ID   DEND_HAEIN              Reviewed;         315 AA.
AC   P44094;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 103.
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}; OrderedLocusNames=HI_1014;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
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=0.23 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC         KM=0.61 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC         Note=kcat is 1.9 sec(-1) with NAD(+) as cosubstrate. kcat is 0.88
CC         sec(-1) with NADP(+) as cosubstrate. {ECO:0000269|PubMed:27402745};
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22675.1; -; Genomic_DNA.
DR   PIR; D64018; D64018.
DR   RefSeq; NP_439175.1; NC_000907.1.
DR   RefSeq; WP_005693350.1; NC_000907.1.
DR   AlphaFoldDB; P44094; -.
DR   SMR; P44094; -.
DR   STRING; 71421.HI_1014; -.
DR   EnsemblBacteria; AAC22675; AAC22675; HI_1014.
DR   KEGG; hin:HI_1014; -.
DR   PATRIC; fig|71421.8.peg.1058; -.
DR   eggNOG; COG0451; Bacteria.
DR   HOGENOM; CLU_007383_19_0_6; -.
DR   OMA; HWHASPR; -.
DR   PhylomeDB; P44094; -.
DR   BioCyc; HINF71421:G1GJ1-1054-MON; -.
DR   BioCyc; MetaCyc:MON-20182; -.
DR   Proteomes; UP000000579; Chromosome.
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..315
FT                   /note="D-erythronate dehydrogenase"
FT                   /id="PRO_0000077991"
FT   ACT_SITE        143
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P09147"
FT   BINDING         119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09147"
FT   BINDING         143
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09147"
FT   BINDING         147
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P09147"
SQ   SEQUENCE   315 AA;  35145 MW;  51595A24A5B54823 CRC64;
     MKVVITGGQG FLGQRLAKTL LAQNNVHIDD LILIDVVKPI APNNDPRVRC YEMNLRYPTG
     LDELITEETD AIFHLAAIVS SHAEQDPDLG YETNFLATRN ILEICRKNNP KVRFIFSSSL
     AIFGGELPET ILDSTAFTPQ STYGTQKAMC ELLINDYSRK GFVDGIVVRL PTICIRPGKP
     NKAASSFVSS IMREPLHGED AVCPVSEELR LWLSSPNTVV ANFIHALQLP SLPLRSWHTI
     NLPGFSVTVK QMLSDLTQVK GEAILEHIKF EFDESINNIV ASWPSRIDNT QALALGFKVD
     SNFQNVIQQF IEYDM