URODH_PSESM
ID URODH_PSESM Reviewed; 275 AA.
AC Q888H1; B0G0W7; F5HD46;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=PSPTO_1053;
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 [GENOMIC DNA], IDENTIFICATION, FUNCTION, GENE NAME,
RP CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=ATCC BAA-871 / DC3000;
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 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).
CC -!- FUNCTION: Catalyzes the oxidation of beta-D-galacturonate and beta-D-
CC glucuronate to galactarate and D-glucarate, respectively. Cannot use
CC NADP(+) instead of NAD(+) as cosubstrate.
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=0.28 mM for D-glucuronate {ECO:0000269|PubMed:19060141};
CC KM=0.04 mM for D-galacturonate {ECO:0000269|PubMed:19060141};
CC KM=0.17 mM for NAD(+) {ECO:0000269|PubMed:19060141};
CC Note=kcat is 74 sec(-1) and 24 sec(-1) with D-glucuronate and D-
CC galacturonate as substrate, respectively.;
CC pH dependence:
CC Optimum pH is 8. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU377538; ABY64888.1; -; Genomic_DNA.
DR EMBL; AE016853; AAO54584.1; -; Genomic_DNA.
DR RefSeq; NP_790889.1; NC_004578.1.
DR RefSeq; WP_011103399.1; NC_004578.1.
DR AlphaFoldDB; Q888H1; -.
DR SMR; Q888H1; -.
DR STRING; 223283.PSPTO_1053; -.
DR EnsemblBacteria; AAO54584; AAO54584; PSPTO_1053.
DR GeneID; 1182687; -.
DR KEGG; pst:PSPTO_1053; -.
DR PATRIC; fig|223283.9.peg.1065; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_079334_0_0_6; -.
DR OMA; RYYFDRF; -.
DR OrthoDB; 1180629at2; -.
DR PhylomeDB; Q888H1; -.
DR BioCyc; MetaCyc:MON-15612; -.
DR BRENDA; 1.1.1.203; 10904.
DR UniPathway; UPA01050; -.
DR Proteomes; UP000002515; 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..275
FT /note="Uronate dehydrogenase"
FT /id="PRO_0000429435"
FT ACT_SITE 145
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 22..23
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 42..44
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 60..61
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 80..84
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 275 AA; 30598 MW; F24A0E96386BCD7C CRC64;
MASAHTTQTP FNRLLLTGAA GGLGKVLRET LRPYSHILRL SDIAEMAPAV GDHEEVQVCD
LADKDAVHRL VEGVDAILHF GGVSVERPFE EILGANICGV FHIYEAARRH GVKRVIFASS
NHVIGFYKQN ETIDAHSPRR PDSYYGLSKS YGEDMASFYF DRYGIETVSI RIGSSFPEPQ
NRRMMSTWLS FDDLTRLLER ALYTPDVGHT VVYGVSDNKT VWWDNRFASK LDYAPKDSSE
VFRAKVDAQP MPADDDPAMV YQGGAFVASG PFGDK
