NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-11.
STRAIN=ATCC 31821 / ZM4 / CP4;
PubMed=7916685 [NCBI, ExPASy, EBI, Israel, Japan]
Zhao G., Xia T., Ingram L.O., Jensen R.A.;
"An allosterically insensitive class of cyclohexadienyl dehydrogenase from Zymomonas mobilis.";
Eur. J. Biochem. 212:157-165(1993).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 31821 / ZM4 / CP4;
DOI=10.1038/nbt1045; PubMed=15592456 [NCBI, ExPASy, EBI, Israel, Japan]
Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
"The genome sequence of the ethanologenic bacterium Zymomonas mobilis ZM4.";
Nat. Biotechnol. 23:63-68(2005).

Comments

FUNCTION: Is competent to function as either prephenate dehydrogenase or as arogenate dehydrogenase.
CATALYTIC ACTIVITY: L-arogenate + NAD⁺ = L-tyrosine + NADH + CO₂.
CATALYTIC ACTIVITY: Prephenate + NAD⁺ = 4-hydroxyphenylpyruvate + CO₂ + NADH.
ENZYME REGULATION: Insensitive to feedback inhibition by L-tyrosine.
PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from L-arogenate: step 1/1 .
PATHWAY: Amino-acid biosynthesis; L-tyrosine biosynthesis; L-tyrosine from prephenate: step 1/2 .
SUBUNIT: Homodimer.
SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain.

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

M75891; AAA27684.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X67208; CAA47647.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE008692; AAV89044.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S29384; S29384.

RefSeq

YP_162155.1; -.

3D structure databases

ModBase

Q04983.

Enzyme and pathway databases

BioCyc

ZMOB264203:ZMO0420-MON; -.

Ontologies

GO:0047794;	Molecular function: cyclohexadienyl dehydrogenase activity (inferred from electronic annotation from EC).
GO:0008977;	Molecular function: prephenate dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016040; NAD(P)-bd.
IPR003099; Prephen_DHase.
Graphical view of domain structure.

Gene3D

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

PANTHER

PTHR21363; Prephen_DH; 1.

Pfam

PF02153; PDH; 1.
Pfam graphical view of domain structure.

PROSITE

PS51176; PDH_ADH; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q04983.

Genome annotation databases

GeneID

3188887; -.

GenomeReviews

AE008692_GR; ZMO0420.

KEGG

zmo:ZMO0420; -.

NMPDR

fig|264203.3.peg.916; -.

Phylogenomic databases

HOGENOM

Q04983; -.

Genome annotation databases

CMR

Q04983; ZMO0420.

Other

ProtoNet

Q04983.

UniRef

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

Keywords

Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Complete proteome; Direct protein sequencing; NAD; Oxidoreductase; Tyrosine biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 293`	`293`	`Protein tyrC.`	`PRO_0000119209`
`DOMAIN`	`5 293`	`289`	`Prephenate/arogenate dehydrogenase.`
`NP_BIND`	`6 30`	`25`	`NAD (Potential).`
`CONFLICT`	`42 42`		`R -> C (in Ref. 1; AAA27684/CAA47647).`
`CONFLICT`	`268 268`		`G -> E (in Ref. 1; AAA27684/CAA47647).`
`CONFLICT`	`292 292`		`R -> H (in Ref. 1; AAA27684/CAA47647).`

Sequence information

Length: 293 AA [This is the length of the unprocessed precursor]

Molecular weight: 32051 Da [This is the MW of the unprocessed precursor]

CRC64: 027683380D81146C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVFKHIAII GLGLIGSSAA RATKAYCPDV TVSLYDKSEF VRDRARALNL GDNVTDDIQD 

        70         80         90        100        110        120 
AVREADLVLL CVPVRAMGIV AAAMAPALKK DVIICDTGSV KVSVIKTLQD NLPNHIIVPS 

       130        140        150        160        170        180 
HPLAGTENNG PDAGFAELFQ DHPVILTPDA HTPAQAIAYI ADYWEEIGGR INLMSAEHHD 

       190        200        210        220        230        240 
HVLALTSHLP HVIAYQLIGM VSGYEKKSRT PIMRYSAGSF RDATRVAASE PRLWQDIMLE 

       250        260        270        280        290 
NAPALLPVLD HFIADLKKLR TAIASQDGDY LLEHFKESQK ARLALKTDHD IRP

Q04983 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