(data stored in ACNUC7421 zone)

SWISSPROT: Q145P4_PARXL

ID   Q145P4_PARXL            Unreviewed;       535 AA.
AC   Q145P4;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 83.
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   ORFNames=Bxe_A4054 {ECO:0000313|EMBL:ABE28945.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE28945.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE28945.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE28945.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., 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 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}.
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DR   EMBL; CP000270; ABE28945.1; -; Genomic_DNA.
DR   STRING; 266265.Bxe_A4054; -.
DR   EnsemblBacteria; ABE28945; ABE28945; Bxe_A4054.
DR   KEGG; bxe:Bxe_A4054; -.
DR   eggNOG; ENOG4105C7B; Bacteria.
DR   eggNOG; COG1171; LUCA.
DR   HOGENOM; HOG000046975; -.
DR   KO; K01754; -.
DR   OMA; KHICDSH; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001817; Chromosome 1.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-UniRule.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; Q145P4.
DR   SWISS-2DPAGE; Q145P4.
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:UP000001817};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:ABE28945.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817}.
FT   DOMAIN      361    432       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      455    526       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   535 AA;  58704 MW;  51EBADC974301B3C CRC64;
     MHKPKALAHT VGAIIDPFRS HTALRATRMA SHDYLKKTLT ARVYDVARET ELERAPNLSA
     RLRNPVYLKR EDNQPVFSFK VRGAYNKMAH IPAEALERGV ITASAGNHAQ GVALSAARMG
     VKAIIVVPVT TPQVKVDAVR AHGGPTVEVV QFGESYSDAY GHAVKLQEER DLTFVHPFDD
     PYVIAGQGTV AMEILSQHQG PIHAIFVPIG GGGLAAGVAA YVKSVRPEIK VIGVQTDDSC
     AMAASLKAGE RVTLNEVGLF SDGTAVKLVG EETFRLCREY LDDVLLVDTD ALCAAIKDVF
     QDTRSVLEPA GSLAVAGAKQ YAEREGIENQ TLIAITSGAN MNFDRMRFVA ERAEVGEARE
     AVFAVTIPEE RGSFRRFCEL VGTRSVTEFN YRIADANSAH IFVGVQIRNR SESAQIAGAF
     EAHGFATVDL TFDELSKQHI RYMVGGRSPL AHDERLFRFE FPERPGALMK FLSSMAPNWN
     ISLFHYRNQG ADYSSILVGI QVPESEDAAF DQFLATLGYP NWEETRNPVY RLFLA
//

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