Q43135 (C79A1_SORBI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine N-monooxygenase
EC=1.14.13.41

Alternative name(s):
Cytochrome P450 79A1
Cytochrome P450Tyr

Gene names

Name:	CYP79A1
Synonyms:	CYP79

Organism

Sorghum bicolor (Sorghum) (Sorghum vulgare)

Taxonomic identifier

4558 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Sorghum

Protein attributes

Sequence length	558 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	N-hydroxylase that converts L-tyrosine to p-hydroxyphenylacetaldehyde oxime.
Catalytic activity	L-tyrosine + O2 + NADPH = N-hydroxy-L-tyrosine + NADP+ + H2O. N-hydroxy-L-tyrosine + O2 + NADPH = N,N-dihydroxy-L-tyrosine + NADP+ + H2O. N,N-dihydroxy-L-tyrosine = (Z)-[4-hydroxyphenylacetaldehyde oxime] + CO2 + H2O.
Cofactor	Heme group By similarity.
Pathway	Secondary metabolite biosynthesis; dhurrin biosynthesis; dhurrin from L-tyrosine: step 1/3.
Subcellular location	Endoplasmic reticulum membrane; Single-pass membrane protein Potential.
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding NADP
Molecular function	Monooxygenase Oxidoreductase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro tyrosine N-monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 558	557	Tyrosine N-monooxygenase		PRO_0000052152
Regions
	Transmembrane	13 – 33	21	Helical; Potential
Sites
	Metal binding	493	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43135 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 83F435793CF651BA	FASTA	558	61,887
	10 20 30 40 50 60 MATMEVEAAA ATVLAAPLLS SSAILKLLLF VVTLSYLARA LRRPRKSTTK CSSTTCASPP 70 80 90 100 110 120 AGVGNPPLPP GPVPWPVVGN LPEMLLNKPA FRWIHQMMRE MGTDIACVKL GGVHVVSITC 130 140 150 160 170 180 PEIAREVLRK QDANFISRPL TFASETFSGG YRNAVLSPYG DQWKKMRRVL TSEIICPSRH 190 200 210 220 230 240 AWLHDKRTDE ADNLTRYVYN LATKAATGDV AVDVRHVARH YCGNVIRRLM FNRRYFGEPQ 250 260 270 280 290 300 ADGGPGPMEV LHMDAVFTSL GLLYAFCVSD YLPWLRGLDL DGHEKIVKEA NVAVNRLHDT 310 320 330 340 350 360 VIDDRWRQWK SGERQEMEDF LDVLITLKDA QGNPLLTIEE VKAQSQDITF AAVDNPSNAV 370 380 390 400 410 420 EWALAEMVNN PEVMAKAMEE LDRVVGRERL VQESDIPKLN YVKACIREAF RLHPVAPFNV 430 440 450 460 470 480 PHVALADTTI AGYRVPKGSH VILSRTGLGR NPRVWDEPLR FYPDRHLATA ASDVALTEND 490 500 510 520 530 540 LRFISFSTGR RGCIAASLGT AMSVMLFGRL LQGFTWSKPA GVEAVDLSES KSDTFMATPL 550 VLHAEPRLPA HLYPSISI

References

[1]

"The primary sequence of cytochrome P450tyr, the multifunctional N-hydroxylase catalyzing the conversion of L-tyrosine to p-hydroxyphenylacetaldehyde oxime in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench." Koch B.M., Sibbesen O., Halkier B.A., Svendsen I., Moeller B.L. Arch. Biochem. Biophys. 323:177-186(1995) [PubMed: 7487064] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 197-204; 277-282; 330-361; 363-376; 390-399; 454-460; 473-480; 484-490 AND 532-558. Strain: cv. SS1000. Tissue: Etiolated seedling.

[2]

"Isolation of the heme-thiolate enzyme cytochrome P-450TYR, which catalyzes the committed step in the biosynthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor (L.) Moench." Sibbesen O., Koch B., Halkier B.A., Moller B.L. Proc. Natl. Acad. Sci. U.S.A. 91:9740-9744(1994) [PubMed: 7937883] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-17.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U32624 mRNA. Translation: AAA85440.1.
PIR	S68203.
RefSeq	XP_002466099.1. XM_002466054.1.
UniGene	Sbi.13772.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	Sb01g001200.1; Sb01g001200.1; Sb01g001200.
GeneID	8061413.
KEGG	sbi:SORBI_01g001200.
Organism-specific databases
Gramene	Q43135.
Phylogenomic databases
GeneTree	EPGT00070000027894.
OMA	WKLAGSE.
PhylomeDB	Q43135.
ProtClustDB	CLSN2723637.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-521.
Family and domain databases
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002401. Cyt_P450_E_grp-I. [Graphical view]
Gene3D	G3DSA:1.10.630.10. Cyt_P450. 1 hit.
KO	K13027.
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00463. EP450I. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C79A1_SORBI

Accession

Primary (citable) accession number: Q43135

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 23, 2007
Last modified:	December 14, 2011
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program