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Protein

Protein henna

Gene

Hn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Cofactori

Enzyme regulationi

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.

Pathwayi: L-phenylalanine degradation

This protein is involved in step 1 of the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine.
Proteins known to be involved in the 6 steps of the subpathway in this organism are:
  1. Protein henna (Hn)
  2. no protein annotated in this organism
  3. no protein annotated in this organism
  4. Homogentisate 1,2-dioxygenase (hgo)
  5. Probable maleylacetoacetate isomerase 1 (GstZ1), Probable maleylacetoacetate isomerase 2 (GstZ2)
  6. no protein annotated in this organism
This subpathway is part of the pathway L-phenylalanine degradation, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes acetoacetate and fumarate from L-phenylalanine, the pathway L-phenylalanine degradation and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi284 – 2841IronBy similarity
Metal bindingi289 – 2891IronBy similarity
Metal bindingi329 – 3291IronBy similarity

GO - Molecular functioni

GO - Biological processi

  • eye pigment biosynthetic process Source: FlyBase
  • long-term memory Source: FlyBase
  • L-phenylalanine catabolic process Source: FlyBase
  • phagocytosis Source: FlyBase
  • serotonin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Phenylalanine catabolism, Serotonin biosynthesis

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiR-DME-71182. Phenylalanine and tyrosine catabolism.
UniPathwayiUPA00139; UER00337.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Hn
Synonyms:pah, Tph
ORF Names:CG7399
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0001208. Hn.

Subcellular locationi

GO - Cellular componenti

  • lipid particle Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 452452Protein hennaPRO_0000205552Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721Phosphoserine; by CaMK2By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP17276.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiP17276.
ExpressionAtlasiP17276. differential.
GenevisibleiP17276. DM.

Interactioni

Protein-protein interaction databases

BioGridi64301. 41 interactions.
DIPiDIP-20514N.
IntActiP17276. 14 interactions.
MINTiMINT-321332.
STRINGi7227.FBpp0076523.

Structurei

3D structure databases

ProteinModelPortaliP17276.
SMRiP17276. Positions 34-451.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 10772ACTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ACT domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3820. Eukaryota.
COG3186. LUCA.
GeneTreeiENSGT00390000010268.
InParanoidiP17276.
KOiK00500.
OMAiEFFVECD.
OrthoDBiEOG7KM5T1.
PhylomeDBiP17276.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR002912. 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]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFiPIRSF000336. TH. 1 hit.
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17276-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYQRQVSFDK PTRVEDSAYI VEGVDIKEAR NTCLLFSPKD SSLSSGALAN
60 70 80 90 100
ILAIFKKHDI NLVHIESRSS LRVPGYEFFV EADGKSGALG KAIEDVKEQC
110 120 130 140 150
SYFNIISRDY KDNATAVPWF PRRIRDLDRF ANQILSYGSE LDADHPGFTD
160 170 180 190 200
PEYRKRRKYF ADIAYNYKHG EPLPHVDYTK EEIETWGIIF RNLTKLYKTH
210 220 230 240 250
ACREYNHVFP LLVDNCGFRE DNIPQLEDVS NFLRDCTGFT LRPVAGLLSS
260 270 280 290 300
RDFLAGLAFR VFHSTQYIRH PSKPMYTPEP DVCHELMGHV PLFADPAFAQ
310 320 330 340 350
FSQEIGLASL GAPDDYIEKL STIFWFTVEY GVCRQEGELK AYGAGLLSSY
360 370 380 390 400
GELEYCLTDK PQLKDFEPEV TGVTKYPITQ FQPLYYVADS FETAKEKTIK
410 420 430 440 450
FANSIPRPFG VRYNAYTQSV EVLDSKPQIS NLMDNINSEF QILQNAVAKL

RV
Length:452
Mass (Da):51,660
Last modified:December 1, 2000 - v3
Checksum:i990F554150056867
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281E → A in AAA69513 (PubMed:2121612).Curated
Sequence conflicti39 – 479KDSSLSSGA → RIRRCPAEL in AAA69513 (PubMed:2121612).Curated
Sequence conflicti55 – 562FK → LR in AAA69513 (PubMed:2121612).Curated
Sequence conflicti63 – 719VHIESRSSL → CILSRILAPWF in AAA69513 (PubMed:2121612).Curated
Sequence conflicti74 – 11441PGYEF…YKDNA → SSCFWRRMENRSLGKSHRGC EGAMLATLTSSCRELQGVMP in AAA69513 (PubMed:2121612).CuratedAdd
BLAST
Sequence conflicti154 – 1541R → A in AAA69513 (PubMed:2121612).Curated
Sequence conflicti164 – 1641A → G in AAA69513 (PubMed:2121612).Curated
Sequence conflicti171 – 1711E → Q in AAA69513 (PubMed:2121612).Curated
Sequence conflicti264 – 2641S → C in AAA69513 (PubMed:2121612).Curated
Sequence conflicti297 – 2971A → S in AAA69513 (PubMed:2121612).Curated
Sequence conflicti332 – 3321V → L in M81833 (PubMed:1371286).Curated
Sequence conflicti332 – 3321V → L in AAA69513 (PubMed:2121612).Curated
Sequence conflicti333 – 3353CRQ → LAK in AAA69513 (PubMed:2121612).Curated
Sequence conflicti370 – 3701V → S in AAA69513 (PubMed:2121612).Curated
Sequence conflicti449 – 4524KLRV → NCASE in M81833 (PubMed:1371286).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA42271.
JC4888.
JQ0766.
RefSeqiNP_001014573.1. NM_001014573.2.
NP_001261542.1. NM_001274613.1.
NP_523963.2. NM_079239.4.
UniGeneiDm.7375.

Genome annotation databases

EnsemblMetazoaiFBtr0076811; FBpp0076523; FBgn0001208.
FBtr0334645; FBpp0306707; FBgn0001208.
GeneIDi38871.
KEGGidme:Dmel_CG7399.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiA42271.
JC4888.
JQ0766.
RefSeqiNP_001014573.1. NM_001014573.2.
NP_001261542.1. NM_001274613.1.
NP_523963.2. NM_079239.4.
UniGeneiDm.7375.

3D structure databases

ProteinModelPortaliP17276.
SMRiP17276. Positions 34-451.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64301. 41 interactions.
DIPiDIP-20514N.
IntActiP17276. 14 interactions.
MINTiMINT-321332.
STRINGi7227.FBpp0076523.

Proteomic databases

PaxDbiP17276.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076811; FBpp0076523; FBgn0001208.
FBtr0334645; FBpp0306707; FBgn0001208.
GeneIDi38871.
KEGGidme:Dmel_CG7399.

Organism-specific databases

CTDi38871.
FlyBaseiFBgn0001208. Hn.

Phylogenomic databases

eggNOGiKOG3820. Eukaryota.
COG3186. LUCA.
GeneTreeiENSGT00390000010268.
InParanoidiP17276.
KOiK00500.
OMAiEFFVECD.
OrthoDBiEOG7KM5T1.
PhylomeDBiP17276.

Enzyme and pathway databases

UniPathwayiUPA00139; UER00337.
ReactomeiR-DME-71182. Phenylalanine and tyrosine catabolism.

Miscellaneous databases

ChiTaRSiHn. fly.
GenomeRNAii38871.
NextBioi810779.
PROiP17276.

Gene expression databases

BgeeiP17276.
ExpressionAtlasiP17276. differential.
GenevisibleiP17276. DM.

Family and domain databases

Gene3Di1.10.800.10. 1 hit.
InterProiIPR002912. 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]
PANTHERiPTHR11473. PTHR11473. 1 hit.
PfamiPF00351. Biopterin_H. 1 hit.
[Graphical view]
PIRSFiPIRSF000336. TH. 1 hit.
PRINTSiPR00372. FYWHYDRXLASE.
SUPFAMiSSF56534. SSF56534. 1 hit.
TIGRFAMsiTIGR01268. Phe4hydrox_tetr. 1 hit.
PROSITEiPS51671. ACT. 1 hit.
PS00367. BH4_AAA_HYDROXYL_1. 1 hit.
PS51410. BH4_AAA_HYDROXYL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  6. 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).

Entry informationi

Entry nameiPH4H_DROME
AccessioniPrimary (citable) accession number: P17276
Secondary accession number(s): O46110, Q27599, Q27600
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: December 1, 2000
Last modified: May 11, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

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.

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.