(data stored in ACNUC1104 zone)

SWISSPROT: D3VHW0_XENNA

ID   D3VHW0_XENNA            Unreviewed;       515 AA.
AC   D3VHW0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   16-JAN-2019, entry version 47.
DE   RecName: Full=L-threonine dehydratase {ECO:0000256|RuleBase:RU362012};
DE            EC=4.3.1.19 {ECO:0000256|RuleBase:RU362012};
DE   AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU362012};
GN   Name=ilvA {ECO:0000256|RuleBase:RU362012,
GN   ECO:0000313|EMBL:CBJ88449.1};
GN   OrderedLocusNames=XNC1_0372 {ECO:0000313|EMBL:CBJ88449.1};
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:CBJ88449.1, 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:CBJ88449.1, 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 anaerobic formation of alpha-ketobutyrate
CC       and ammonia from threonine in a two-step reaction. The first step
CC       involved a dehydration of threonine and a production of enamine
CC       intermediates (aminocrotonate), which tautomerizes to its imine
CC       form (iminobutyrate). Both intermediates are unstable and short-
CC       lived. The second step is the nonenzymatic hydrolysis of the
CC       enamine/imine intermediates to form 2-ketobutyrate and free
CC       ammonia. In the low water environment of the cell, the second step
CC       is accelerated by RidA. {ECO:0000256|RuleBase:RU362012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:22108, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|RuleBase:RU362012};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|RuleBase:RU362012}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU362012}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|RuleBase:RU362012}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667742; CBJ88449.1; -; Genomic_DNA.
DR   STRING; 406817.XNC1_0372; -.
DR   EnsemblBacteria; CBJ88449; CBJ88449; XNC1_0372.
DR   KEGG; xne:XNC1_0372; -.
DR   eggNOG; ENOG4105C7B; Bacteria.
DR   eggNOG; COG1171; LUCA.
DR   HOGENOM; HOG000046975; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1020.10; -; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR001721; TD_ACT-like.
DR   InterPro; IPR038110; TD_ACT-like_sf.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 2.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01124; ilvA_2Cterm; 1.
DR   PROSITE; PS51672; ACT_LIKE; 2.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHW0.
DR   SWISS-2DPAGE; D3VHW0.
KW   Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Branched-chain amino acid biosynthesis
KW   {ECO:0000256|RuleBase:RU362012};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:CBJ88449.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075}.
FT   DOMAIN      338    413       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      436    506       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   515 AA;  56493 MW;  91B0A121BEB03844 CRC64;
     MAVYPLNSEP NGAEYLKAAL SAPVYDVAQV TPLQEMKKIS SRLNNTILVK REDRQLVHSF
     KLRGAYAMIA GLTEEQKTKG VITASAGNHA QGVALSASKV GVKATIVMPI ATADIKVDAV
     RSFGGAVLLH GANFDEAKAK AIEMAKEHGY TFVPPFDHPV VIAGQATLAM ELLQQDVHLD
     RIFVPVGGGG LIAGVAVLIK QLVPEMKVIG VEAEDSACLK AALEAGHPVD LPRIGLFAEG
     VAVKRIGDET FRLCQQYVDD VITVDSDAIC AAMKDIFEDV RAIAEPSGAL ALAGLKKYVQ
     QYQIQGERLA HILSGANVNF HGLRYVSERC ELGEQREALL AVTIPEQKGS FLHFCQILGP
     RVVTEFSYRY SDATDPNKAC IFVGIRLSRG NAERREIIEE LNSSGYQVAD FTDDEMAKLH
     VRYMIGGRPS KPLQERLFSF AFPESPGALL KFLQTLGTHW NITLFHYRSH GTDYGRVLAA
     FELAEPEVRF DRHLEVLGYE YHDETDNPSF NLLLK
//

If you have problems or comments...

PBIL Back to PBIL home page