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P17276 (PH4H_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein henna

EC=1.14.16.1
EC=1.14.16.4
Alternative name(s):
Phe-4-monooxygenase
Phenylalanine-4-hydroxylase
Short name=PAH
Tryptophan 5-hydroxylase
Short name=TRH
Tryptophan 5-monooxygenase
Gene names
Name:Hn
Synonyms:pah, Tph
ORF Names:CG7399
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin.

L-tryptophan + tetrahydrobiopterin + O2 = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.

Cofactor

Fe2+ ion.

Enzyme regulation

N-terminal region of PAH is thought to contain allosteric binding sites for phenylalanine and to constitute an "inhibitory" domain that regulates the activity of a catalytic domain in the C-terminal portion of the molecule.

Pathway

Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6.

Tissue specificity

Phenylalanine hydrolase activity is found in yolk granules of embryos, and female abdomen and fat body tissues. Tryptophan hydroxylase is expressed in serotonergic neurons. Both enzymes are present in cuticular tissues.

Miscellaneous

In Drosophila, the 2 enzymes, PAH and TRH are found to be encoded by the same gene. Preference for the substrate is probably due to post-translational modifications such as phosphorylation, or by changes in the N-terminal regulatory domain.

Sequence similarities

Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.

Contains 1 ACT domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 452452Protein henna
PRO_0000205552

Regions

Domain36 – 10772ACT

Sites

Metal binding2841Iron By similarity
Metal binding2891Iron By similarity
Metal binding3291Iron By similarity

Amino acid modifications

Modified residue2721Phosphoserine; by CaMK2 By similarity

Experimental info

Sequence conflict281E → A in AAA69513. Ref.2
Sequence conflict39 – 479KDSSLSSGA → RIRRCPAEL in AAA69513. Ref.2
Sequence conflict55 – 562FK → LR in AAA69513. Ref.2
Sequence conflict63 – 719VHIESRSSL → CILSRILAPWF in AAA69513. Ref.2
Sequence conflict74 – 11441PGYEF…YKDNA → SSCFWRRMENRSLGKSHRGC EGAMLATLTSSCRELQGVMP in AAA69513. Ref.2
Sequence conflict1541R → A in AAA69513. Ref.2
Sequence conflict1641A → G in AAA69513. Ref.2
Sequence conflict1711E → Q in AAA69513. Ref.2
Sequence conflict2641S → C in AAA69513. Ref.2
Sequence conflict2971A → S in AAA69513. Ref.2
Sequence conflict3321V → L in M81833. Ref.1
Sequence conflict3321V → L in AAA69513. Ref.2
Sequence conflict333 – 3353CRQ → LAK in AAA69513. Ref.2
Sequence conflict3701V → S in AAA69513. Ref.2
Sequence conflict449 – 4524KLRV → NCASE in M81833. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P17276 [UniParc].

Last modified December 1, 2000. Version 3.
Checksum: 990F554150056867

FASTA45251,660
        10         20         30         40         50         60 
MYQRQVSFDK PTRVEDSAYI VEGVDIKEAR NTCLLFSPKD SSLSSGALAN ILAIFKKHDI 

        70         80         90        100        110        120 
NLVHIESRSS LRVPGYEFFV EADGKSGALG KAIEDVKEQC SYFNIISRDY KDNATAVPWF 

       130        140        150        160        170        180 
PRRIRDLDRF ANQILSYGSE LDADHPGFTD PEYRKRRKYF ADIAYNYKHG EPLPHVDYTK 

       190        200        210        220        230        240 
EEIETWGIIF RNLTKLYKTH ACREYNHVFP LLVDNCGFRE DNIPQLEDVS NFLRDCTGFT 

       250        260        270        280        290        300 
LRPVAGLLSS RDFLAGLAFR VFHSTQYIRH PSKPMYTPEP DVCHELMGHV PLFADPAFAQ 

       310        320        330        340        350        360 
FSQEIGLASL GAPDDYIEKL STIFWFTVEY GVCRQEGELK AYGAGLLSSY GELEYCLTDK 

       370        380        390        400        410        420 
PQLKDFEPEV TGVTKYPITQ FQPLYYVADS FETAKEKTIK FANSIPRPFG VRYNAYTQSV 

       430        440        450 
EVLDSKPQIS NLMDNINSEF QILQNAVAKL RV 

« Hide

References

« Hide 'large scale' references
[1]"A single locus encodes both phenylalanine hydroxylase and tryptophan hydroxylase activities in Drosophila."
Neckameyer W.S., White K.
J. Biol. Chem. 267:4199-4206(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
Strain: Canton-S and Oregon-R.
Tissue: Embryo and Head.
[2]"Sequence and expression of the Drosophila phenylalanine hydroxylase mRNA."
Morales G., Requena J.M., Jimenez-Ruiz A., Lopez M.C., Ugarte M., Alonso C.
Gene 93:213-219(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Structure of the phenylalanine hydroxylase gene in Drosophila melanogaster and evidence of alternative promoter usage."
Ruiz-Vazquez P., Moulard M., Silva F.J.
Biochem. Biophys. Res. Commun. 225:238-242(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Canton-S.
[4]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[5]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[6]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Berkeley.
Tissue: Head.
[7]"Aberrant splicing of the Drosophila melanogaster phenylalanine hydroxylase pre-mRNA caused by the insertion of a B104/roo transposable element in the Henna locus."
Ruiz-Vazquez P., Silva F.J.
Insect Biochem. Mol. Biol. 29:311-318(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 5-93 AND 161-412 (MUTANT HN-R3).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81833 Genomic RNA. No translation available.
M32802 mRNA. Translation: AAA69513.1.
X98116 Genomic DNA. Translation: CAA66797.1.
X98116 Genomic DNA. Translation: CAA66798.1.
AE014296 Genomic DNA. Translation: AAF50517.1.
AY069306 mRNA. Translation: AAL39451.1.
AJ001718 Genomic DNA. Translation: CAA04950.1.
AJ001719, AJ001720 Genomic DNA. Translation: CAB51601.1.
AJ001722 mRNA. Translation: CAB51599.1.
AJ001723 mRNA. Translation: CAB51597.1.
PIRA42271.
JC4888.
JQ0766.
RefSeqNP_001014573.1. NM_001014573.2.
NP_001261542.1. NM_001274613.1.
NP_523963.2. NM_079239.4.
UniGeneDm.7375.

3D structure databases

ProteinModelPortalP17276.
SMRP17276. Positions 34-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64301. 39 interactions.
DIPDIP-20514N.
IntActP17276. 14 interactions.
MINTMINT-321332.

Proteomic databases

PaxDbP17276.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0076811; FBpp0076523; FBgn0001208.
GeneID38871.
KEGGdme:Dmel_CG7399.

Organism-specific databases

CTD38871.
FlyBaseFBgn0001208. Hn.

Phylogenomic databases

eggNOGCOG3186.
GeneTreeENSGT00390000010268.
InParanoidP17276.
KOK00500.
OMARYNAYTQ.
OrthoDBEOG7KM5T1.
PhylomeDBP17276.

Enzyme and pathway databases

UniPathwayUPA00139; UER00337.

Gene expression databases

BgeeP17276.

Family and domain databases

Gene3D1.10.800.10. 1 hit.
InterProIPR002912. ACT_dom.
IPR001273. ArAA_hydroxylase.
IPR018301. ArAA_hydroxylase_Fe/CU_BS.
IPR019774. Aromatic-AA_hydroxylase_C.
IPR005961. Phe-4-hydroxylase_tetra.
IPR019773. Tyrosine_3-monooxygenase-like.
[Graphical view]
PANTHERPTHR11473. PTHR11473. 1 hit.
PfamPF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFPIRSF000336. TH. 1 hit.
PRINTSPR00372. FYWHYDRXLASE.
SUPFAMSSF56534. SSF56534. 1 hit.
TIGRFAMsTIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITEPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHn. drosophila.
GenomeRNAi38871.
NextBio810779.
PROP17276.

Entry information

Entry namePH4H_DROME
AccessionPrimary (citable) accession number: P17276
Secondary accession number(s): O46110, Q27599, Q27600
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase