ID B0F9F6_RHOER Unreviewed; 453 AA.
AC B0F9F6;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Putrescine oxidase {ECO:0000313|EMBL:ABY74497.1};
DE Flags: Fragment;
GN Name=puo {ECO:0000313|EMBL:ABY74497.1};
OS Rhodococcus erythropolis (Arthrobacter picolinophilus).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=1833 {ECO:0000313|EMBL:ABY74497.1};
RN [1] {ECO:0000313|EMBL:ABY74497.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NCIMB 11540 {ECO:0000313|EMBL:ABY74497.1};
RX PubMed=18183391; DOI=10.1007/s00253-007-1310-4;
RA van Hellemond E.W., van Dijk M., Heuts D.P., Janssen D.B., Fraaije M.W.;
RT "Discovery and characterization of a putrescine oxidase from Rhodococcus
RT erythropolis NCIMB 11540.";
RL Appl. Microbiol. Biotechnol. 78:455-463(2008).
RN [2] {ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD.
RX PubMed=21486042; DOI=10.1021/bi200372u;
RA Kopacz M.M., Rovida S., van Duijn E., Fraaije M.W., Mattevi A.;
RT "Structure-based redesign of cofactor binding in putrescine oxidase.";
RL Biochemistry 50:4209-4217(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the flavin monoamine oxidase family.
CC {ECO:0000256|ARBA:ARBA00005995}.
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DR EMBL; EU240877; ABY74497.1; -; Genomic_DNA.
DR PDB; 2YG3; X-ray; 2.00 A; A/B=1-453.
DR PDB; 2YG4; X-ray; 2.30 A; A/B=1-453.
DR PDB; 2YG5; X-ray; 1.90 A; A=1-453.
DR PDB; 2YG6; X-ray; 2.50 A; A/B=1-453.
DR PDB; 2YG7; X-ray; 2.75 A; A/B=1-453.
DR PDBsum; 2YG3; -.
DR PDBsum; 2YG4; -.
DR PDBsum; 2YG5; -.
DR PDBsum; 2YG6; -.
DR PDBsum; 2YG7; -.
DR AlphaFoldDB; B0F9F6; -.
DR SMR; B0F9F6; -.
DR BRENDA; 1.4.3.10; 5389.
DR EvolutionaryTrace; B0F9F6; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.405.10; Guanine Nucleotide Dissociation Inhibitor, domain 1; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR001613; Flavin_amine_oxidase.
DR PANTHER; PTHR43563; AMINE OXIDASE; 1.
DR PANTHER; PTHR43563:SF1; AMINE OXIDASE [FLAVIN-CONTAINING] B; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR PRINTS; PR00757; AMINEOXDASEF.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4};
KW FAD {ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4};
KW Flavoprotein {ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4};
KW Nucleotide-binding {ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 16..448
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT BINDING 15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 16
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 37
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 59
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 60
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 235
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 385
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 431
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT BINDING 433
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0007829|PDB:2YG3, ECO:0007829|PDB:2YG4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABY74497.1"
SQ SEQUENCE 453 AA; 49343 MW; 367B0103726886D2 CRC64;
VPTLQRDVAI VGAGPSGLAA ATALRKAGLS VAVIEARDRV GGRTWTDTID GAVLEIGGQW
VSPDQTALIS LLDELGLKTF ERYREGESVY ISSAGERTRY TGDSFPTNET TKKEMDRLID
EMDDLAAQIG AEEPWAHPLA RDLDTVSFKQ WLINQSDDAE ARDNIGLFIA GGMLTKPAHS
FSALQAVLMA ASAGSFSHLV DEDFILDKRV IGGMQQVSIR MAEALGDDVF LNAPVRTVKW
NESGATVLAD GDIRVEASRV ILAVPPNLYS RISYDPPLPR RQHQMHQHQS LGLVIKVHAV
YETPFWREDG LSGTGFGASE VVQEVYDNTN HEDDRGTLVA FVSDEKADAM FELSAEERKA
TILASLARYL GPKAEEPVVY YESDWGSEEW TRGAYAASFD LGGLHRYGAD SRTPVGPIHF
SCSDIAAEGY QHVDGAVRMG QRTAADIIAR SKA
//