(data stored in SCRATCH zone)

SWISSPROT: C5BBA6_EDWI9

ID   C5BBA6_EDWI9            Unreviewed;       514 AA.
AC   C5BBA6;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 52.
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=NT01EI_0081 {ECO:0000313|EMBL:ACR67341.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67341.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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: L-threonine = 2-oxobutanoate + NH(3).
CC       {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; CP001600; ACR67341.1; -; Genomic_DNA.
DR   RefSeq; WP_015869562.1; NC_012779.2.
DR   STRING; 634503.NT01EI_0081; -.
DR   EnsemblBacteria; ACR67341; ACR67341; NT01EI_0081.
DR   GeneID; 7959800; -.
DR   KEGG; eic:NT01EI_0081; -.
DR   PATRIC; fig|634503.3.peg.74; -.
DR   eggNOG; ENOG4105C7B; Bacteria.
DR   eggNOG; COG1171; LUCA.
DR   HOGENOM; HOG000046975; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   OrthoDB; POG091H01W2; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001485; 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   InterPro; IPR001721; ACT-like_dom.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR005787; Thr_deHydtase_biosynth.
DR   InterPro; IPR001926; TrpB-like_PLP-dep.
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; C5BBA6.
DR   SWISS-2DPAGE; C5BBA6.
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:UP000001485};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:ACR67341.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN      339    411       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      434    504       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   514 AA;  55878 MW;  17BD75BC49AF7999 CRC64;
     MTSNPFISSA PDGAEYLRAV LRSPVYEVAQ VTPLQMMEKL SGRLGNHILV KREDRQPVHS
     FKLRGAYAMI AGLNETQRAC GVITASAGNH AQGVALSASR LGIAATIVMP RATAEIKVEA
     VRGFGGRVLL YGANFDEAKA HAIQMAQETG MTFIPPFDHP AVIAGQGTLA LELLQQDAHL
     DRIFVPVGGG GLAAGVAVLI KQLMPQIKVI GVEAEDSACL RAALDAGRPV DLPRVGLFAE
     GVAVKRIGDE TFRLCQRYLD DVITVDSDAI CAAVKDLFED VRAVAEPSGA LALAGLKQYV
     QRHALRGERL AHVLSGANLN FHGLRYVSER CELGEQREAL LAVTIPERKG SFLTFCQLLG
     GRSVTEFNYR YADADSACIF VGVRLTGGRG EREEIIASLR GGGYQVVDLS DDEMAKLHVR
     YMVGGRPSKP LQERLYSFEF PEAPGALLKF LHTLGTHWNI SLFHYRSHGT DFGRVLAAFE
     RPDSDASFEA RLKELGYECH DETGNPAFRF FLQG
//

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