Reviewed, UniProtKB/Swiss-Prot P93836 (HPPD_ARATH)

Names and origin

Protein names

Recommended name:
    4-hydroxyphenylpyruvate dioxygenase
    EC=1.13.11.27
Alternative name(s):
    4-hydroxyphenylpyruvic acid oxidase
      Short name=HPPDase
      Short name=4HPPD
      Short name=HPD

Gene names

Name:	HPD
Ordered Locus Names:	At1g06570
ORF Names:	F12K11.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	445 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 + O(2) = homogentisate + CO(2).
Cofactor	Binds 1 iron ion per subunit.
Pathway	Amino-acid degradation; L-phenylalanine degradation; acetoacetic acid and fumarate from L-phenylalanine: step 3/6. Cofactor biosynthesis; prenylquinone biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the 4HPPD family.

Ontologies

Keywords
Biological process	Phenylalanine catabolism Tyrosine catabolism
Cellular component	Cytoplasm
Ligand	Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase
Technical term	3D-structure Complete proteome
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4-hydroxyphenylpyruvate dioxygenase activity Inferred from electronic annotation. Source: InterPro identical protein binding Ref.7 Inferred from physical interaction. Source: IntAct iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1251387,EBI-1251387

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 445

445

4-hydroxyphenylpyruvate dioxygenase

PRO_0000088397

Sites

Metal binding

226

1

Iron By similarity

Metal binding

308

1

Iron By similarity

Metal binding

394

1

Iron By similarity

Amino acid modifications

Disulfide bond

401 ↔ 416

Secondary structure

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445

Helix Strand Turn

Details...

Beta strand

44 – 53

10

Helix

57 – 68

12

Beta strand

71 – 77

7

Helix

78 – 80

3

Beta strand

83 – 92

10

Beta strand

95 – 102

8

Helix

105 – 107

3

Turn

108 – 110

3

Helix

113 – 115

3

Helix

125 – 135

11

Beta strand

137 – 147

11

Helix

149 – 158

10

Beta strand

163 – 170

8

Turn

171 – 173

3

Beta strand

174 – 182

9

Beta strand

185 – 192

8

Turn

211 – 213

3

Beta strand

219 – 230

12

Helix

234 – 245

12

Beta strand

248 – 253

6

Beta strand

265 – 271

7

Beta strand

277 – 284

8

Helix

293 – 301

9

Beta strand

305 – 314

10

Helix

316 – 326

11

Helix

327 – 329

3

Helix

340 – 350

11

Turn

351 – 353

3

Helix

356 – 365

10

Beta strand

368 – 371

4

Beta strand

373 – 382

10

Beta strand

385 – 389

5

Beta strand

392 – 400

9

Turn

414 – 417

4

Helix

423 – 430

8

Helix

432 – 436

5

Sequences

	Sequence		Length	Mass (Da)
	P93836-1 [UniParc]. Last modified January 1, 1998. Version 2. Checksum: FD0442F93556B3F5	FASTA	445	48,816
	10 20 30 40 50 60 MGHQNAAVSE NQNHDDGAAS SPGFKLVGFS KFVRKNPKSD KFKVKRFHHI EFWCGDATNV 70 80 90 100 110 120 ARRFSWGLGM RFSAKSDLST GNMVHASYLL TSGDLRFLFT APYSPSLSAG EIKPTTTASI 130 140 150 160 170 180 PSFDHGSCRS FFSSHGLGVR AVAIEVEDAE SAFSISVANG AIPSSPPIVL NEAVTIAEVK 190 200 210 220 230 240 LYGDVVLRYV SYKAEDTEKS EFLPGFERVE DASSFPLDYG IRRLDHAVGN VPELGPALTY 250 260 270 280 290 300 VAGFTGFHQF AEFTADDVGT AESGLNSAVL ASNDEMVLLP INEPVHGTKR KSQIQTYLEH 310 320 330 340 350 360 NEGAGLQHLA LMSEDIFRTL REMRKRSSIG GFDFMPSPPP TYYQNLKKRV GDVLSDDQIK 370 380 390 400 410 420 ECEELGILVD RDDQGTLLQI FTKPLGDRPT IFIEIIQRVG CMMKDEEGKA YQSGGCGGFG 430 440 KGNFSELFKS IEEYEKTLEA KQLVG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of an Arabidopsis thaliana cDNA for p-hydroxyphenylpyruvate dioxygenase." Bartley G.E., Maxwell C.A., Wittenbach V.A., Scolnik P.A. (er) Plant Gene Register PGR97-065 Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Wassilewskija.
[2]	Norris S.R., Dellapenna D. Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Columbia.
[3]	"Characterization and subcellular compartmentation of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis in transgenic tobacco." Garcia I., Rodgers M., Pepin R., Hsieh T.-F., Matringe M. Plant Physiol. 119:1507-1516(1999) [PubMed: 10198110] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Structural basis for herbicidal inhibitor selectivity revealed by comparison of crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases." Yang C., Pflugrath J.W., Camper D.L., Foster M.L., Pernich D.J., Walsh T.A. Biochemistry 43:10414-10423(2004) [PubMed: 15301540] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-445, METAL-BINDING SITES, SUBUNIT.
[7]	"The crystal structures of Zea mays and Arabidopsis 4-hydroxyphenylpyruvate dioxygenase." Fritze I.M., Linden L., Freigang J., Auerbach G., Huber R., Steinbacher S. Plant Physiol. 134:1388-1400(2004) [PubMed: 15084729] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), SUBUNIT.

Cross-references

Sequence databases

EMBLGenBankDDBJ

U89267 mRNA. Translation: AAB70025.1.
AF000228 mRNA. Translation: AAB58404.1.
AF047834 mRNA. Translation: AAC15697.1.
AC007592 Genomic DNA. Translation: AAF24813.1. Different initiation.
AF428446 mRNA. Translation: AAL16215.1.
AY072329 mRNA. Translation: AAL61936.1.
AY128745 mRNA. Translation: AAM91145.1.

PIR

B86201.
T51585.

UniGene

At.48158

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SP9	X-ray	3.00	A/B	1-445	[»]
1SQD	X-ray	1.80	A	23-445	[»]
1TFZ	X-ray	1.80	A	23-445	[»]
1TG5	X-ray	1.90	A	23-445	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P93836.

Genome annotation databases

NMPDR

fig|3702.1.peg.833.

Organism-specific databases

TAIR

At1g06570.

Gene expression databases

GermOnline

AT1G06570. Arabidopsis thaliana.

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_ARATH

Accession

Primary (citable) accession number: P93836
Secondary accession number(s): O04330, Q9SHK1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	November 25, 2008
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)