RNLS_PSESM
ID RNLS_PSESM Reviewed; 328 AA.
AC Q888A4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Renalase {ECO:0000250|UniProtKB:Q48MT7};
DE EC=1.6.3.5 {ECO:0000250|UniProtKB:Q48MT7};
GN OrderedLocusNames=PSPTO_1126 {ECO:0000312|EMBL:AAO54655.1};
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH FAD.
RG Northeast structural genomics consortium (NESG);
RT "X-ray structure of P. syringae Q888A4 oxidoreductase at resolution 2.5A,
RT Northeast Structural Genomics Consortium target PsR10.";
RL Submitted (NOV-2009) to the PDB data bank.
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)+. Has a
CC preference for 1,2-dihydro-beta-NAD as substrate. May serve to protect
CC primary metabolism dehydrogenases from inhibition by the 1,2-
CC dihydro- and 1,6-dihydro-beta-NAD(P) isomers.
CC {ECO:0000250|UniProtKB:Q48MT7}.
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:0000250|UniProtKB:Q48MT7};
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:0000250|UniProtKB:Q48MT7};
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:0000250|UniProtKB:Q48MT7};
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:0000250|UniProtKB:Q48MT7};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q48MT7};
CC -!- SIMILARITY: Belongs to the bacterial renalase family. {ECO:0000305}.
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DR EMBL; AE016853; AAO54655.1; -; Genomic_DNA.
DR RefSeq; NP_790960.1; NC_004578.1.
DR RefSeq; WP_005768828.1; NC_004578.1.
DR PDB; 3KKJ; X-ray; 2.50 A; A/B=1-328.
DR PDBsum; 3KKJ; -.
DR AlphaFoldDB; Q888A4; -.
DR SMR; Q888A4; -.
DR STRING; 223283.PSPTO_1126; -.
DR DrugBank; DB03147; Flavin adenine dinucleotide.
DR EnsemblBacteria; AAO54655; AAO54655; PSPTO_1126.
DR GeneID; 1182762; -.
DR KEGG; pst:PSPTO_1126; -.
DR PATRIC; fig|223283.9.peg.1136; -.
DR eggNOG; COG3380; Bacteria.
DR HOGENOM; CLU_036034_0_0_6; -.
DR OMA; VCGDWCL; -.
DR OrthoDB; 1442136at2; -.
DR PhylomeDB; Q888A4; -.
DR EvolutionaryTrace; Q888A4; -.
DR Proteomes; UP000002515; 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; 3.50.50.60; -; 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 Pfam; PF01593; Amino_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 1: Evidence at protein level;
KW 3D-structure; FAD; Flavoprotein; NAD; NADP; Nucleotide-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..328
FT /note="Renalase"
FT /id="PRO_0000437675"
FT BINDING 13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 32..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 56..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 57..61
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48MT7"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48MT7"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48MT7"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q48MT7"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|Ref.2, ECO:0007744|PDB:3KKJ"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 63..75
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:3KKJ"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 269..283
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 288..292
FT /evidence="ECO:0007829|PDB:3KKJ"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:3KKJ"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3KKJ"
FT HELIX 309..326
FT /evidence="ECO:0007829|PDB:3KKJ"
SQ SEQUENCE 328 AA; 35840 MW; 672D6BC25518DE76 CRC64;
MTVPIAIIGT GIAGLSAAQA LTAAGHQVHL FDKSRGSGGR MSSKRSDAGA LDMGAQYFTA
RDRRFATAVK QWQAQGHVAE WTPLLYNFHA GRLSPSPDEQ VRWVGKPGMS AITRAMRGDM
PVSFSCRITE VFRGEEHWNL LDAEGQNHGP FSHVIIATPA PQASTLLAAA PKLASVVAGV
KMDPTWAVAL AFETPLQTPM QGCFVQDSPL DWLARNRSKP ERDDTLDTWI LHATSQWSRQ
NLDASREQVI EHLHGAFAEL IDCTMPAPVF SLAHRWLYAR PAGAHEWGAL SDADLGIYVC
GDWCLSGRVE GAWLSGQEAA RRLLEHLQ
