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Protein

Peroxisomal primary amine oxidase

Gene

AMO

Organism
Pichia angusta (Yeast) (Hansenula polymorpha)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

RCH2NH2 + H2O + O2 = RCHO + NH3 + H2O2.2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Cu cation2 Publications, Zn2+1 PublicationNote: Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (PubMed:10933787).3 Publications
  • L-topaquinone2 PublicationsNote: Contains 1 topaquinone per subunit.2 Publications
  • Mn2+By similarityNote: Binds 1 Mn2+ ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei319 – 3191Proton acceptor1 Publication
Active sitei405 – 4051Schiff-base intermediate with substrate; via topaquinoneCombined sources2 Publications
Metal bindingi456 – 4561Copper; via tele nitrogenCombined sources2 Publications
Metal bindingi458 – 4581Copper; via tele nitrogenCombined sources2 Publications
Metal bindingi465 – 4651ManganeseBy similarity
Metal bindingi613 – 6131ManganeseBy similarity
Metal bindingi614 – 6141Manganese; via carbonyl oxygenBy similarity
Metal bindingi624 – 6241Copper; via pros nitrogenCombined sources2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Copper, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi1.4.3.21. 2587.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal primary amine oxidase (EC:1.4.3.212 Publications)
Alternative name(s):
Copper amine oxidase
Methylamine oxidase
Gene namesi
Name:AMO
OrganismiPichia angusta (Yeast) (Hansenula polymorpha)
Taxonomic identifieri870730 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaeOgataea

Subcellular locationi

  • Peroxisome 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi319 – 3191D → E: Strongly reduced activity. 1 Publication
Mutagenesisi319 – 3191D → N: Loss of activity. 1 Publication

Chemistry

ChEMBLiCHEMBL5020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 692692Peroxisomal primary amine oxidasePRO_0000064106Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi243 – 2431N-linked (GlcNAc...)1 Publication
Disulfide bondi338 ↔ 364Combined sources2 Publications
Modified residuei405 – 40512',4',5'-topaquinoneCombined sources1 Publication

Post-translational modificationi

Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Expressioni

Inductioni

By methylamine.

Interactioni

Subunit structurei

Homodimer.3 Publications

Chemistry

BindingDBiP12807.

Structurei

Secondary structure

1
692
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4314Combined sources
Turni44 – 463Combined sources
Beta strandi49 – 579Combined sources
Helixi61 – 699Combined sources
Beta strandi78 – 858Combined sources
Beta strandi89 – 979Combined sources
Turni98 – 1014Combined sources
Beta strandi102 – 1098Combined sources
Helixi118 – 1225Combined sources
Helixi124 – 1307Combined sources
Helixi132 – 1409Combined sources
Helixi145 – 1506Combined sources
Beta strandi151 – 1577Combined sources
Turni162 – 1665Combined sources
Beta strandi170 – 1778Combined sources
Helixi185 – 1873Combined sources
Beta strandi193 – 1975Combined sources
Turni198 – 2014Combined sources
Beta strandi202 – 2076Combined sources
Helixi225 – 2328Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi264 – 2718Combined sources
Turni272 – 2743Combined sources
Beta strandi275 – 28511Combined sources
Beta strandi288 – 30518Combined sources
Helixi312 – 3143Combined sources
Helixi319 – 3224Combined sources
Turni325 – 3284Combined sources
Turni333 – 3375Combined sources
Beta strandi343 – 3508Combined sources
Beta strandi356 – 37722Combined sources
Helixi379 – 3813Combined sources
Beta strandi385 – 40218Combined sources
Beta strandi405 – 4139Combined sources
Beta strandi419 – 4279Combined sources
Beta strandi431 – 4333Combined sources
Turni441 – 4433Combined sources
Beta strandi444 – 4485Combined sources
Beta strandi451 – 4544Combined sources
Beta strandi456 – 46611Combined sources
Beta strandi473 – 48210Combined sources
Helixi490 – 4923Combined sources
Beta strandi498 – 5047Combined sources
Helixi508 – 5114Combined sources
Helixi517 – 5193Combined sources
Beta strandi522 – 5265Combined sources
Turni533 – 5353Combined sources
Beta strandi540 – 5445Combined sources
Helixi558 – 5625Combined sources
Helixi564 – 5674Combined sources
Beta strandi568 – 5747Combined sources
Helixi597 – 6026Combined sources
Beta strandi610 – 6123Combined sources
Beta strandi614 – 62411Combined sources
Helixi628 – 6303Combined sources
Beta strandi631 – 6333Combined sources
Beta strandi637 – 65115Combined sources
Turni653 – 6564Combined sources
Beta strandi660 – 6634Combined sources
Helixi665 – 6717Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2VX-ray2.40A/B/C/D/E/F18-672[»]
1EKMX-ray2.50A/B/C17-672[»]
2OOVX-ray1.70A/B/C/D/E/F13-672[»]
2OQEX-ray1.60A/B/C/D/E/F13-672[»]
3N9HX-ray2.50A/B/C/D/E/F1-692[»]
3NBBX-ray2.05A/B/C/D/E/F1-692[»]
3NBJX-ray1.90A/B/C/D/E/F1-692[»]
3SX1X-ray1.73A/B/C1-692[»]
3SXXX-ray1.27A/B/C/D/E/F1-692[»]
3T0UX-ray1.90A/B/C1-692[»]
4EV2X-ray2.18A/B/C/D/E/F1-692[»]
4EV5X-ray2.25A/B/C/D/E/F1-692[»]
4KFDX-ray1.69A/B/C/D/E/F1-692[»]
4KFEX-ray2.10A/B/C/D/E/F1-692[»]
4KFFX-ray2.15A/B/C1-692[»]
ProteinModelPortaliP12807.
SMRiP12807. Positions 17-672.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12807.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 32812Substrate bindingCombined sourcesAdd
BLAST
Regioni402 – 4076Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the copper/topaquinone oxidase family.Curated

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P12807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERLRQIASQ ATAASAAPAR PAHPLDPLST AEIKAATNTV KSYFAGKKIS
60 70 80 90 100
FNTVTLREPA RKAYIQWKEQ GGPLPPRLAY YVILEAGKPG VKEGLVDLAS
110 120 130 140 150
LSVIETRALE TVQPILTVED LCSTEEVIRN DPAVIEQCVL SGIPANEMHK
160 170 180 190 200
VYCDPWTIGY DERWGTGKRL QQALVYYRSD EDDSQYSHPL DFCPIVDTEE
210 220 230 240 250
KKVIFIDIPN RRRKVSKHKH ANFYPKHMIE KVGAMRPEAP PINVTQPEGV
260 270 280 290 300
SFKMTGNVME WSNFKFHIGF NYREGIVLSD VSYNDHGNVR PIFHRISLSE
310 320 330 340 350
MIVPYGSPEF PHQRKHALDI GEYGAGYMTN PLSLGCDCKG VIHYLDAHFS
360 370 380 390 400
DRAGDPITVK NAVCIHEEDD GLLFKHSDFR DNFATSLVTR ATKLVVSQIF
410 420 430 440 450
TAANYEYCLY WVFMQDGAIR LDIRLTGILN TYILGDDEEA GPWGTRVYPN
460 470 480 490 500
VNAHNHQHLF SLRIDPRIDG DGNSAAACDA KSSPYPLGSP ENMYGNAFYS
510 520 530 540 550
EKTTFKTVKD SLTNYESATG RSWDIFNPNK VNPYSGKPPS YKLVSTQCPP
560 570 580 590 600
LLAKEGSLVA KRAPWASHSV NVVPYKDNRL YPSGDHVPQW SGDGVRGMRE
610 620 630 640 650
WIGDGSENID NTDILFFHTF GITHFPAPED FPLMPAEPIT LMLRPRHFFT
660 670 680 690
ENPGLDIQPS YAMTTSEAKR AVHKETKDKT SRLAFEGSCC GK
Length:692
Mass (Da):77,534
Last modified:October 1, 1989 - v1
Checksum:i65B13F0EF5656027
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15111 Genomic DNA. Translation: CAA33209.1.
PIRiS04963.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15111 Genomic DNA. Translation: CAA33209.1.
PIRiS04963.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A2VX-ray2.40A/B/C/D/E/F18-672[»]
1EKMX-ray2.50A/B/C17-672[»]
2OOVX-ray1.70A/B/C/D/E/F13-672[»]
2OQEX-ray1.60A/B/C/D/E/F13-672[»]
3N9HX-ray2.50A/B/C/D/E/F1-692[»]
3NBBX-ray2.05A/B/C/D/E/F1-692[»]
3NBJX-ray1.90A/B/C/D/E/F1-692[»]
3SX1X-ray1.73A/B/C1-692[»]
3SXXX-ray1.27A/B/C/D/E/F1-692[»]
3T0UX-ray1.90A/B/C1-692[»]
4EV2X-ray2.18A/B/C/D/E/F1-692[»]
4EV5X-ray2.25A/B/C/D/E/F1-692[»]
4KFDX-ray1.69A/B/C/D/E/F1-692[»]
4KFEX-ray2.10A/B/C/D/E/F1-692[»]
4KFFX-ray2.15A/B/C1-692[»]
ProteinModelPortaliP12807.
SMRiP12807. Positions 17-672.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP12807.
ChEMBLiCHEMBL5020.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.4.3.21. 2587.

Miscellaneous databases

EvolutionaryTraceiP12807.

Family and domain databases

Gene3Di2.70.98.20. 1 hit.
InterProiIPR000269. Cu_amine_oxidase.
IPR015798. Cu_amine_oxidase_C.
IPR016182. Cu_amine_oxidase_N-reg.
IPR015800. Cu_amine_oxidase_N2.
IPR015802. Cu_amine_oxidase_N3.
[Graphical view]
PANTHERiPTHR10638. PTHR10638. 1 hit.
PfamiPF01179. Cu_amine_oxid. 1 hit.
PF02727. Cu_amine_oxidN2. 1 hit.
PF02728. Cu_amine_oxidN3. 1 hit.
[Graphical view]
SUPFAMiSSF49998. SSF49998. 1 hit.
SSF54416. SSF54416. 2 hits.
PROSITEiPS01164. COPPER_AMINE_OXID_1. 1 hit.
PS01165. COPPER_AMINE_OXID_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAMO_PICAN
AccessioniPrimary (citable) accession number: P12807
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: January 20, 2016
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.