(data stored in SCRATCH zone)

SWISSPROT: Q5LWG1_RUEPO

ID   Q5LWG1_RUEPO            Unreviewed;       408 AA.
AC   Q5LWG1;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 94.
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:AAV93351.1};
GN   OrderedLocusNames=SPO0020 {ECO:0000313|EMBL:AAV93351.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93351.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93351.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93351.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93351.1; -; Genomic_DNA.
DR   RefSeq; WP_011045792.1; NC_003911.12.
DR   STRING; 246200.SPO0020; -.
DR   EnsemblBacteria; AAV93351; AAV93351; SPO0020.
DR   KEGG; sil:SPO0020; -.
DR   eggNOG; ENOG4105C7B; Bacteria.
DR   eggNOG; COG1171; LUCA.
DR   HOGENOM; HOG000046973; -.
DR   KO; K01754; -.
DR   OMA; AEQGCEH; -.
DR   OrthoDB; 1876944at2; -.
DR   BioCyc; RPOM246200:G1G48-20-MONOMER; -.
DR   UniPathway; UPA00047; UER00054.
DR   Proteomes; UP000001023; 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; IPR011820; IlvA.
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; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF00585; Thr_dehydrat_C; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR02079; THD1; 1.
DR   PROSITE; PS51672; ACT_LIKE; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LWG1.
DR   SWISS-2DPAGE; Q5LWG1.
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:UP000001023};
KW   Isoleucine biosynthesis {ECO:0000256|RuleBase:RU362012};
KW   Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:AAV93351.1};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU362012};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023}.
FT   DOMAIN      326    399       ACT-like. {ECO:0000259|PROSITE:PS51672}.
SQ   SEQUENCE   408 AA;  44902 MW;  9A4C9B50E2AD6BA8 CRC64;
     MSDFMTRARA AEQAMREVFP ATPLQRNDHL SARYGADIWL KREDLSPVRS YKIRGAFNAM
     RKQPGQGLFV CASAGNHAQG VAFMCRHMGV RGVIFMPVTT PQQKIQKTRM FGGDQVEIHL
     TGDYFDQTLA AAQAWCAQEG GHFLSPFDDA DVIEGQASLA VEIEEQLGGV PDHVVLPVGG
     GGMSAGVATW FGDRSHCIFV EPEGGACLRA ALAAGHPVKL DHVDNFVDGA AVGRIGEKTF
     ELLKSRHMSD VLVMPEDRIC TTIIEMLNVE GIVLEPAGAL SVEAVADVQS FVRGKTVVCV
     TSGGNFDFER LPEVKERAQR YLGVKKYFLL RLPQRPGALK EFLNILGPDD DIARFEYMKK
     SARNFGSVLI GIETARPENF ERLYARLDEA GFTYTDITRN ETLAQFVI
//

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