RNLS_PSE14
ID RNLS_PSE14 Reviewed; 328 AA.
AC Q48MT7;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Renalase {ECO:0000303|PubMed:26016690};
DE EC=1.6.3.5 {ECO:0000269|PubMed:26016690};
GN OrderedLocusNames=PSPPH_1014 {ECO:0000312|EMBL:AAZ37485.1};
OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=264730;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1448A / Race 6;
RX PubMed=16159782; DOI=10.1128/jb.187.18.6488-6498.2005;
RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R.,
RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., Gwinn Giglio M.,
RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J.,
RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R.,
RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M.,
RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A.,
RA Buell R.;
RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola
RT 1448A reveals divergence among pathovars in genes involved in virulence and
RT transposition.";
RL J. Bacteriol. 187:6488-6498(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.66 ANGSTROMS) IN COMPLEXES WITH BETA-NADH;
RP BETA-NAD(+) AND FAD, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=1448A / Race 6;
RX PubMed=26016690; DOI=10.1021/acs.biochem.5b00451;
RA Hoag M.R., Roman J., Beaupre B.A., Silvaggi N.R., Moran G.R.;
RT "Bacterial renalase: structure and kinetics of an enzyme with 2- and 6-
RT dihydro-beta-NAD(P) oxidase activity from Pseudomonas phaseolicola.";
RL Biochemistry 54:3791-3802(2015).
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:0000269|PubMed:26016690}.
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:0000269|PubMed:26016690};
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:0000269|PubMed:26016690};
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:0000269|PubMed:26016690};
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:0000269|PubMed:26016690};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:26016690};
CC -!- SIMILARITY: Belongs to the bacterial renalase family. {ECO:0000305}.
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DR EMBL; CP000058; AAZ37485.1; -; Genomic_DNA.
DR RefSeq; WP_011167855.1; NC_005773.3.
DR PDB; 4ZCC; X-ray; 2.00 A; A/B/C/D=1-328.
DR PDB; 4ZCD; X-ray; 1.66 A; A/B=1-328.
DR PDB; 5KRQ; X-ray; 2.09 A; A/B=1-328.
DR PDBsum; 4ZCC; -.
DR PDBsum; 4ZCD; -.
DR PDBsum; 5KRQ; -.
DR AlphaFoldDB; Q48MT7; -.
DR SMR; Q48MT7; -.
DR STRING; 264730.PSPPH_1014; -.
DR EnsemblBacteria; AAZ37485; AAZ37485; PSPPH_1014.
DR KEGG; psp:PSPPH_1014; -.
DR eggNOG; COG3380; Bacteria.
DR HOGENOM; CLU_036034_0_0_6; -.
DR OMA; VCGDWCL; -.
DR OrthoDB; 1442136at2; -.
DR BRENDA; 1.6.3.5; 5174.
DR Proteomes; UP000000551; Chromosome.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB.
DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IDA:UniProtKB.
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.
FT CHAIN 1..328
FT /note="Renalase"
FT /id="PRO_0000437674"
FT BINDING 13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 32..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 56..57
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 57..61
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26016690"
FT BINDING 96..98
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26016690"
FT BINDING 128
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26016690"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:26016690"
FT BINDING 309
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:26016690"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 12..23
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 171..178
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 182..194
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 207..215
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 227..233
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:4ZCD"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 269..283
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:4ZCD"
FT TURN 293..296
FT /evidence="ECO:0007829|PDB:4ZCD"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4ZCD"
FT HELIX 309..326
FT /evidence="ECO:0007829|PDB:4ZCD"
SQ SEQUENCE 328 AA; 35712 MW; B3225EA8F53B5EE6 CRC64;
MTVPIAIIGT GIAGLSAAQA LTSAGHQVHL FDKSRGSGGR MSSKRSDAGS LDMGAQYFTA
RDRRFATAVK QWQAQGHVSE WTPLLYNFHG GRLSPSPDEQ VRWVGEPGMS AITRAMRGDL
PVSFSCRITD VFRGEQHWNL LDAEGENHGP FSHVIIATPA PQATALLAAA PKLASVVAGV
KMDPTWAVAL AFETPLQTPM QGCFVQDSPL DWLARNRSKP GRDDTLDSWV LHATSQWSRQ
NLDASREQVI EHLHGAFAEL IDCAMPAPVF SLAHRWLYAR PAGSHEWGAL SDADLGIYVC
GDWCLSGRVE GAWLSGQEAA RRLLEHLQ
