(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZL26_PSEAB

ID   A0A0H2ZL26_PSEAB        Unreviewed;       504 AA.
AC   A0A0H2ZL26;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=ilvA1 {ECO:0000313|EMBL:ABJ15294.1};
GN   Synonyms=ilvA {ECO:0000256|RuleBase:RU362012};
GN   OrderedLocusNames=PA14_04320 {ECO:0000313|EMBL:ABJ15294.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15294.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15294.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15294.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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: 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; CP000438; ABJ15294.1; -; Genomic_DNA.
DR   EnsemblBacteria; ABJ15294; ABJ15294; PA14_04320.
DR   KEGG; pau:PA14_04320; -.
DR   KO; K01754; -.
DR   OMA; RNHGAAY; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000000653; 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; A0A0H2ZL26.
DR   SWISS-2DPAGE; A0A0H2ZL26.
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:UP000000653};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012}.
FT   DOMAIN      329    401       ACT-like. {ECO:0000259|PROSITE:PS51672}.
FT   DOMAIN      424    495       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   504 AA;  55383 MW;  ECBB784539BC4A7C CRC64;
     MLEQYVKKIL TSRVYDVAVE TPLQPARQLS ERLGNQVLLK REDLQPVFSF KIRGAYNKVA
     QLTEEEKARG VIAASAGNHA QGLALAAKRQ GIRAVIVMPK TTPEIKVQAV RAHGAKAVLH
     GDAFPEALAH ALKLVDEKGY TFVHPYDDPD TIAGQGTVAM EILRQQPGRL DAIFVPVGGG
     GLVAGIAAYV KYLRPEIKVI GVEPDESNCL QAAMAAGERV MLGQVGLFAD GVAVAQIGQH
     TFDICKDHVD EVITVSTDEI CAAIKDIYDD TRSITEPAGA LAVAGIKKYV ERERAEGQTL
     VAIDSGANVN FDRLRHVAER AELGERREAI IAVTIPERPG SFKAFCEAVG KRQITEFNYR
     YHSGSEAHIF VGVQTHPEND PREALVAYLR EKGFPVLDLT DNELAKLHIR HMVGGHAVKV
     SDEMVFRFEF PERPGALFNF LTKLGGRWNI SMFHYRNHGA ADGRVVAGLQ VPEDERHLIP
     QTLEAIGYPY WDETANPAYQ LFLG
//

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