Reviewed, UniProtKB/Swiss-Prot Q58054 (PHEA_METJA)

Names and origin

Protein names

Recommended name:
    Prephenate dehydratase
      Short name=PDT
    EC=4.2.1.51
Alternative name(s):
    MjPDT

Gene names

Name:	pheA
Ordered Locus Names:	MJ0637

Organism

Methanocaldococcus jannaschii (Methanococcus jannaschii) [Complete proteome] [HAMAP]

Taxonomic identifier

2190 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanocaldococcaceae › Methanocaldococcus

Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Prephenate = phenylpyruvate + H2O + CO2.
Enzyme regulation	Inhibited by L-phenylalanine but not by L-tyrosine or L-tryptophan.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Subunit structure	Homodimer. Ref.2
Sequence similarities	Contains 1 ACT domain. Contains 1 prephenate dehydratase domain.
Biophysicochemical properties	Kinetic parameters: KM=22 µM for prephenate pH dependence: Optimum pH is 5-10. Temperature dependence: Thermostable.
Mass spectrometry	Molecular mass is 31413 Da from positions 1 - 272. Determined by ESI. Ref.2

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	L-phenylalanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amino acid binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro monooxygenase activity Inferred from electronic annotation. Source: InterPro prephenate dehydratase 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 – 272	272	Prephenate dehydratase		PRO_0000119180
Regions
	Domain	4 – 179	176	Prephenate dehydratase
Sites
	Site	172	1	Essential for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q58054-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 0A5FDCE74AB7C3AD	FASTA	272	31,415
	10 20 30 40 50 60 MNKAVIYTLP KGTYSEKATK KFLDYIDGDY KIDYCNSIYD VFERVDNNGL GVVPIENSIE 70 80 90 100 110 120 GSVSLTQDLL LQFKDIKILG ELALDIHHNL IGYDKNKIKT VISHPQALAQ CRNYIKKHGW 130 140 150 160 170 180 DVKAVESTAK AVKIVAESKD ETLGAIGSKE SAEHYNLKIL DENIEDYKNN KTRFILIGKK 190 200 210 220 230 240 VKFKYHPKNY KVSIVFELKE DKPGALYHIL KEFAERNINL TRIESRPSKK RLGTYIFYID 250 260 270 FENNKEKLEE ILKSLERHTT FINLLGKYPV FD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii." Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R., Kirkness E.F., Weinstock K.G. , Merrick J.M., Glodek A., Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C. Science 273:1058-1073(1996) [PubMed: 8688087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
[2]	"A monofunctional and thermostable prephenate dehydratase from the archaeon Methanocaldococcus jannaschii." Kleeb A.C., Kast P., Hilvert D. Biochemistry 45:14101-14110(2006) [PubMed: 17115705] [Abstract] Cited for: BIOPHYSICAL CHARACTERIZATION, SUBUNIT, MASS SPECTROMETRY, INHIBITION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L77117 Genomic DNA. Translation: AAB98631.1.
PIR	E64379.
RefSeq	NP_247621.1.
3D structure databases
HSSP	HSSP built from PDB template 1PHZ based on UniProtKB P04176.
ModBase	Search...
Genome annotation databases
GeneID	1451503.
GenomeReviews	Gene locus MJ0637 in contig L77117_GR.
KEGG	mja:MJ0637.
NMPDR	fig|243232.1.peg.658.
TIGR	MJ0637.
Phylogenomic databases
HOGENOM	Q58054.
OMA	NCTRFVL.
Enzyme and pathway databases
BioCyc	MJAN243232:MJ_0637-MON.
BRENDA	4.2.1.51. 256362.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001273. ArAA_hydroxylase. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Gene3D	G3DSA:1.10.800.10. Aaa_hydroxylase. 1 hit.
Pfam	PF01842. ACT. 1 hit. PF00800. PDT. 1 hit. [Graphical view]
PROSITE	PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. 1 hit. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_METJA

Accession

Primary (citable) accession number: Q58054

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)