[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1126/science.1078197; PubMed=12511643 [NCBI, ExPASy, EBI, Israel, Japan] Walther D.J., Peter J.-U., Bashammakh S., Hortnagl H., Voits M., Fink H., Bader M.; "Synthesis of serotonin by a second tryptophan hydroxylase isoform."; Science 299:76-76(2003).

Comments

CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O₂ = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion (By similarity).
PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2 .
SIMILARITY: Belongs to the biopterin-dependent aromatic amino acid hydroxylase family.
SIMILARITY: Contains 1 ACT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY098915; AAM28947.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_776211.1; -.

UniGene

Rn.28510

3D structure databases

HSSP

P04177; 1TOH. [HSSP ENTRY / PDB]

SMR

Q8CGU9; 146-434.

ModBase

Q8CGU9.

Organism-specific databases

RGD

631332; Tph2.

Gene expression databases

GermOnline

ENSRNOG00000003880; Rattus norvegicus.

Family and domain databases

InterPro

IPR001273; Aaa_hydroxylase.
IPR002912; ACT_bd.
IPR005963; Tyr_5_mOase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.800.10; Aaa_hydroxylase; 1.

PANTHER

PTHR11473; Aaa_hydroxylase; 1.

Pfam

PF01842; ACT; 1.
PF00351; Biopterin_H; 1.
Pfam graphical view of domain structure.

PRINTS

PR00372; FYWHYDRXLASE.

ProDom

PD002559; Aaa_hydroxylase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01270; Trp_5_monoox; 1.

PROSITE

PS00367; BIOPTERIN_HYDROXYL; 1.

BLOCKS

Q8CGU9.

Genome annotation databases

Ensembl

ENSRNOG00000003880; Rattus norvegicus. [Contig view]

GeneID

317675; -.

KEGG

rno:317675; -.

Phylogenomic databases

HOVERGEN

Q8CGU9; -.

Other

Q8CGU9; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Iron; Metal-binding; Monooxygenase; Oxidoreductase; Phosphoprotein; Serotonin biosynthesis.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 485`	`485`	`Tryptophan 5-hydroxylase 2.`	`PRO_0000205576`
`DOMAIN`	`59 131`	`73`	`ACT.`
`METAL`	`313 313`		`Iron (By similarity).`
`METAL`	`318 318`		`Iron (By similarity).`
`METAL`	`358 358`		`Iron (By similarity).`
`MOD_RES`	`377 377`		`Phosphoserine (By similarity).`
`MOD_RES`	`387 387`		`Phosphoserine (By similarity).`

Sequence information

Length: 485 AA [This is the length of the unprocessed precursor]

Molecular weight: 55621 Da [This is the MW of the unprocessed precursor]

CRC64: C859B87C04BE743D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQPAMMMFSS KYWARRGLSL DSAVPEEHQI LGGLTQNKAT ASKSEDKRSG KDTSESSKTA 

        70         80         90        100        110        120 
VVFSLKNEVG GLVRALRLFQ EKHVNMLHIE SRRSRRRSSE VEIFVDCECG KTEFNELIQL 

       130        140        150        160        170        180 
LKFQTTIVTL NPPDNIWTEE EELEDVPWFP RKISELDRCS HRVLMYGTEL DADHPGFKDN 

       190        200        210        220        230        240 
VYRQRRKYFV DVAMGYKYGQ PIPRVEYTEE ETKTWGVVFR ELSKLYPTHA CREYLKNFPL 

       250        260        270        280        290        300 
LTKYCGYRED NVPQLEDVSM FLKERSGFTV RPVAGYLSPR DFLAGLAYRV FHCTQYVRHG 

       310        320        330        340        350        360 
SDPLYTPEPD TCHELLGHVP LLADPKFAQF SQEIGLASLG ASDEDVQKLA TCYFFTIEFG 

       370        380        390        400        410        420 
LCKQEGQLRA YGAGLLSSIG ELKHALSDKA CVKAFDPKTT CLQECLITTF QDAYFVSESF 

       430        440        450        460        470        480 
EEAKEKMRDF AKSITRPFSV YFNPYTQSIE ILKDTRSIEN VVQDLRSDLN TVCDALNKMN 


QYLGI

Q8CGU9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools