ID A0A166UYV0_9GAMM Unreviewed; 513 AA.
AC A0A166UYV0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
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 ORFNames=N475_23595 {ECO:0000313|EMBL:KZN31528.1};
OS Pseudoalteromonas luteoviolacea DSM 6061.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1365250 {ECO:0000313|EMBL:KZN31528.1, ECO:0000313|Proteomes:UP000076643};
RN [1] {ECO:0000313|EMBL:KZN31528.1, ECO:0000313|Proteomes:UP000076643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6061 {ECO:0000313|EMBL:KZN31528.1,
RC ECO:0000313|Proteomes:UP000076643};
RA Vynne N.G., Mansson M., Gram L.;
RT "Comparative Genomic and Metabolomic Analysis of Twelve Strains of
RT Pseudoalteromonas luteoviolacea.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU362012}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000256|ARBA:ARBA00010869, ECO:0000256|RuleBase:RU362012}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KZN31528.1}.
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DR EMBL; AUYB01000140; KZN31528.1; -; Genomic_DNA.
DR RefSeq; WP_063365985.1; NZ_AUYB01000140.1.
DR AlphaFoldDB; A0A166UYV0; -.
DR STRING; 43657.S4054249_01475; -.
DR PATRIC; fig|1365250.3.peg.4677; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000076643; Unassembled WGS sequence.
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; cd04906; ACT_ThrD-I_1; 1.
DR CDD; cd04907; ACT_ThrD-I_2; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
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; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01124; ilvA_2Cterm; 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; 2.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51672; ACT_LIKE; 2.
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};
KW Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:KZN31528.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012};
KW Reference proteome {ECO:0000313|Proteomes:UP000076643};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 328..400
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
FT DOMAIN 423..494
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 513 AA; 56201 MW; 570E674B30491D98 CRC64;
MVAQELDYFR AIIQANMAPL VRQTEVSSLT GLSKKLANQI WLKREDQQPV YSFKLRGAFN
KLRKLPMHSH VVTASAGNHA QGVALSAAHL GHKATIVMPV TTPEIKVNAV RNLGGNVVLH
GHHFDAANSY AQALCERESG VFVPPFDDKD VIVGQGTVAR EMMQQLDKLD AVFVPVGGGG
LLAGMAVYIK SLRPDIRVIG VEATESACLQ AAMEKGQPVE LEQVGSFADG IAVKKIGEET
FRLAQTYCDE VVVVSTDEIC AAVQDIFVET RAIAEPSGAV ALAGLKKWCE LHKSQGLSLA
AVLSGANLNF DRLRYIAERT ALGAKSEALF GVTIDEQKGS FKQFCQTLGG RAITEFNYRY
AGGREAQIFV GVGLRGGEAE LQELQANLAD NGYAFTDLSD NELAKLHIRY MVGGKPPVSL
EERLLRFEFP EYPGALLRFL ETLGSEWNIT LFHYRNHGAA KGQVLAGFQL GPQECPKFEE
HLERLGYSYQ DETNNPCFSQ YLQSNEEYTR KVG
//
