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L-threonine 3-dehydrogenase (TDH) (EC 1.1.1.103)

 TDH_FRATF               Reviewed;         351 AA.
A7NDM9;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
02-OCT-2007, sequence version 1.
22-NOV-2017, entry version 73.
RecName: Full=L-threonine 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00627};
Short=TDH {ECO:0000255|HAMAP-Rule:MF_00627};
EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627};
Name=tdh {ECO:0000255|HAMAP-Rule:MF_00627};
OrderedLocusNames=FTA_1607;
Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA).
Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
Francisellaceae; Francisella.
NCBI_TaxID=458234;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=FTNF002-00 / FTA;
PubMed=19756146; DOI=10.1371/journal.pone.0007041;
Barabote R.D., Xie G., Brettin T.S., Hinrichs S.H., Fey P.D.,
Jay J.J., Engle J.L., Godbole S.D., Noronha J.M., Scheuermann R.H.,
Zhou L.W., Lion C., Dempsey M.P.;
"Complete genome sequence of Francisella tularensis subspecies
holarctica FTNF002-00.";
PLoS ONE 4:E7041-E7041(2009).
-!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine
to 2-amino-3-ketobutyrate. {ECO:0000255|HAMAP-Rule:MF_00627}.
-!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3-
oxobutanoate + NADH. {ECO:0000255|HAMAP-Rule:MF_00627}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00627};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
Rule:MF_00627};
-!- PATHWAY: Amino-acid degradation; L-threonine degradation via
oxydo-reductase pathway; glycine from L-threonine: step 1/2.
{ECO:0000255|HAMAP-Rule:MF_00627}.
-!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00627}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000255|HAMAP-Rule:MF_00627}.
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EMBL; CP000803; ABU62082.1; -; Genomic_DNA.
RefSeq; WP_003016849.1; NC_009749.1.
ProteinModelPortal; A7NDM9; -.
SMR; A7NDM9; -.
EnsemblBacteria; ABU62082; ABU62082; FTA_1607.
KEGG; fta:FTA_1607; -.
HOGENOM; HOG000294686; -.
KO; K00060; -.
OMA; ETWYAMS; -.
UniPathway; UPA00046; UER00505.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
HAMAP; MF_00627; Thr_dehydrog; 1.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR002328; ADH_Zn_CS.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR004627; L-Threonine_3-DHase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR00692; tdh; 1.
PROSITE; PS00059; ADH_ZINC; 1.
3: Inferred from homology;
Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
CHAIN 1 351 L-threonine 3-dehydrogenase.
/FTId=PRO_1000051637.
NP_BIND 271 273 NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
NP_BIND 295 296 NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
ACT_SITE 41 41 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_00627}.
ACT_SITE 44 44 Charge relay system. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 39 39 Zinc 1; catalytic. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 64 64 Zinc 1; via tele nitrogen; catalytic.
{ECO:0000255|HAMAP-Rule:MF_00627}.
METAL 65 65 Zinc 1; catalytic. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 94 94 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 97 97 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 100 100 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00627}.
METAL 108 108 Zinc 2. {ECO:0000255|HAMAP-
Rule:MF_00627}.
BINDING 176 176 NAD; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00627}.
BINDING 196 196 NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
BINDING 201 201 NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
SITE 149 149 Important for catalytic activity for the
proton relay mechanism but does not
participate directly in the coordination
of zinc atom. {ECO:0000255|HAMAP-
Rule:MF_00627}.
SEQUENCE 351 AA; 38400 MW; 1E07E9CCC5A58A79 CRC64;
MKALAKLKKQ PGIWMINDAP IPEYGYNDVL IKIKKTAICG TDLHIYNWDK WSQNTIPVPM
ITGHEFAGEV VAKGDGVTSV DIGDRVSGEG HLVCGQCRNC RAGKRHLCRK TIGIGVNVQG
AFAEYLVMPA VNVFKIPDSI SDDIASTFDP MGNAIHTALS FNLTGEDVLI TGAGPIGLMA
VKIARFCGAR RIVITDINEY RLQMARDFGA TVALNVAPFK NQDELVKQMR KVMSDIGMTE
GFDVGLEMSG INSAISMMLD VMNHGGKLSL LGISAGDISV DWGAILFKGL TLKGIYGREM
FETWYLMTSM LQAGMDMNPI ITHRLHIDEF QKGFEIMKSG QCGKVILDWS S


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