ID B5ZZC2_RHILW Unreviewed; 416 AA.
AC B5ZZC2;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 98.
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=Rleg2_1421 {ECO:0000313|EMBL:ACI54715.1};
OS Rhizobium leguminosarum bv. trifolii (strain WSM2304).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=395492 {ECO:0000313|EMBL:ACI54715.1, ECO:0000313|Proteomes:UP000008330};
RN [1] {ECO:0000313|EMBL:ACI54715.1, ECO:0000313|Proteomes:UP000008330}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM2304 {ECO:0000313|EMBL:ACI54715.1,
RC ECO:0000313|Proteomes:UP000008330};
RX PubMed=21304679; DOI=10.4056/sigs.44642;
RA Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K., Tiwari R.,
RA Malfatti S., Kiss H., Lapidus A., Copeland A., Nolan M., Land M.,
RA Ivanova N., Mavromatis K., Markowitz V., Kyrpides N., Melino V., Denton M.,
RA Yates R., Howieson J.;
RT "Complete genome sequence of Rhizobium leguminosarum bv trifolii strain
RT WSM2304, an effective microsymbiont of the South American clover Trifolium
RT polymorphum.";
RL Stand. Genomic Sci. 2:66-76(2010).
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC ammonia from threonine in a two-step reaction. The first step involved
CC a dehydration of threonine and a production of enamine intermediates
CC (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC Both intermediates are unstable and short-lived. The second step is the
CC nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC ketobutyrate and free ammonia. In the low water environment of the
CC cell, the second step is accelerated by RidA.
CC {ECO:0000256|ARBA:ARBA00025527, ECO:0000256|RuleBase:RU362012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC Evidence={ECO:0000256|ARBA:ARBA00001274,
CC ECO:0000256|RuleBase:RU362012};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU362012};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC oxobutanoate from L-threonine: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004810, ECO:0000256|RuleBase:RU362012}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881,
CC ECO:0000256|RuleBase:RU362012}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
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DR EMBL; CP001191; ACI54715.1; -; Genomic_DNA.
DR RefSeq; WP_012557427.1; NC_011369.1.
DR AlphaFoldDB; B5ZZC2; -.
DR STRING; 395492.Rleg2_1421; -.
DR KEGG; rlt:Rleg2_1421; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_5; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000008330; 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 CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR011820; IlvA.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
DR InterPro; IPR038110; TD_ACT-like_sf.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR02079; THD1; 1.
DR PANTHER; PTHR48078:SF11; THREONINE DEHYDRATASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF00585; Thr_dehydrat_C; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51672; ACT_LIKE; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU362012};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|RuleBase:RU362012};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624,
KW ECO:0000256|RuleBase:RU362012}; Lyase {ECO:0000256|RuleBase:RU362012};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012}.
FT DOMAIN 334..407
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 416 AA; 44915 MW; 9729D194F405B3CD CRC64;
MTRLDVESAE EAMRSLFPAT PLQLNDHLSA RYGADIWLKR EDLSPVRSYK IRGAFNFFRK
AIGQGASGKT FVCASAGNHA QGFAFVCRHF GVPGVVFMPV TTPQQKIDKT RMFGAEFITI
GLFGDFFDQC YQAARDHVEA VGGVMVPPFD HADIIEGQAT VAAEIMQQLP EGTVPDMVVL
PVGGGGLAAG ITGYLDGKVP KSAFVFTEPA GAPSLRRSIE AGKVTTLAKV DNFVDGAAVA
RIGDLNFAAL RDFPASQVQL MPENAICVTI QEMLNVEGVV LEPAGALSLT AIAAMDAQAI
RGKTIVAIVS GGNFDFERLP DVKERAMRYA GLKKYFILRL AQRPGALRDF LNLLGPDDDI
ARFEYLKKSA RNFGSILIGI ETKAPENFAR LIGNFEAAGM GYEDITENEI LANLII
//
