(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NUT7_YERPA

ID   A0A0E1NUT7_YERPA        Unreviewed;       514 AA.
AC   A0A0E1NUT7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   05-DEC-2018, entry version 21.
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   OrderedLocusNames=YPA_0125 {ECO:0000313|EMBL:ABG12094.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12094.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12094.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12094.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG12094.1; -; Genomic_DNA.
DR   RefSeq; WP_002212013.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12094; ABG12094; YPA_0125.
DR   EnsemblBacteria; AJJ80719; AJJ80719; CH58_2967.
DR   KEGG; ypa:YPA_0125; -.
DR   PATRIC; fig|360102.15.peg.3116; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001971; 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; A0A0E1NUT7.
DR   SWISS-2DPAGE; A0A0E1NUT7.
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:UP000001971};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:ABG12094.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012}.
SQ   SEQUENCE   514 AA;  55935 MW;  A49EA796A2CE6640 CRC64;
     MAVSQPLSAA PCGAEYLRAI LRAPVYEVAQ VTPLQVMEKI SSRVGNTVLV KREDRQPVHS
     FKLRGAYAMI SSLTEEQKAC GVVTASAGNH AQGVALSAHK MGIKALIVMP VATADIKVDA
     VRAFGGEVLL FGANFDEAKT KAIALAQEQG YTFVPPFDHP AVIAGQGTLA MELLQQDAHL
     DRVFVPVGGG GLVAGVAVLI KQLMPQIKVI GVEAEDSACL RAALDAGQPV DLARVGLFAE
     GVAVKRIGDE PFRLCQEYLD DVITVDSDAI CAAVKDLFED VRAIAEPSGA LALAGLKKYV
     QQHNIQGERL AHVLSGANVN FHGLRYVSER CELGEQREAL LAVTIPEQKG SFLRFCELLG
     GRSVTEFNYR YADAENACIF VGVRLTRGYA ERVEILAELQ DKGYQVVDLS DDEMAKLHVR
     YMVGGRPSKP LRERLFSFEF PESPGALLKF LHTLGTHWNI SLFHYRSHGT DFGRVLAAFE
     LSATEPQFEE RLAALGYYCH DETDNPAFKF FLAG
//

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