LTND_PECAS
ID LTND_PECAS Reviewed; 304 AA.
AC Q6CZ26;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=ECA4327 {ECO:0000312|EMBL:CAG77224.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=SCRI 1043 / ATCC BAA-672;
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=0.13 mM for NAD(+) {ECO:0000269|PubMed:27402745};
CC KM=0.97 mM for NADP(+) {ECO:0000269|PubMed:27402745};
CC Note=kcat is 54 sec(-1) with NAD(+) as cosubstrate. kcat is 4.7 sec(-
CC 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; BX950851; CAG77224.1; -; Genomic_DNA.
DR RefSeq; WP_011095791.1; NC_004547.2.
DR AlphaFoldDB; Q6CZ26; -.
DR SMR; Q6CZ26; -.
DR STRING; 218491.ECA4327; -.
DR EnsemblBacteria; CAG77224; CAG77224; ECA4327.
DR GeneID; 57211020; -.
DR KEGG; eca:ECA4327; -.
DR PATRIC; fig|218491.5.peg.4406; -.
DR eggNOG; COG2084; Bacteria.
DR HOGENOM; CLU_035117_1_2_6; -.
DR OMA; QMFMQAS; -.
DR OrthoDB; 1194694at2; -.
DR BRENDA; 1.1.1.411; 9330.
DR Proteomes; UP000007966; Chromosome.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:UniProt.
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..304
FT /note="L-threonate dehydrogenase"
FT /id="PRO_0000439749"
FT ACT_SITE 178
FT /evidence="ECO:0000250|UniProtKB:Q9I5I6"
FT BINDING 7..35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 102
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
FT BINDING 246
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P31937"
SQ SEQUENCE 304 AA; 31629 MW; 8BF253F3427198FC CRC64;
MKKTSDYAVA VIGLGSMGFG AAASCINAGL TTYGVDINPQ ALEKLRQAGA AQADTRIDAF
ADKLDAVVLL VVNATQVNGI LFGEPQVAAK LKPGTVVMVS STISAQDAKN IEQRLAEHQL
VMLDAPVSGG AAKAAAGDMT VMASGSDLAF EKLKPVLDAV AGKVYRIGEE IGLGATVKII
HQLLAGVHIA AGAEAMALAA RADIPLDIMY DVVTNAAGNS WMFENRMRHV VDGDYTPKSA
VDIFVKDLGL VTDTAKSLHF PLPLASTAFN MFTAASNAGF GKEDDSAVIK IFNGITLPEK
KEAP
