(data stored in SCRATCH zone)

SWISSPROT: TDH_XANAC

ID   TDH_XANAC               Reviewed;         340 AA.
AC   Q8PNN2;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   11-DEC-2019, entry version 114.
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=XAC1022;
OS   Xanthomonas axonopodis pv. citri (strain 306).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190486;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=306;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(2002).
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; AE008923; AAM35905.1; -; Genomic_DNA.
DR   RefSeq; WP_011050655.1; NC_003919.1.
DR   SMR; Q8PNN2; -.
DR   STRING; 190486.XAC1022; -.
DR   EnsemblBacteria; AAM35905; AAM35905; XAC1022.
DR   KEGG; xac:XAC1022; -.
DR   eggNOG; ENOG4105CPQ; Bacteria.
DR   eggNOG; COG1063; LUCA.
DR   HOGENOM; HOG000294686; -.
DR   KO; K00060; -.
DR   OMA; ETWYAMS; -.
DR   BioCyc; XAXO190486:XAC_RS05225-MONOMER; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000000576; Chromosome.
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; Q8PNN2.
DR   SWISS-2DPAGE; Q8PNN2.
KW   Cytoplasm; Metal-binding; NAD; Oxidoreductase; Zinc.
FT   CHAIN           1..340
FT                   /note="L-threonine 3-dehydrogenase"
FT                   /id="PRO_0000160870"
FT   NP_BIND         261..263
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00627"
FT   NP_BIND         285..286
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;  37126 MW;  A39E667C146074A2 CRC64;
     MKALVKREAN KGIWLEQVPV PTPGPNEVLI KLEKTAICGT DLHIYLWDEW SQRTIEPGLT
     IGHEFVGRVA ELGSAVTGYQ IGQRVSAEGH IVCGHCRNCR GGRPHLCPNT VGIGVNVNGA
     FAEYMVMPAS NLWPIPDQIP SELAAFFDPY GNAAHCALEF DVIGEDVLIT GAGPIGIIAA
     GICKHIGARN VVVTDVNDFR LKLAADMGAT RVVNVSKTSL KDVMADLHME GFDVGLEMSG
     NSRAFNDMLD CMYHGGKIAM LGIMPRGAGC DWDKIIFKGL TVQGIYGRKM YETWYKMTQL
     VLSGFPLHKV LTHQLPIDDF QKGFDLMEEG KAGKVVLSWN
//

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