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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)DescriptionActionsGraphical viewLength
Active sitei319Proton acceptor1 Publication1
Active sitei405Schiff-base intermediate with substrate; via topaquinoneCombined sources2 Publications1
Metal bindingi456Copper; via tele nitrogenCombined sources2 Publications1
Metal bindingi458Copper; via tele nitrogenCombined sources2 Publications1
Metal bindingi465ManganeseBy similarity1
Metal bindingi613ManganeseBy similarity1
Metal bindingi614Manganese; via carbonyl oxygenBy similarity1
Metal bindingi624Copper; via pros nitrogenCombined sources2 Publications1

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)DescriptionActionsGraphical viewLength
Mutagenesisi319D → E: Strongly reduced activity. 1 Publication1
Mutagenesisi319D → N: Loss of activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL5020.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000641061 – 692Peroxisomal primary amine oxidaseAdd BLAST692

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi243N-linked (GlcNAc...)1 Publication1
Disulfide bondi338 ↔ 364Combined sources2 Publications
Modified residuei4052',4',5'-topaquinoneCombined sources1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, TPQ

Proteomic databases

PRIDEiP12807.

Expressioni

Inductioni

By methylamine.

Interactioni

Subunit structurei

Homodimer.3 Publications

Chemistry databases

BindingDBiP12807.

Structurei

Secondary structure

1692
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 43Combined sources14
Turni44 – 46Combined sources3
Beta strandi49 – 57Combined sources9
Helixi61 – 69Combined sources9
Beta strandi78 – 85Combined sources8
Beta strandi89 – 97Combined sources9
Turni98 – 101Combined sources4
Beta strandi102 – 109Combined sources8
Helixi118 – 122Combined sources5
Helixi124 – 130Combined sources7
Helixi132 – 140Combined sources9
Helixi145 – 150Combined sources6
Beta strandi151 – 157Combined sources7
Turni162 – 166Combined sources5
Beta strandi170 – 177Combined sources8
Helixi185 – 187Combined sources3
Beta strandi193 – 197Combined sources5
Turni198 – 201Combined sources4
Beta strandi202 – 207Combined sources6
Helixi225 – 232Combined sources8
Beta strandi243 – 245Combined sources3
Beta strandi253 – 255Combined sources3
Beta strandi258 – 261Combined sources4
Beta strandi264 – 271Combined sources8
Turni272 – 274Combined sources3
Beta strandi275 – 285Combined sources11
Beta strandi288 – 305Combined sources18
Helixi312 – 314Combined sources3
Helixi319 – 322Combined sources4
Turni325 – 328Combined sources4
Turni333 – 337Combined sources5
Beta strandi343 – 350Combined sources8
Beta strandi356 – 377Combined sources22
Helixi379 – 381Combined sources3
Beta strandi385 – 402Combined sources18
Beta strandi405 – 413Combined sources9
Beta strandi419 – 427Combined sources9
Beta strandi431 – 433Combined sources3
Turni441 – 443Combined sources3
Beta strandi444 – 448Combined sources5
Beta strandi451 – 454Combined sources4
Beta strandi456 – 466Combined sources11
Beta strandi473 – 482Combined sources10
Helixi490 – 492Combined sources3
Beta strandi498 – 504Combined sources7
Helixi508 – 511Combined sources4
Helixi517 – 519Combined sources3
Beta strandi522 – 526Combined sources5
Turni533 – 535Combined sources3
Beta strandi540 – 544Combined sources5
Helixi558 – 562Combined sources5
Helixi564 – 567Combined sources4
Beta strandi568 – 574Combined sources7
Helixi597 – 602Combined sources6
Beta strandi610 – 612Combined sources3
Beta strandi614 – 624Combined sources11
Helixi628 – 630Combined sources3
Beta strandi631 – 633Combined sources3
Beta strandi637 – 651Combined sources15
Turni653 – 656Combined sources4
Beta strandi660 – 663Combined sources4
Helixi665 – 671Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12807.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 328Substrate bindingCombined sourcesAdd BLAST12
Regioni402 – 407Substrate bindingBy similarity6

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP12807.
ChEMBLiCHEMBL5020.

Proteomic databases

PRIDEiP12807.

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: November 2, 2016
This is version 112 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.