(data stored in ACNUC7421 zone)

SWISSPROT: TDH_EDWI9

ID   TDH_EDWI9               Reviewed;         341 AA.
AC   C5BB99;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 60.
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};
GN   OrderedLocusNames=NT01EI_0074;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine
CC       to 2-amino-3-ketobutyrate. {ECO:0000255|HAMAP-Rule:MF_00627}.
CC   -!- CATALYTIC ACTIVITY: L-threonine + NAD(+) = L-2-amino-3-
CC       oxobutanoate + NADH. {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
CC       oxydo-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; CP001600; ACR67334.1; -; Genomic_DNA.
DR   RefSeq; WP_015869555.1; NC_012779.2.
DR   ProteinModelPortal; C5BB99; -.
DR   SMR; C5BB99; -.
DR   STRING; 634503.NT01EI_0074; -.
DR   EnsemblBacteria; ACR67334; ACR67334; NT01EI_0074.
DR   GeneID; 7959793; -.
DR   KEGG; eic:NT01EI_0074; -.
DR   PATRIC; fig|634503.3.peg.67; -.
DR   eggNOG; ENOG4105CPQ; Bacteria.
DR   eggNOG; COG1063; LUCA.
DR   HOGENOM; HOG000294686; -.
DR   KO; K00060; -.
DR   OMA; ETWYAMS; -.
DR   OrthoDB; POG091H03K6; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008743; F:L-threonine 3-dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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.
DR   InterPro; IPR004627; L-Threonine_3-DHase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
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; C5BB99.
DR   SWISS-2DPAGE; C5BB99.
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN         1    341       L-threonine 3-dehydrogenase.
FT                                /FTId=PRO_1000212312.
FT   NP_BIND     262    264       NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   NP_BIND     286    287       NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   ACT_SITE     40     40       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   ACT_SITE     43     43       Charge relay system. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        38     38       Zinc 1; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        63     63       Zinc 1; via tele nitrogen; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   METAL        64     64       Zinc 1; catalytic. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        93     93       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        96     96       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        99     99       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL       107    107       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
FT   BINDING     175    175       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   BINDING     195    195       NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   BINDING     200    200       NAD. {ECO:0000255|HAMAP-Rule:MF_00627}.
FT   SITE        148    148       Important for catalytic activity for the
FT                                proton relay mechanism but does not
FT                                participate directly in the coordination
FT                                of zinc atom. {ECO:0000255|HAMAP-
FT                                Rule:MF_00627}.
SQ   SEQUENCE   341 AA;  37138 MW;  2A607758C440C24B CRC64;
     MKALSKLKAE EGIWMTDVPL PALGHNDIMI KIRKAAICGT DVHIYNWDTW SQKTIPVPMV
     VGHEYVGEVV AVGQEVRGFR IGDRVSGEGH ITCGHCRNCR AGRTHLCRNT IGVGVNRQGA
     FAEYLVIPAF NAFKIPDNIP DALAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA
     AVCRHVGARH VVITDVNDYR LDLARKMGVT RAVNVSRESL PEVMQALGMS EGFDVGLEMS
     GAPPAFHTML DTMNHGGKIA MLGIPPGDMA IDWNQVIFKG LLIKGIYGRE MFETWYKMAA
     LIQSGLDLTP IITHQYAIDD FQKGFDVMRS GHSGKVILNW S
//

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