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Database: UniProt
Entry: B0F9F6_RHOER
LinkDB: B0F9F6_RHOER
Original site: B0F9F6_RHOER 
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
//
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