Reviewed, UniProtKB/Swiss-Prot P80064 (HPPD_PSEUJ)

Names and origin

Protein names

Recommended name:
    4-hydroxyphenylpyruvate dioxygenase
      Short name=HPPDase
      Short name=4HPPD
      Short name=HPD
    EC=1.13.11.27

Gene names

Name:

hpd

Organism

Pseudomonas sp. (strain P.J. 874)

Taxonomic identifier

72587 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria

Protein attributes

Sequence length	357 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	4-hydroxyphenylpyruvate + O2 = homogentisate + CO2.
Cofactor	Binds 1 iron ion per subunit.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 3/6.
Subunit structure	Homotetramer.
Sequence similarities	Belongs to the 4HPPD family.

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	L-phenylalanine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW tyrosine catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-hydroxyphenylpyruvate dioxygenase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 357

357

4-hydroxyphenylpyruvate dioxygenase

PRO_0000088408

Regions

Compositional bias

167 – 196

30

Tyr-rich

Sites

Metal binding

161

1

Iron

Metal binding

240

1

Iron

Metal binding

322

1

Iron

Secondary structure

1

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357

Helix Strand Turn

Details...

Beta strand

10 – 19

10

Helix

27 – 32

6

Beta strand

36 – 51

16

Beta strand

54 – 59

6

Beta strand

62 – 64

3

Helix

65 – 73

9

Beta strand

74 – 85

12

Helix

87 – 96

10

Beta strand

115 – 117

3

Helix

119 – 121

3

Beta strand

123 – 127

5

Beta strand

131 – 133

3

Helix

136 – 140

5

Beta strand

141 – 143

3

Beta strand

155 – 162

8

Helix

170 – 182

13

Beta strand

185 – 193

9

Beta strand

198 – 205

8

Beta strand

212 – 218

7

Helix

225 – 233

9

Beta strand

235 – 237

3

Beta strand

240 – 246

7

Helix

248 – 257

10

Helix

268 – 272

5

Helix

274 – 277

4

Helix

285 – 291

7

Beta strand

294 – 300

7

Beta strand

303 – 312

10

Beta strand

319 – 328

10

Helix

334 – 351

18

Sequences

	Sequence		Length	Mass (Da)
	P80064-1 [UniParc]. Last modified May 1, 1992. Version 1. Checksum: 26CF4A80B1484BD0	FASTA	357	40,061
	10 20 30 40 50 60 ADLYENPMGL MGFEFIELAS PTPNTLEPIF EIMGFTKVAT HRSKDVHLYR QGAINLILNN 70 80 90 100 110 120 EPHSVASYFA AEHGPSVCGM AFRVKDSQKA YKRALELGAQ PIHIETGPME LNLPAIKGIG 130 140 150 160 170 180 GAPLYLIDRF GEGSSIYDID FVFLEGVDRH PVGAGLKIID HLTHNVYRGR MAYWANFYEK 190 200 210 220 230 240 LFNFREIRYF DIKGEYTGLT SKAMTAPDGM IRIPLNEESS KGAGQIEEFL MQFNGEGIQH 250 260 270 280 290 300 VAFLSDDLIK TWDHLKSIGM RFMTAPPDTY YEMLEGRLPN HGEPVGELQA RGILLDGSSE 310 320 330 340 350 SGDKRLLLQI FSETLMGPVF FEFIQRKGDD GFGEGNFKAL FESIERDQVR RGVLSTD

References

[1]	"Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme." Rueetschi U., Odelhoeg B., Lindstedt S., Barros-Soederling J., Persson B., Joernvall H. Eur. J. Biochem. 205:459-466(1992) [PubMed: 1572351] [Abstract] Cited for: PROTEIN SEQUENCE.
[2]	"Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway." Serre L., Sailland A., Sy D., Boudec P., Rolland A., Pebay-Peyroula E., Cohen-Addad C. Structure 7:977-988(1999) [PubMed: 10467142] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

PIR

S21209.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CJX	X-ray	2.40	A/B/C/D	1-357	[»]

ModBase

Search...

Enzyme and pathway databases

BioCyc

MetaCyc:MON-12032.

Family and domain databases

InterPro

IPR005956. 4OHPhenylPyrv_dOase.
IPR004360. Glyas_bleo-R_dOase.
[Graphical view]

PANTHER

PTHR11959. HPP_dOase. 1 hit.

Pfam

PF00903. Glyoxalase. 1 hit.
[Graphical view]

PIRSF

PIRSF009283. HPP_dOase. 1 hit.

TIGRFAMs

TIGR01263. 4HPPD. 1 hit.

ProtoNet

Search...

Entry information

Entry name

HPPD_PSEUJ

Accession

Primary (citable) accession number: P80064

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 68 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)