ID C1DEU3_AZOVD Unreviewed; 329 AA.
AC C1DEU3;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Renalase {ECO:0000256|HAMAP-Rule:MF_02074};
DE EC=1.6.3.5 {ECO:0000256|HAMAP-Rule:MF_02074};
GN OrderedLocusNames=Avin_41390 {ECO:0000313|EMBL:ACO80272.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO80272.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO80272.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02074}.
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DR EMBL; CP001157; ACO80272.1; -; Genomic_DNA.
DR RefSeq; WP_012702645.1; NC_012560.1.
DR AlphaFoldDB; C1DEU3; -.
DR STRING; 322710.Avin_41390; -.
DR EnsemblBacteria; ACO80272; ACO80272; Avin_41390.
DR KEGG; avn:Avin_41390; -.
DR eggNOG; COG3380; Bacteria.
DR HOGENOM; CLU_036034_0_0_6; -.
DR OMA; VCGDWCL; -.
DR OrthoDB; 5792777at2; -.
DR Proteomes; UP000002424; 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 110..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 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
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 329 AA; 35887 MW; F70A78CE7B7BFD7C CRC64;
MTFPIAIIGT GIAGLSAAGA LRAAGLEVQL FDKGRGSGGR MASKRTEVGA LDLGAQYFTC
RDRRFAEAVQ QWRDRGWIAE WQPSLYDSAN GTLRPSQDEQ IRWIGTPRMS ALTRGLLGDM
PVRFSCRITE VFHGKQHWML QDADGKAYGP FNQVVVATPS PQAAQLLAAA PKLASSVASV
AMEPNWAVAL SFEQPLDTPV DGCFIQDSPL EWASRNHGKP GRASQPDTWV LQANSRWTRQ
YLDLAKDQVI EQLYGAFAEM IGCTVPEPVF SLAHRWLYGR PVGSHGWGAL ADSSLGLYAC
GDWCLSGRVE GAWLSGQAVA RKLLQHRAS
//