[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=PD713; Gafni Y., Manulis S., Kunik T., Lichter A.L., Barash I.B., Ophir Y.; "Characterization of the auxin synthesis genes of Erwinia herbicola pv. gypsophilae."; Isr. J. Plant Sci. 45:279-284(1997).

Comments

CATALYTIC ACTIVITY: L-tryptophan + O₂ = (indol-3-yl)acetamide + CO₂ + H₂O.
PATHWAY: Plant hormone metabolism; auxin biosynthesis .
SIMILARITY: Belongs to the tryptophan 2-monooxygenase family.

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

L33867; AAC17187.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q47861.

Ontologies

GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050361;	Molecular function: tryptophan 2-monooxygenase activity (inferred from electronic annotation from EC).
GO:0009851;	Biological process: auxin biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
IPR002937; Amino_oxidase.
Graphical view of domain structure.

Pfam

PF01593; Amino_oxidase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.

Other

ProtoNet

Q47861.

UniRef

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

Keywords

Auxin biosynthesis; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 562`	`562`		`Tryptophan 2-monooxygenase.`	`PRO_0000065589`

Sequence information

Length: 562 AA [This is the length of the unprocessed precursor]

Molecular weight: 62513 Da [This is the MW of the unprocessed precursor]

CRC64: 621E7AA389DDF886 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKPHSVFADS LWPSIDLLYD YAPFLQQSMV DGHIGFFPTG ITPPRVAIIG AGISGLIAAT 

        70         80         90        100        110        120 
ELLRAGVRDI TLFEARDRLG GRAWSQLFDP HYYPRLIAEM GAMRFPPSAT GLFHYLNRFS 

       130        140        150        160        170        180 
IQTSASFPDP GIVDTELHYR GVRHLWPAGE QPPALFTRVH NGWRALLYEG CLLDGVSLVG 

       190        200        210        220        230        240 
PLQITAMLKS ERFDEAAEAW QIWLNVFRDC SFYSAMVTIF TGTNPPGGIA WERRDDFELF 

       250        260        270        280        290        300 
GALGIGSGGF LPVYQAGFTE ILRMVINGYE DDQRLIIGGI STLAEQLARQ EIRGTTPGRH 

       310        320        330        340        350        360 
VRFSKVNRIS KDNGKISLAT DVKPVDAFDR VIVTSNNRAM QMVHGLSADE TFLNQDVCRA 

       370        380        390        400        410        420 
VRETHLTGSS KLFMLTRDKF WLKNKLPLTI QSDGLVRGVY VLDYESDNPE GRGVVLLSYT 

       430        440        450        460        470        480 
WEDDAHKLLA ITDKKQRGQH LVDELSAIHP EFARYLVPAG ADYERYVLHH DWLTDPCSAG 

       490        500        510        520        530        540 
AFKLNYPGED VYSQRLFFQF KTANHPEQDS GLLLAGCGCS FTGGWVEGAV QTAVNSACAV 

       550        560 
IRSTGGTLYG NPLDSVHSIY DY

Q47861 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