Prephenate dehydrogenase - Aquifex aeolicus (strain VF5)

Preferred order of sections

Names and origin

Protein names

Submitted name:
Prephenate dehydrogenase EMBL AAC07589.1

Gene names

Name:	tyrA EMBL AAC07589.1
Ordered Locus Names:	aq_1755

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	311 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP Nucleotide-binding PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP
Technical term	3D-structure PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	tyrosine biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: InterPro prephenate dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Regions

Nucleotide binding

40 – 41

2

NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Nucleotide binding

151 – 156

6

NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Sites

Binding site

62

1

NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Binding site

67

1

NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Binding site

99

1

NAD; via carbonyl oxygen PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Binding site

126

1

NAD PDB 3GGO PDB 2G5C PDB 3GGG PDB 3GGP

Sequences

Sequence

Length

Mass (Da)

Tools

O67636 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: CCA6DA3EFC7A18CD
Show »

FASTA

311

34,850

        10         20         30         40         50         60 
MAILSSMFNP SPPQGFCKKN IIKILKSLSM QNVLIVGVGF MGGSFAKSLR RSGFKGKIYG 

        70         80         90        100        110        120 
YDINPESISK AVDLGIIDEG TTSIAKVEDF SPDFVMLSSP VRTFREIAKK LSYILSEDAT 

       130        140        150        160        170        180 
VTDQGSVKGK LVYDLENILG KRFVGGHPIA GTEKSGVEYS LDNLYEGKKV ILTPTKKTDK 

       190        200        210        220        230        240 
KRLKLVKRVW EDVGGVVEYM SPELHDYVFG VVSHLPHAVA FALVDTLIHM STPEVDLFKY 

       250        260        270        280        290        300 
PGGGFKDFTR IAKSDPIMWR DIFLENKENV MKAIEGFEKS LNHLKELIVR EAEEELVEYL 

       310 
KEVKIKRMEI D

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.
[2]	"Crystal structure of prephenate dehydrogenase from Aquifex aeolicus. Insights into the catalytic mechanism." Sun W., Singh S., Zhang R., Turnbull J.L., Christendat D. J. Biol. Chem. 281:12919-12928(2006) [PubMed: 16513644] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 31-310 IN COMPLEX WITH NAD.
[3]	"The crystal structure of Aquifex aeolicus prephenate dehydrogenase reveals the mode of tyrosine inhibition." Sun W., Shahinas D., Bonvin J., Hou W., Kimber M.S., Turnbull J., Christendat D. J. Biol. Chem. 284:13223-13232(2009) [PubMed: 19279014] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 19-311 IN COMPLEX WITH NAD.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AE000657 Genomic DNA. Translation: AAC07589.1.

PIR

B70451.

RefSeq

NP_214202.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2G5C	X-ray	1.90	A/B/C/D	31-310	[»]
3GGG	X-ray	2.21	A/B/C/D	19-311	[»]
3GGO	X-ray	2.15	A/B/C/D	19-311	[»]
3GGP	X-ray	2.25	A/B/C/D	19-311	[»]

ProteinModelPortal

O67636.

SMR

O67636. Positions 31-310.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

1193351.

GenomeReviews

Gene locus aq_1755 in contig AE000657_GR.

KEGG

aae:aq_1755.

NMPDR

fig|224324.1.peg.1217.

PATRIC

20960500. VBIAquAeo85532_1354.

Phylogenomic databases

HOGENOM

HBG544990.

OMA

FENAFYI.

PhylomeDB

O67636.

ProtClustDB

CLSK2299820.

Family and domain databases

InterPro

IPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR003099. Prephen_DH.
[Graphical view]

Gene3D

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

KO

K04517.

Pfam

PF02153. PDH. 1 hit.
[Graphical view]

SUPFAM

SSF48179. 6DGDH_C_like. 1 hit.

PROSITE

PS51176. PDH_ADH. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O67636_AQUAE

Accession

Primary (citable) accession number: O67636

Entry history

Integrated into UniProtKB/TrEMBL:	August 1, 1998
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)