DEND_CUPNH
ID DEND_CUPNH Reviewed; 324 AA.
AC Q0KBD2;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=D-erythronate dehydrogenase {ECO:0000303|PubMed:27402745};
DE EC=1.1.1.410 {ECO:0000269|PubMed:27402745};
GN Name=denD {ECO:0000303|PubMed:27402745};
GN OrderedLocusNames=H16_A1557 {ECO:0000312|EMBL:CAJ92689.1};
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=27402745; DOI=10.1073/pnas.1605546113;
RA Zhang X., Carter M.S., Vetting M.W., San Francisco B., Zhao S.,
RA Al-Obaidi N.F., Solbiati J.O., Thiaville J.J., de Crecy-Lagard V.,
RA Jacobson M.P., Almo S.C., Gerlt J.A.;
RT "Assignment of function to a domain of unknown function: DUF1537 is a new
RT kinase family in catabolic pathways for acid sugars.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E4161-E4169(2016).
CC -!- FUNCTION: Catalyzes oxidation of D-erythronate to 2-oxo-tetronate. Can
CC use either NAD(+) or NADP(+) as cosubstrate, with a preference for
CC NAD(+). {ECO:0000269|PubMed:27402745}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythronate + NAD(+) = 2-dehydro-D-erythronate + H(+) +
CC NADH; Xref=Rhea:RHEA:52544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:136591, ChEBI:CHEBI:136668;
CC EC=1.1.1.410; Evidence={ECO:0000269|PubMed:27402745};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.59 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC KM=2.4 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC Note=kcat is 19 sec(-1) with NAD(+) as cosubstrate. kcat is 3.0 sec(-
CC 1) with NADP(+) as cosubstrate. {ECO:0000269|PubMed:27402745};
CC -!- DISRUPTION PHENOTYPE: Deletion mutant is unable to use D-erythronate as
CC a carbon source. {ECO:0000269|PubMed:27402745}.
CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC family. {ECO:0000305}.
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DR EMBL; AM260479; CAJ92689.1; -; Genomic_DNA.
DR RefSeq; WP_011615150.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0KBD2; -.
DR SMR; Q0KBD2; -.
DR STRING; 381666.H16_A1557; -.
DR EnsemblBacteria; CAJ92689; CAJ92689; H16_A1557.
DR GeneID; 57643656; -.
DR KEGG; reh:H16_A1557; -.
DR PATRIC; fig|381666.6.peg.1942; -.
DR eggNOG; COG0451; Bacteria.
DR HOGENOM; CLU_007383_19_0_4; -.
DR OMA; HWHASPR; -.
DR OrthoDB; 1180629at2; -.
DR BRENDA; 1.1.1.410; 231.
DR Proteomes; UP000008210; Chromosome 1.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
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 Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..324
FT /note="D-erythronate dehydrogenase"
FT /id="PRO_0000439746"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 149
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
FT BINDING 153
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P09147"
SQ SEQUENCE 324 AA; 34270 MW; 4D55F79BF40C8456 CRC64;
MNVLITGGAG FLGLQLARLL LQRGTLNLDG QPVAIKRLTL LDVVAPQGLD DARVRVVTGD
LSDPAVLRQA IDTDTGAVFH LAAVVSGQAE ADFDLGMRVN LDASRALLET CRELGHQPRV
LFTSSVAVYG GQLPPVVQDD TALNPQSSYG VQKAIGELLL SDYSRRGFVD GRVLRLPTIS
VRPGKPNAAA SSFASGIIRE PLSGVAANCP VAPETPLWLL SPRAAVAALV NGIELAGERL
GNRRVVNLPG LSVTAAGMIE ALRRVAGNAV ADRVTWEREA RVENIVGTWP AAWNAERALA
LGFQSDASFD EVIRAYMEDA GLAK
