ID   LTND_HAEIN              Reviewed;         301 AA.
AC   P44979;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=L-threonate dehydrogenase {ECO:0000303|PubMed:27402745};
DE            EC=1.1.1.411 {ECO:0000269|PubMed:27402745};
GN   Name=ltnD {ECO:0000303|PubMed:27402745}; OrderedLocusNames=HI_1010;
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 L-threonate 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=L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH;
CC         Xref=Rhea:RHEA:52548, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57561, ChEBI:CHEBI:57945, ChEBI:CHEBI:136669;
CC         EC=1.1.1.411; Evidence={ECO:0000269|PubMed:27402745};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.024 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC         KM=0.14 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC         Note=kcat is 9.7 sec(-1) with NAD(+) as cosubstrate. kcat is 2.9
CC         sec(-1) with NADP(+) as cosubstrate. {ECO:0000269|PubMed:27402745};
CC   -!- SIMILARITY: Belongs to the HIBADH-related family. L-threonate
CC       dehydrogenase subfamily. {ECO:0000305}.
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DR   EMBL; L42023; AAC22671.1; -; Genomic_DNA.
DR   PIR; B64164; B64164.
DR   RefSeq; NP_439171.1; NC_000907.1.
DR   RefSeq; WP_005665973.1; NC_000907.1.
DR   AlphaFoldDB; P44979; -.
DR   SMR; P44979; -.
DR   STRING; 71421.HI_1010; -.
DR   EnsemblBacteria; AAC22671; AAC22671; HI_1010.
DR   KEGG; hin:HI_1010; -.
DR   PATRIC; fig|71421.8.peg.1054; -.
DR   eggNOG; COG2084; Bacteria.
DR   HOGENOM; CLU_035117_1_2_6; -.
DR   OMA; QMFMQAS; -.
DR   PhylomeDB; P44979; -.
DR   BioCyc; HINF71421:G1GJ1-1050-MON; -.
DR   BioCyc; MetaCyc:MON-20181; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0016054; P:organic acid catabolic process; IEA:UniProt.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   InterPro; IPR002204; 3-OH-isobutyrate_DH-rel_CS.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR006115; 6PGDH_NADP-bd.
DR   InterPro; IPR015815; HIBADH-related.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR029154; NADP-bd.
DR   Pfam; PF14833; NAD_binding_11; 1.
DR   Pfam; PF03446; NAD_binding_2; 1.
DR   PIRSF; PIRSF000103; HIBADH; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00895; 3_HYDROXYISOBUT_DH; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; NAD; NADP; Oxidoreductase; Reference proteome.
FT   CHAIN           1..301
FT                   /note="L-threonate dehydrogenase"
FT                   /id="PRO_0000173063"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250|UniProtKB:Q9I5I6"
FT   BINDING         6..34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P31937"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P31937"
FT   BINDING         245
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P31937"
SQ   SEQUENCE   301 AA;  31035 MW;  7C615A25B0947D18 CRC64;
     MENQNYSVAV IGLGSMGMGA AVSCINAGLT TYGIDLNPVA LEKLKAAGAK AVAANGYDFA
     HELDAVVILV VNAAQANAVL FGENGIAKKL KAGTAVMVSS TMAAQDAQII SQKLTELGLI
     MLDAPVSGGA AKALKGEMTV MASGSKQAFE LLQPVLDATA AKVYNIGEEI GLGATVKIVH
     QLLAGVHIAA GAEAMALASK AGIPLDVMYD VVTNAAGNSW MFENRMKHVV EGDYTPLSMV
     DIFVKDLGLV NDTAKSLHFP LHLASTAYSM FTEASNAGYG KEDDSAVIKI FSGVSLPKKG
     A