
	Binding site	116	1	Substrate By similarity
	Binding site	214	1	NAD; via amide nitrogen By similarity
	Binding site	244	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q32GE1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 88B8547CFBFE6D5B	FASTA	297	32,390
	10 20 30 40 50 60 MKNTCSTNWK HHPAKYELIG LMAYPIRHSL SPEMQNKALE KAGLPFTYMA FEVDNDSFPG 70 80 90 100 110 120 AIEGLKALKM RGTGVSMPNK QLACEYVDEL TPAAKLVGAI NTIVNDDGYL RGYNTDGTGH 130 140 150 160 170 180 IRAIKESGFD IKGKTMVLLG AGGASTAIGA QGAIEGLKEI KLFNRRDEFF DKALAFAQRV 190 200 210 220 230 240 NENTDCVVTV TDLADQQAFA EALASDDILT NGTKVGMKPL ENKSLVNDIS LLHPGLLVTE 250 260 270 280 290 CVYNPHMTKL LQQAQQAGCK TIDGYGMLLW QGAEQFTLWT GKDFPLEYVK QVMGFGA

References

[1]

"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery." Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q. Nucleic Acids Res. 33:6445-6458(2005) [PubMed: 16275786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sd197.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000034 Genomic DNA. Translation: ABB61614.1.
RefSeq	YP_403105.1. NC_007606.1.
3D structure databases
HSSP	HSSP built from PDB template 2GPT based on UniProtKB Q9SQT8.
ProteinModelPortal	Q32GE1.
SMR	Q32GE1. Positions 14-297.
ModBase	Search...
Protein-protein interaction databases
STRING	Q32GE1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000083001; EBESCP00000079981; EBESCG00000082047.
GeneID	3797995.
GenomeReviews	Gene locus SDY_1475 in contig CP000034_GR.
KEGG	sdy:SDY_1475.
NMPDR	fig|216598.1.peg.800.
PATRIC	18692619. VBIShiDys99784_1759.
Phylogenomic databases
eggNOG	COG0169.
GeneTree	EBGT00050000010797.
HOGENOM	HBG553408.
OMA	AWEVESK.
PhylomeDB	Q32GE1.
ProtClustDB	PRK12749.
Enzyme and pathway databases
BioCyc	SDYS300267:SDY_1475-MONOMER.
Family and domain databases
HAMAP	MF_01578. Shikimate_DH_YdiB. [Tree]
InterPro	IPR016040. NAD(P)-bd_dom. IPR022872. Quinate/Shikimate_DH. IPR013708. Shikimate_DH-bd_N. IPR022893. Shikimate_quinate_DH. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K05887.
Pfam	PF01488. Shikimate_DH. 1 hit. PF08501. Shikimate_dh_N. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YDIB_SHIDS

Accession

Primary (citable) accession number: Q32GE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 20, 2007
Last sequence update:	December 6, 2005
Last modified:	January 25, 2012
This is version 53 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program