Reviewed, UniProtKB/Swiss-Prot Q44104 (PHEA_AMYME)

Names and origin

Protein names

Recommended name:
    Prephenate dehydratase
      Short name=PDT
    EC=4.2.1.51

Gene names

Name:	pheA
Synonyms:	pdt

Organism

Amycolatopsis methanolica

Taxonomic identifier

1814 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Pseudonocardineae › Pseudonocardiaceae › Amycolatopsis

Protein attributes

Sequence length	304 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

General annotation (Comments)

Catalytic activity	Prephenate = phenylpyruvate + H2O + CO2.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1.
Sequence similarities	Contains 1 ACT domain. Contains 1 prephenate dehydratase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Molecular function	Lyase
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 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 – 304	304	Prephenate dehydratase		PRO_0000119175
Regions
	Domain	3 – 178	176	Prephenate dehydratase
	Domain	192 – 269	78	ACT
Sites
	Site	171	1	Essential for activity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q44104-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: E19052658CC9E52F	FASTA	304	32,321
	10 20 30 40 50 60 MSRIAYFGPV GTFTEQAART FMAAGDELVA AETIPKALDA VRRGEADAAC VPVENSVEGA 70 80 90 100 110 120 VPATLDSLAV GEPLIGVAEA LLPVHFSVLT RDDVGEIRTV ASHPHALAQV RKWLEDNLPG 130 140 150 160 170 180 ARVVAAGSTA AAAVAVQAGE FDAAVTAPVA VEHYPLKVLA TEVADVRDAR TRFLLMRRPP 190 200 210 220 230 240 VVLPEPTGAD RTSIVAAAAN RTGTLAELLT ELATRGINLT RLDARPHKQN FGEYRFFIDF 250 260 270 280 290 300 EGHVAEPRIA DALAALRRRC RDVRFLGSFA RADGVAATIE PAARNEDFTD AADWVAAVQR GEQA

References

[1]

"Molecular cloning with a pMEA300-derived shuttle vector and characterization of the Amycolatopsis methanolica prephenate dehydratase gene." Vrijbloed J.W., van Hylckama Vlieg J., van der Put N.M., Hessels G.I., Dijkhuizen L. J. Bacteriol. 177:6666-6669(1995) [PubMed: 7592448] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	L47666 Genomic DNA. Translation: AAA88840.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	4.2.1.51. 3718.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Pfam	PF01842. ACT. 1 hit. PF00800. PDT. 1 hit. [Graphical view]
PROSITE	PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. False negative. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_AMYME

Accession

Primary (citable) accession number: Q44104

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 46 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)