ID A0A1T1HRS8_9PSED Unreviewed; 328 AA.
AC A0A1T1HRS8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Renalase {ECO:0000256|HAMAP-Rule:MF_02074};
DE EC=1.6.3.5 {ECO:0000256|HAMAP-Rule:MF_02074};
GN ORFNames=MF4836_24425 {ECO:0000313|EMBL:OOV92555.1};
OS Pseudomonas sp. MF4836.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1960827 {ECO:0000313|EMBL:OOV92555.1, ECO:0000313|Proteomes:UP000190183};
RN [1] {ECO:0000313|Proteomes:UP000190183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF4836 {ECO:0000313|Proteomes:UP000190183};
RA Fagerlund A.;
RT "Genome sequencing of bacteria from food industry.";
RL Submitted (FEB-2017) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OOV92555.1}.
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DR EMBL; MVOL01000011; OOV92555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T1HRS8; -.
DR STRING; 1960827.MF4836_24425; -.
DR Proteomes; UP000190183; Unassembled WGS sequence.
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:SF8; EXPRESSED PROTEIN; 1.
DR PANTHER; PTHR16128; 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 109..323
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; 35732 MW; 9FFE7F0A489B77D2 CRC64;
MTVPIAIIGT GIAGLSAAQA LHDAGHVVQL FDKSRGSGGR MSSKRSDAGA LDMGAQYFTA
RDRRFVTEVQ RWQANGWVAE WTPQLYNSHG GQLSPSPDEQ TRWVGTPRMS AITRALLGDM
EVHFACRITE VFRGEQHWHL QDAEGVTHGP FSHVVIATPA PQATALLTAA PKLAGAAAGV
KMDPTWAIAL AFDTPLETPM QGCFVQDSPL DWLARNRSKP GRDSTLDTWV LHATSAWSRQ
NIDLSKEAVI EQLHGAFAEL LHSAMPAPTF SLAHRWLYAR PATSHEWGAL ADADLGLYVC
GDWCLSGRVE GAWLSGQEAA RRLHENLQ
//
