[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Retina; PubMed=8189245 [NCBI, ExPASy, EBI, Israel, Japan] Green C.B., Besharse J.C.; "Tryptophan hydroxylase expression is regulated by a circadian clock in Xenopus laevis retina."; J. Neurochem. 62:2420-2428(1994).

Comments

CATALYTIC ACTIVITY: L-tryptophan + tetrahydrobiopterin + O₂ = 5-hydroxy-L-tryptophan + 4a-hydroxytetrahydrobiopterin.
COFACTOR: Fe(2+) ion.
PATHWAY: Aromatic compound metabolism; serotonin biosynthesis; serotonin from L-tryptophan: step 1/2 .
SUBUNIT: Multimer of identical subunits (By similarity).
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

L20679; AAA21306.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

I51567; I51567.

NP_001080923.1; -.

3D structure databases

HSSP

P17752; 1MLW. [HSSP ENTRY / PDB]

SMR

Q92142; 141-430.

ModBase

Q92142.

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

Q92142.

Genome annotation databases

GeneID

387560; -.

KEGG

xla:387560; -.

Phylogenomic databases

HOVERGEN

Q92142; -.

Other

ProtoNet

Q92142.

UniRef

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 481`	`481`	`Tryptophan 5-hydroxylase.`	`PRO_0000205573`
`DOMAIN`	`55 129`	`75`	`ACT.`
`METAL`	`309 309`		`Iron (By similarity).`
`METAL`	`314 314`		`Iron (By similarity).`
`METAL`	`354 354`		`Iron (By similarity).`

Sequence information

Length: 481 AA [This is the length of the unprocessed precursor]

Molecular weight: 55406 Da [This is the MW of the unprocessed precursor]

CRC64: 6852C33EFF8DEBA0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYSNRKECPR RVKSFDSVNS GLDENQINNE FNKSTYIKIE DNKEYSENVC ERGKASVIFS 

        70         80         90        100        110        120 
LKNEIGGLVK ALKLFQEKHV NLIHIESRKS KRRNSEFEIF VDCDSNREQL NEIFQLLKPH 

       130        140        150        160        170        180 
VNVISMSPPE NFTVQEDDME SVPWFPKKIS DLDKCANRVL MYGSDLDADH PGFKDNVYRK 

       190        200        210        220        230        240 
RRKYFADVAM SYKYGDPIPH IEFTEEEIQT WGTVFRELNK LYPTHACREY LKNLPLLSKH 

       250        260        270        280        290        300 
CGYREDNIPQ LEDVSRFLRE RTGFTIRPVA GYLSPRDFLA GLAFRVFHCT QYVRHDSDPL 

       310        320        330        340        350        360 
NTPEPDTCHE LLGHVPLLAE PSFAQFSQEI GLASLGASDE AVQKLATCYF FTVEFGLCKQ 

       370        380        390        400        410        420 
EGKLKVYGAG LLSSISELKH SLSGNAKVKP FDPMVTCNQE CIITSFQELY FVSESFEEAK 

       430        440        450        460        470        480 
EKMREFAKTI QRPFGLKYNP FTQSVDILKD TKSIAMVVRE LRHELDIVND ALNKMNKQLG 


V

Q92142 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