(data stored in SCRATCH zone)

SWISSPROT: D3VGV1_XENNA

ID   D3VGV1_XENNA            Unreviewed;       341 AA.
AC   D3VGV1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
DE   RecName: Full=L-threonine 3-dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00368434};
DE            Short=TDH {ECO:0000256|HAMAP-Rule:MF_00627};
DE            EC=1.1.1.103 {ECO:0000256|HAMAP-Rule:MF_00627};
GN   Name=tdh {ECO:0000256|HAMAP-Rule:MF_00627,
GN   ECO:0000313|EMBL:CBJ88236.1};
GN   OrderedLocusNames=XNC1_0148 {ECO:0000313|EMBL:CBJ88236.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88236.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88236.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine
CC       to 2-amino-3-ketobutyrate. {ECO:0000256|HAMAP-Rule:MF_00627,
CC       ECO:0000256|SAAS:SAAS00527196}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + H(+)
CC         + NADH; Xref=Rhea:RHEA:13161, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57926, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:78948; EC=1.1.1.103; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00627, ECO:0000256|SAAS:SAAS01122051};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00627};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00321706}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00627,
CC       ECO:0000256|SAAS:SAAS00367962}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627,
CC       ECO:0000256|SAAS:SAAS00322478}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00627,
CC       ECO:0000256|SAAS:SAAS00571236}.
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DR   EMBL; FN667742; CBJ88236.1; -; Genomic_DNA.
DR   RefSeq; WP_013183117.1; NC_014228.1.
DR   STRING; 406817.XNC1_0148; -.
DR   EnsemblBacteria; CBJ88236; CBJ88236; XNC1_0148.
DR   KEGG; xne:XNC1_0148; -.
DR   eggNOG; ENOG4105CPQ; Bacteria.
DR   eggNOG; COG1063; LUCA.
DR   HOGENOM; HOG000294686; -.
DR   KO; K00060; -.
DR   OMA; MLTIKGI; -.
DR   UniPathway; UPA00046; UER00505.
DR   Proteomes; UP000008075; 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; D3VGV1.
DR   SWISS-2DPAGE; D3VGV1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00627,
KW   ECO:0000256|SAAS:SAAS00321720};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00627,
KW   ECO:0000256|SAAS:SAAS00326561};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00321751};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00627,
KW   ECO:0000256|SAAS:SAAS00326557, ECO:0000313|EMBL:CBJ88236.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00627, ECO:0000256|SAAS:SAAS00326562}.
FT   DOMAIN       12    338       PKS_ER. {ECO:0000259|SMART:SM00829}.
FT   NP_BIND     262    264       NAD. {ECO:0000256|HAMAP-Rule:MF_00627}.
FT   NP_BIND     286    287       NAD. {ECO:0000256|HAMAP-Rule:MF_00627}.
FT   ACT_SITE     40     40       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00627}.
FT   ACT_SITE     43     43       Charge relay system. {ECO:0000256|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        38     38       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        63     63       Zinc 1; via tele nitrogen; catalytic.
FT                                {ECO:0000256|HAMAP-Rule:MF_00627}.
FT   METAL        64     64       Zinc 1; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00627}.
FT   METAL        93     93       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00627}.
FT   METAL        96     96       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00627}.
FT   METAL        99     99       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00627}.
FT   METAL       107    107       Zinc 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00627}.
FT   BINDING     175    175       NAD; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00627}.
FT   BINDING     195    195       NAD. {ECO:0000256|HAMAP-Rule:MF_00627}.
FT   BINDING     200    200       NAD. {ECO:0000256|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:0000256|HAMAP-Rule:
FT                                MF_00627}.
SQ   SEQUENCE   341 AA;  37254 MW;  5EFBB32B61CEB56B CRC64;
     MKALSKLKPE AGIWMTDVPT PELGHNDVMI KIRKTAICGT DVHIYNWDDW SQKTIPVPMV
     IGHEYVGEVV AIGQEVKGFN IGDRVSGEGH ITCGHCRNCR GGRTHLCRNT TGVGVNRAGA
     FAEYLVIPAF NTFKIPDNIP DELAAIFDPF GNAVHTALSF DLVGEDVLVS GAGPIGIMAA
     AVCKHVGARH VVITDVNEYR LELARKIGVT RAVNVSKENL TDVMAELGMT EGFDVGLEMS
     GAPPAFRTLL NTMNHGGRIA LLGIPPSDMA IDWNQVIFKG LFIKGIYGRE MFETWYKMAA
     LIQSGLDLTP IITHQFSIDD YQKGFDIMRS GQSGKVILNW D
//

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