AMO_PICAN
ID AMO_PICAN Reviewed; 692 AA.
AC P12807;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Peroxisomal primary amine oxidase;
DE EC=1.4.3.21 {ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552};
DE AltName: Full=Copper amine oxidase;
DE AltName: Full=Methylamine oxidase;
GN Name=AMO;
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=2500147; DOI=10.1016/0167-4781(80)90003-2;
RA Bruinenberg P.G., Evers M., Waterham H.R., Kuipers J., Arnberg A.C., Ab G.;
RT "Cloning and sequencing of the peroxisomal amine oxidase gene from
RT Hansenula polymorpha.";
RL Biochim. Biophys. Acta 1008:157-167(1989).
RN [2]
RP PROTEIN SEQUENCE OF 231-238, COFACTOR, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=7556609; DOI=10.1016/0014-5793(95)00907-q;
RA Plastino J., Klinman J.P.;
RT "Limited proteolysis of Hansenula polymorpha yeast amine oxidase: isolation
RT of a C-terminal fragment containing both a copper and quino-cofactor.";
RL FEBS Lett. 371:276-278(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH COPPER IONS,
RP TOPAQUINONE AT TYR-405, GLYCOSYLATION AT ASN-243, MUTAGENESIS OF ASP-319,
RP SUBUNIT, CATALYTIC ACTIVITY, ACTIVE SITE, AND DISULFIDE BOND.
RX PubMed=9551552; DOI=10.1016/s0969-2126(98)00033-1;
RA Li R., Klinman J.P., Mathews F.S.;
RT "Copper amine oxidase from Hansenula polymorpha: the crystal structure
RT determined at 2.4-A resolution reveals the active conformation.";
RL Structure 6:293-307(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 17-672 IN COMPLEX WITH ZINC IONS,
RP ACTIVE SITE, AND DISULFIDE BOND.
RX PubMed=10933787; DOI=10.1021/bi000639f;
RA Chen Z.-W., Schwartz B., Williams N.K., Li R., Klinman J.P., Mathews F.S.;
RT "Crystal structure at 2.5 A resolution of zinc-substituted copper amine
RT oxidase of Hansenula polymorpha expressed in Escherichia coli.";
RL Biochemistry 39:9709-9717(2000).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+);
CC Xref=Rhea:RHEA:16153, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:17478, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:58001; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:7556609,
CC ECO:0000269|PubMed:9551552};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552};
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:10933787};
CC Note=Binds 1 copper ion per subunit. Can also use zinc ion as cofactor
CC (PubMed:10933787). {ECO:0000269|PubMed:10933787,
CC ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552};
CC -!- COFACTOR:
CC Name=L-topaquinone; Xref=ChEBI:CHEBI:79027;
CC Evidence={ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552};
CC Note=Contains 1 topaquinone per subunit. {ECO:0000269|PubMed:7556609,
CC ECO:0000269|PubMed:9551552};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q43077};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000250|UniProtKB:Q43077};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10933787,
CC ECO:0000269|PubMed:7556609, ECO:0000269|PubMed:9551552}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305|PubMed:9551552}.
CC -!- INDUCTION: By methylamine.
CC -!- PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of
CC a specific tyrosyl residue. {ECO:0000269|PubMed:10933787,
CC ECO:0000269|PubMed:9551552}.
CC -!- SIMILARITY: Belongs to the copper/topaquinone oxidase family.
CC {ECO:0000305}.
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DR EMBL; X15111; CAA33209.1; -; Genomic_DNA.
DR PIR; S04963; S04963.
DR PDB; 1A2V; X-ray; 2.40 A; A/B/C/D/E/F=18-672.
DR PDB; 1EKM; X-ray; 2.50 A; A/B/C=17-672.
DR PDB; 2OOV; X-ray; 1.70 A; A/B/C/D/E/F=13-672.
DR PDB; 2OQE; X-ray; 1.60 A; A/B/C/D/E/F=13-672.
DR PDB; 3N9H; X-ray; 2.50 A; A/B/C/D/E/F=1-692.
DR PDB; 3NBB; X-ray; 2.05 A; A/B/C/D/E/F=1-692.
DR PDB; 3NBJ; X-ray; 1.90 A; A/B/C/D/E/F=1-692.
DR PDB; 3SX1; X-ray; 1.73 A; A/B/C=1-692.
DR PDB; 3SXX; X-ray; 1.27 A; A/B/C/D/E/F=1-692.
DR PDB; 3T0U; X-ray; 1.90 A; A/B/C=1-692.
DR PDB; 4EV2; X-ray; 2.18 A; A/B/C/D/E/F=1-692.
DR PDB; 4EV5; X-ray; 2.25 A; A/B/C/D/E/F=1-692.
DR PDB; 4KFD; X-ray; 1.69 A; A/B/C/D/E/F=1-692.
DR PDB; 4KFE; X-ray; 2.10 A; A/B/C/D/E/F=1-692.
DR PDB; 4KFF; X-ray; 2.15 A; A/B/C=1-692.
DR PDBsum; 1A2V; -.
DR PDBsum; 1EKM; -.
DR PDBsum; 2OOV; -.
DR PDBsum; 2OQE; -.
DR PDBsum; 3N9H; -.
DR PDBsum; 3NBB; -.
DR PDBsum; 3NBJ; -.
DR PDBsum; 3SX1; -.
DR PDBsum; 3SXX; -.
DR PDBsum; 3T0U; -.
DR PDBsum; 4EV2; -.
DR PDBsum; 4EV5; -.
DR PDBsum; 4KFD; -.
DR PDBsum; 4KFE; -.
DR PDBsum; 4KFF; -.
DR AlphaFoldDB; P12807; -.
DR SMR; P12807; -.
DR BindingDB; P12807; -.
DR ChEMBL; CHEMBL5020; -.
DR iPTMnet; P12807; -.
DR PRIDE; P12807; -.
DR BRENDA; 1.4.3.21; 2587.
DR EvolutionaryTrace; P12807; -.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0052595; F:aliphatic-amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0052594; F:aminoacetone:oxygen oxidoreductase(deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0052596; F:phenethylamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0008131; F:primary amine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0052593; F:tryptamine:oxygen oxidoreductase (deaminating) activity; IEA:UniProtKB-EC.
DR GO; GO:0009308; P:amine metabolic process; IEA:InterPro.
DR Gene3D; 2.70.98.20; -; 1.
DR InterPro; IPR000269; Cu_amine_oxidase.
DR InterPro; IPR015798; Cu_amine_oxidase_C.
DR InterPro; IPR036460; Cu_amine_oxidase_C_sf.
DR InterPro; IPR016182; Cu_amine_oxidase_N-reg.
DR InterPro; IPR015800; Cu_amine_oxidase_N2.
DR InterPro; IPR015802; Cu_amine_oxidase_N3.
DR PANTHER; PTHR10638; PTHR10638; 1.
DR Pfam; PF01179; Cu_amine_oxid; 1.
DR Pfam; PF02727; Cu_amine_oxidN2; 1.
DR Pfam; PF02728; Cu_amine_oxidN3; 1.
DR SUPFAM; SSF49998; SSF49998; 1.
DR SUPFAM; SSF54416; SSF54416; 2.
DR PROSITE; PS01164; COPPER_AMINE_OXID_1; 1.
DR PROSITE; PS01165; COPPER_AMINE_OXID_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Manganese; Metal-binding; Oxidoreductase; Peroxisome; TPQ.
FT CHAIN 1..692
FT /note="Peroxisomal primary amine oxidase"
FT /id="PRO_0000064106"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 319
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:9551552"
FT ACT_SITE 405
FT /note="Schiff-base intermediate with substrate; via
FT topaquinone"
FT /evidence="ECO:0000269|PubMed:10933787,
FT ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1EKM,
FT ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ,
FT ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4KFF"
FT BINDING 317..328
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4EV2, ECO:0007744|PDB:4EV5"
FT BINDING 402..407
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P46883"
FT BINDING 456
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10933787,
FT ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V,
FT ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV,
FT ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H,
FT ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ,
FT ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2,
FT ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD,
FT ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF"
FT BINDING 458
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10933787,
FT ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V,
FT ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV,
FT ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H,
FT ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ,
FT ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2,
FT ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD,
FT ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF"
FT BINDING 465
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 613
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 614
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q43077"
FT BINDING 624
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /evidence="ECO:0000269|PubMed:10933787,
FT ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V,
FT ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV,
FT ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H,
FT ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ,
FT ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2,
FT ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD,
FT ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF"
FT MOD_RES 405
FT /note="2',4',5'-topaquinone"
FT /evidence="ECO:0000269|PubMed:9551552,
FT ECO:0007744|PDB:1A2V, ECO:0007744|PDB:2OQE"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:9551552"
FT DISULFID 338..364
FT /evidence="ECO:0000269|PubMed:10933787,
FT ECO:0000269|PubMed:9551552, ECO:0007744|PDB:1A2V,
FT ECO:0007744|PDB:1EKM, ECO:0007744|PDB:2OOV,
FT ECO:0007744|PDB:2OQE, ECO:0007744|PDB:3N9H,
FT ECO:0007744|PDB:3NBB, ECO:0007744|PDB:3NBJ,
FT ECO:0007744|PDB:3SX1, ECO:0007744|PDB:3SXX,
FT ECO:0007744|PDB:3T0U, ECO:0007744|PDB:4EV2,
FT ECO:0007744|PDB:4EV5, ECO:0007744|PDB:4KFD,
FT ECO:0007744|PDB:4KFE, ECO:0007744|PDB:4KFF"
FT MUTAGEN 319
FT /note="D->E: Strongly reduced activity."
FT /evidence="ECO:0000269|PubMed:9551552"
FT MUTAGEN 319
FT /note="D->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:9551552"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 49..57
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 61..69
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 132..140
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 162..166
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 264..271
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 288..305
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 325..328
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 333..337
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 343..350
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 356..377
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 379..381
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 385..402
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 405..413
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 419..427
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:3N9H"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 456..466
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 473..482
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:4EV5"
FT STRAND 498..504
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 540..544
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 558..562
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 564..567
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 568..574
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 597..602
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 614..624
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 631..633
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 637..651
FT /evidence="ECO:0007829|PDB:3SXX"
FT TURN 653..656
FT /evidence="ECO:0007829|PDB:3SXX"
FT STRAND 660..663
FT /evidence="ECO:0007829|PDB:3SXX"
FT HELIX 665..671
FT /evidence="ECO:0007829|PDB:3SXX"
SQ SEQUENCE 692 AA; 77534 MW; 65B13F0EF5656027 CRC64;
MERLRQIASQ ATAASAAPAR PAHPLDPLST AEIKAATNTV KSYFAGKKIS FNTVTLREPA
RKAYIQWKEQ GGPLPPRLAY YVILEAGKPG VKEGLVDLAS LSVIETRALE TVQPILTVED
LCSTEEVIRN DPAVIEQCVL SGIPANEMHK VYCDPWTIGY DERWGTGKRL QQALVYYRSD
EDDSQYSHPL DFCPIVDTEE KKVIFIDIPN RRRKVSKHKH ANFYPKHMIE KVGAMRPEAP
PINVTQPEGV SFKMTGNVME WSNFKFHIGF NYREGIVLSD VSYNDHGNVR PIFHRISLSE
MIVPYGSPEF PHQRKHALDI GEYGAGYMTN PLSLGCDCKG VIHYLDAHFS DRAGDPITVK
NAVCIHEEDD GLLFKHSDFR DNFATSLVTR ATKLVVSQIF TAANYEYCLY WVFMQDGAIR
LDIRLTGILN TYILGDDEEA GPWGTRVYPN VNAHNHQHLF SLRIDPRIDG DGNSAAACDA
KSSPYPLGSP ENMYGNAFYS EKTTFKTVKD SLTNYESATG RSWDIFNPNK VNPYSGKPPS
YKLVSTQCPP LLAKEGSLVA KRAPWASHSV NVVPYKDNRL YPSGDHVPQW SGDGVRGMRE
WIGDGSENID NTDILFFHTF GITHFPAPED FPLMPAEPIT LMLRPRHFFT ENPGLDIQPS
YAMTTSEAKR AVHKETKDKT SRLAFEGSCC GK
