(data stored in ACNUC7421 zone)

SWISSPROT: TDH_SHESH

ID   TDH_SHESH               Reviewed;         341 AA.
AC   A8FPE0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 73.
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=Ssed_0100;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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; CP000821; ABV34713.1; -; Genomic_DNA.
DR   RefSeq; WP_012004239.1; NC_009831.1.
DR   ProteinModelPortal; A8FPE0; -.
DR   SMR; A8FPE0; -.
DR   STRING; 425104.Ssed_0100; -.
DR   EnsemblBacteria; ABV34713; ABV34713; Ssed_0100.
DR   KEGG; sse:Ssed_0100; -.
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; UP000002015; 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; A8FPE0.
DR   SWISS-2DPAGE; A8FPE0.
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Zinc.
FT   CHAIN         1    341       L-threonine 3-dehydrogenase.
FT                                /FTId=PRO_1000082618.
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;  37266 MW;  E45E4D77D30DA450 CRC64;
     MKALSKLKPE EGIWMVDAPK PEMGHNDLLI KIRKTAICGT DIHIYNWDEW SQKTIPVPMV
     VGHEYVGEVI DMGIEVRGFD VGDRVSGEGH ITCGHCRNCR GGRTHLCRNT SGVGVNRDGA
     FAEYLVIPAF NAFKIPDDIS DDLASIFDPF GNAVHTALSF DLVGEDVLIT GAGPIGIMAA
     AVCRHVGARH VVITDVNEYR LELANKMGAT RAVNVAKESL EGVMEELGMT EGFDVGLEMS
     GVPSAFHSML DTMNHGGKIA MLGIPGGEMA IDWSKVIFKG LILKGIYGRE MFETWYKMAS
     LIQSGLDISP IITHHFKIDD FQQGFDAMRS GQSGKVILNW D
//

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