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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//