URODH_PSEPK
ID URODH_PSEPK Reviewed; 268 AA.
AC Q88NN6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Uronate dehydrogenase;
DE EC=1.1.1.203 {ECO:0000269|PubMed:19060141};
DE AltName: Full=D-galacturonate dehydrogenase;
DE AltName: Full=D-glucuronate dehydrogenase;
DE AltName: Full=Hexuronate dehydrogenase;
GN Name=udh; OrderedLocusNames=PP_1171;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, GENE NAME,
RP CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=19060141; DOI=10.1128/jb.00586-08;
RA Yoon S.H., Moon T.S., Iranpour P., Lanza A.M., Prather K.J.;
RT "Cloning and characterization of uronate dehydrogenases from two
RT pseudomonads and Agrobacterium tumefaciens strain C58.";
RL J. Bacteriol. 191:1565-1573(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
CC -!- FUNCTION: Catalyzes the oxidation of beta-D-galacturonate and beta-D-
CC glucuronate to galactarate and D-glucarate, respectively.
CC {ECO:0000269|PubMed:19060141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-galacturonate + NAD(+) = D-galactaro-1,5-lactone + H(+)
CC + NADH; Xref=Rhea:RHEA:22404, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83383, ChEBI:CHEBI:85312;
CC EC=1.1.1.203; Evidence={ECO:0000269|PubMed:19060141};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-glucuronate + NAD(+) = D-glucaro-1,5-lactone + H(+) +
CC NADH; Xref=Rhea:RHEA:43500, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:83384, ChEBI:CHEBI:85313;
CC EC=1.1.1.203; Evidence={ECO:0000269|PubMed:19060141};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.25 mM for D-glucuronate {ECO:0000269|PubMed:19060141};
CC KM=0.10 mM for D-galacturonate {ECO:0000269|PubMed:19060141};
CC KM=0.21 mM for NAD(+) {ECO:0000269|PubMed:19060141};
CC Note=kcat is 55 sec(-1) and 30 sec(-1) with D-glucuronate and D-
CC galacturonate as substrate, respectively.;
CC pH dependence:
CC Optimum pH is about 7. {ECO:0000269|PubMed:19060141};
CC Temperature dependence:
CC Activity increases with increasing temperatures between 4 and 42
CC degrees Celsius. Activity is below 20% of the maximum after exposure
CC at 37 degrees Celsius for 30 minutes. {ECO:0000269|PubMed:19060141};
CC -!- PATHWAY: Carbohydrate acid metabolism; D-galacturonate degradation via
CC prokaryotic oxidative pathway.
CC -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; BK006380; DAA06455.1; -; Genomic_DNA.
DR EMBL; AE015451; AAN66795.1; -; Genomic_DNA.
DR RefSeq; NP_743331.1; NC_002947.4.
DR RefSeq; WP_010952325.1; NC_002947.4.
DR AlphaFoldDB; Q88NN6; -.
DR SMR; Q88NN6; -.
DR STRING; 160488.PP_1171; -.
DR DNASU; 1045739; -.
DR EnsemblBacteria; AAN66795; AAN66795; PP_1171.
DR KEGG; ppu:PP_1171; -.
DR PATRIC; fig|160488.4.peg.1243; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_079334_0_0_6; -.
DR OMA; RYYFDRF; -.
DR PhylomeDB; Q88NN6; -.
DR BioCyc; PPUT160488:G1G01-1254-MON; -.
DR BRENDA; 1.1.1.203; 10905.
DR UniPathway; UPA01050; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0050388; F:uronate dehydrogenase activity; IEA:UniProtKB-EC.
DR InterPro; IPR001509; Epimerase_deHydtase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF01370; Epimerase; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..268
FT /note="Uronate dehydrogenase"
FT /id="PRO_0000429436"
FT ACT_SITE 140
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 17..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 37..39
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 55..56
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115..117
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 29375 MW; F0D8602F7D8312DC CRC64;
MTTTPFNRLL LTGAAGGLGK VLRERLKGYA EVLRLSDISP MAPAAGPHEE VITCDLADKA
AVHTLVEGVD AIIHFGGVST EHAFEEILGP NICGVFHVYE AARKHGVKRI IFASSNHTIG
FYRQDERIDA HAPRRPDSYY GLSKCYGEDV ASFYFDRYGI ETVSIRIGSS FPQPQNLRML
CTWLSYDDLV QLIERGLFTP GVGHTIVYGA SDNRTVWWDN RHAAHLGYVP KDSSETFRAA
VEAQPAPAAD DPSMVYQGGA FAVAGPFN
