Reviewed, UniProtKB/Swiss-Prot Q8H1H9 (AMO_ARATH)

Names and origin

Protein names

Recommended name:
    Primary amine oxidase
    EC=1.4.3.21
Alternative name(s):
    Amine oxidase [copper-containing]

Gene names

Ordered Locus Names:	At1g62810
ORF Names:	F23N19.18

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	712 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.
Cofactor	Binds 1 copper ion per subunit By similarity. Contains 1 topaquinone per subunit By similarity.
Subunit structure	Homodimer.
Post-translational modification	Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue By similarity.
Sequence similarities	Belongs to the copper/topaquinone oxidase family.
Sequence caution	The sequence AAF19542.1 differs from that shown. Reason: Erroneous gene model prediction. The predicted gene has been split into 3 genes: At1g62810, At1g62820 and At1g62830.

Ontologies

Keywords
Domain	Signal
Ligand	Copper Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein TPQ
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	amine metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	amine oxidase activity Inferred from electronic annotation. Source: EC copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW quinone binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Chain	25 – 712	688	Primary amine oxidase		PRO_0000342892
Sites
	Active site	354	1	Proton acceptor By similarity
	Active site	442	1	Schiff-base intermediate with substrate; via topaquinone By similarity
	Metal binding	499	1	Copper By similarity
	Metal binding	501	1	Copper By similarity
	Metal binding	508	1	Manganese By similarity
	Metal binding	509	1	Manganese; via carbonyl oxygen By similarity
	Metal binding	510	1	Manganese By similarity
	Metal binding	651	1	Manganese By similarity
	Metal binding	652	1	Manganese; via carbonyl oxygen By similarity
	Metal binding	662	1	Copper By similarity
Amino acid modifications
	Modified residue	442	1	2',4',5'-topaquinone By similarity
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	173	1	N-linked (GlcNAc...) Potential
	Glycosylation	516	1	N-linked (GlcNAc...) Potential
	Glycosylation	617	1	N-linked (GlcNAc...) Potential
	Disulfide bond	188 ↔ 210		By similarity
	Disulfide bond	373 ↔ 399		By similarity
Experimental info
	Sequence conflict	201	1	E → K in AAO42785. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8H1H9-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 451908CE887D1F64	FASTA	712	80,138
	10 20 30 40 50 60 MAEPSFARLF LLFFSFLLIF ATYSWVFGPD SGFLFGTRVR KTLGSNRQVH VDHSLEKPHH 70 80 90 100 110 120 PLDPLTVREI NRVRTILSNH DPGFGSGSAT IHSMALDEPE KSRVVQWKKG NKLLSRRAAV 130 140 150 160 170 180 VAYWGGQTHE ITVDLDSGRV VSDVINRTSG YPILTLNDVF AASQVPLKSL EFNRSIEARG 190 200 210 220 230 240 VKFSDLACIT PFAGWFGSEE EGRRVIRVQC FTLQGTTNYF MRPLEGLYVT VDLDKLEVIK 250 260 270 280 290 300 IIDKGPIPIP KASGTEYRFG VQNKPVHMDR INPISMEQPD GPSFRVEDGH LVKWANWVFH 310 320 330 340 350 360 VKADQRAGMI ISQATVRDSE TGEPRSVMYK GFPSELFVPY MDPEEGWYYK GYMDAGELGL 370 380 390 400 410 420 GPTAMPLVPL NDCPRNSYYI DGVFASPDGK PIVQPNMICL FERYAGDISW RHSEILFANA 430 440 450 460 470 480 DIRESRPKVT LVARMATSVG NYDYIFDWEF QTDGLIRVTV AASGMLMVKG TPYDNVDDLG 490 500 510 520 530 540 DREDDAGPLI SENVIGVVHD HFITFHLDMD IDGPMNNSLV KVHLEKQRVP TGKSPRKSYL 550 560 570 580 590 600 KVKKYIAKTE KDAQIKLSLY DPYEFHIVNP NRKSRVGNPA GYRIVPGGNA ASLLDHDDPP 610 620 630 640 650 660 QIRGAFTNNQ IWVTPYNRSE QYAGGVLIYQ SQGDDTLQVW SDRDRSIENK DIVLWYTLGF 670 680 690 700 710 HHVPCQEDYP VMPTVAASFE LKPANFFESN PILGSAPFFE KDLPVCRPFA SS

References

[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC007190 Genomic DNA. Translation: AAF19542.1. Sequence problems. AY149440 mRNA. Translation: AAN12916.1. BT004539 mRNA. Translation: AAO42785.1.
IPI	IPI00529460.
RefSeq	NP_176469.1.
UniGene	At.36219
3D structure databases
HSSP	HSSP built from PDB template 1KSI based on UniProtKB Q43077.
SMR	Q8H1H9. Positions 59-706.
ModBase	Search...
Proteomic databases
PRIDE	Q8H1H9.
Genome annotation databases
GeneID	842580.
GenomeReviews	Gene locus AT1G62810 in contig CT485782_GR.
KEGG	ath:AT1G62810.
NMPDR	fig|3702.1.peg.5674.
Organism-specific databases
TAIR	At1g62810.
Phylogenomic databases
eggNOG	KOG1186.
HOGENOM	HBG325455.
InParanoid	Q8H1H9.
OMA	INPISME.
PhylomeDB	Q8H1H9.
Gene expression databases
Genevestigator	Q8H1H9.
Family and domain databases
InterPro	IPR000269. Cu_amine_oxidase. IPR015798. Cu_amine_oxidase_C. IPR016182. Cu_amine_oxidase_N-reg. IPR015800. Cu_amine_oxidase_N2. IPR015801. Cu_amine_oxidase_N2/3. IPR015802. Cu_amine_oxidase_N3. [Graphical view]
Gene3D	G3DSA:3.10.450.40. CuNH_oxidase. 2 hits. G3DSA:2.70.98.20. Lyase_8_central. 1 hit.
PANTHER	PTHR10638. CuNH_oxidase. 1 hit.
Pfam	PF01179. Cu_amine_oxid. 1 hit. PF02727. Cu_amine_oxidN2. 1 hit. PF02728. Cu_amine_oxidN3. 1 hit. [Graphical view]
PROSITE	PS01164. COPPER_AMINE_OXID_1. False negative. PS01165. COPPER_AMINE_OXID_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AMO_ARATH

Accession

Primary (citable) accession number: Q8H1H9
Secondary accession number(s): Q84W14, Q9SI68

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	March 1, 2003
Last modified:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)