(data stored in ACNUC7421 zone)

SWISSPROT: TDH_PARXL

ID   TDH_PARXL               Reviewed;         343 AA.
AC   Q13SG2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 86.
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=Bxeno_B0009; ORFNames=Bxe_B3020;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000271; ABE32977.1; -; Genomic_DNA.
DR   RefSeq; WP_011490366.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13SG2; -.
DR   SMR; Q13SG2; -.
DR   STRING; 266265.Bxe_B3020; -.
DR   EnsemblBacteria; ABE32977; ABE32977; Bxe_B3020.
DR   GeneID; 4006478; -.
DR   KEGG; bxb:DR64_5349; -.
DR   KEGG; bxe:Bxe_B3020; -.
DR   PATRIC; fig|266265.5.peg.4669; -.
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; UP000001817; Chromosome 2.
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; Q13SG2.
DR   SWISS-2DPAGE; Q13SG2.
KW   Complete proteome; Cytoplasm; Metal-binding; NAD; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN         1    343       L-threonine 3-dehydrogenase.
FT                                /FTId=PRO_1000051629.
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   343 AA;  37476 MW;  62615F4EB03D877A CRC64;
     MKALAKLERA PGLTLTDVKK PEVGHNDVMI RITRTAICGT DIHIWKWDDW AQKTIPVPMH
     VGHEYVGEIV EMGQEVRGFA IGDRVSGEGH ITCGFCRNCR AGRRHLCRNT VGVGVNREGA
     FAEYLVIPAF NAFKIPPEIS DDLAAIFDPF GNATHTALSF NLVGEDVLIT GAGPIGIMAV
     AIAKHVGARN VVITDVNDYR LELARKMGAT RAVNVSRESL RDVMADLHMA EGFDVGLEMS
     GVPSAFTGML EAMNHGGKIA LLGIPPAQTA IDWTQVIFKG LEIKGIYGRE MFETWYKMVA
     MLQSGLDLSP ILTHHFKVDD YREAFATMLS GESGKVILDW TAA
//

If you have problems or comments...

PBIL Back to PBIL home page