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Database: UniProt
Entry: C3KDN5_PSEFS
LinkDB: C3KDN5_PSEFS
Original site: C3KDN5_PSEFS 
ID   C3KDN5_PSEFS            Unreviewed;       328 AA.
AC   C3KDN5;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   24-JAN-2024, entry version 89.
DE   RecName: Full=Renalase {ECO:0000256|HAMAP-Rule:MF_02074};
DE            EC=1.6.3.5 {ECO:0000256|HAMAP-Rule:MF_02074};
GN   OrderedLocusNames=PFLU_0754 {ECO:0000313|EMBL:CAY47022.1};
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595 {ECO:0000313|EMBL:CAY47022.1};
RN   [1] {ECO:0000313|EMBL:CAY47022.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAY47022.1};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
RN   [2] {ECO:0000313|EMBL:CAI2795062.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SBW25 {ECO:0000313|EMBL:CAI2795062.1};
RA   Fortmann-Grote C.;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of the 1,2-dihydro- and 1,6-
CC       dihydro- isomeric forms of beta-NAD(P) back to beta-NAD(P)+. May serve
CC       to protect primary metabolism dehydrogenases from inhibition by the
CC       1,2-dihydro- and 1,6-dihydro-beta-NAD(P) isomers. {ECO:0000256|HAMAP-
CC       Rule:MF_02074}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC         Xref=Rhea:RHEA:40395, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88138; EC=1.6.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02074};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC         Xref=Rhea:RHEA:40399, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88137; EC=1.6.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02074};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-dihydro-beta-NAD + H(+) + O2 = H2O2 + NAD(+);
CC         Xref=Rhea:RHEA:47996, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:57540, ChEBI:CHEBI:88140; EC=1.6.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02074};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,6-dihydro-beta-NADP + H(+) + O2 = H2O2 + NADP(+);
CC         Xref=Rhea:RHEA:48000, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:58349, ChEBI:CHEBI:88139; EC=1.6.3.5;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02074};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_02074};
CC   -!- SIMILARITY: Belongs to the bacterial renalase family.
CC       {ECO:0000256|HAMAP-Rule:MF_02074}.
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DR   EMBL; OV986001; CAI2795062.1; -; Genomic_DNA.
DR   EMBL; AM181176; CAY47022.1; -; Genomic_DNA.
DR   RefSeq; WP_012722126.1; NC_012660.1.
DR   AlphaFoldDB; C3KDN5; -.
DR   STRING; 294.SRM1_04782; -.
DR   PATRIC; fig|216595.4.peg.988; -.
DR   eggNOG; COG3380; Bacteria.
DR   HOGENOM; CLU_036034_0_0_6; -.
DR   OMA; VCGDWCL; -.
DR   OrthoDB; 5792777at2; -.
DR   Proteomes; UP001152918; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.90.660.10; -; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   HAMAP; MF_02074; Bact_renalase; 1.
DR   InterPro; IPR002937; Amino_oxidase.
DR   InterPro; IPR034721; Bac_renal.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR16128; FAD/NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR16128:SF5; FAD/NAD(P)-BINDING OXIDOREDUCTASE FAMILY PROTEIN; 1.
DR   Pfam; PF01593; Amino_oxidase; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|HAMAP-Rule:MF_02074};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_02074};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_02074};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_02074};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02074};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_02074}.
FT   DOMAIN          108..324
FT                   /note="Amine oxidase"
FT                   /evidence="ECO:0000259|Pfam:PF01593"
FT   BINDING         13
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         32..33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         40
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         56..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         57..61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         96..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         128
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         185
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         302
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         308
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
FT   BINDING         309
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02074"
SQ   SEQUENCE   328 AA;  35901 MW;  D4688E595645E8ED CRC64;
     MTVPIAIIGT GIAGLSAARA LRDAGHVVQL FDKSRGSGGR MSSKRSDAGS LDMGAQYFTA
     RDRRFVNEVQ RWQSNGWAEQ WKPQLYNFKS GQLTPSPDEQ IRWVGTPRMS AITRALLDDL
     PVEFGCRITE VFQGKQHWNL LDADSENHGP FSHVIIATPA PQATALLAAA PKLASAAAGV
     KMDPTWAIAL AFDKPLDTPM EGCFVQDSPL DWLARNRSKP GRDTALDTWV LHATSAWSKA
     HLDLSKEAVI EHLHGAFAEL LHSAMPAPSF SLAHRWLYAR PSSSHEFGVL ADADLGLYVC
     GDWCLSGRVE GAWLSGQEAA RRLIEHLQ
//
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