(data stored in ACNUC7421 zone)

SWISSPROT: TDH_LEGPC

ID   TDH_LEGPC               Reviewed;         340 AA.
AC   A5IGK7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=L-threonine 3-dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00627};
DE            Short=TDH {ECO:0000255|HAMAP-Rule:MF_00627};
DE            EC=1.1.1.103 {ECO:0000255|HAMAP-Rule:MF_00627};
GN   Name=tdh {ECO:0000255|HAMAP-Rule:MF_00627}; OrderedLocusNames=LPC_2592;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-
CC       amino-3-ketobutyrate. {ECO:0000255|HAMAP-Rule:MF_00627}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+) +
CC         NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57926, ChEBI:CHEBI:57945, ChEBI:CHEBI:78948;
CC         EC=1.1.1.103; Evidence={ECO:0000255|HAMAP-Rule:MF_00627};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00627};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00627};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via oxydo-
CC       reductase pathway; glycine from L-threonine: step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_00627}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00627}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00627}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00627}.
DR   EMBL; CP000675; ABQ56507.1; -; Genomic_DNA.
DR   RefSeq; WP_011945851.1; NC_009494.2.
DR   SMR; A5IGK7; -.
DR   EnsemblBacteria; ABQ56507; ABQ56507; LPC_2592.
DR   KEGG; lpc:LPC_2592; -.
DR   HOGENOM; HOG000294686; -.
DR   KO; K00060; -.
DR   OMA; ETWYAMS; -.
DR   BioCyc; LPNE400673:LPC_RS03965-MONOMER; -.
DR   UniPathway; UPA00046; UER00505.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019518; P:L-threonine catabolic process to glycine; IEA:UniProtKB-UniPathway.
DR   HAMAP; MF_00627; Thr_dehydrog; 1.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR004627; L-Threonine_3-DHase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00692; tdh; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5IGK7.
DR   SWISS-2DPAGE; A5IGK7.
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..340
FT                   /note="L-threonine 3-dehydrogenase"
FT                   /id="PRO_1000051643"
FT   NP_BIND         262..264
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   NP_BIND         286..287
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   ACT_SITE        40
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   ACT_SITE        43
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           38
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           63
FT                   /note="Zinc 1; via tele nitrogen; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           64
FT                   /note="Zinc 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           93
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           96
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           99
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   METAL           107
FT                   /note="Zinc 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   BINDING         175
FT                   /note="NAD; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   BINDING         195
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   BINDING         200
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   SITE            148
FT                   /note="Important for catalytic activity for the proton
FT                   relay mechanism but does not participate directly in the
FT                   coordination of zinc atom"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
SQ   SEQUENCE   340 AA;  37196 MW;  6DF5DBD9D98187FF CRC64;
     MKSLVKAKKE PGIWMQDVPV PEYGVNDVLI KIKRTAICGT DIHIYSWDEW AQATIPVPMT
     VGHEFYGEIV EVGKEVQGLK VGQRVSGEGH ITCGFCRNCR AGKRHLCRNT LGVGVNRPGC
     FAEYLALPAT NVIALPDNIT EEQAAILDPF GNAAHCALAF DVVGEDVLIT GAGPIGIMAA
     AIVRHIGARH VVITDVNDHR LELARQMGVS RAVNVKYQKL SDVANELGML EGFDVGLEMS
     GNPMALNDMM KAMNHGGHVA LLGIPPQETP IDWNQVIFKG LVIKGIYGRE MFETWYKMIA
     MLQSGLNISP VITHNFPVDE YQHAFQIMAS GQSGKVILNW
//

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