ID I2GS63_9BACT Unreviewed; 423 AA.
AC I2GS63;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=BN8_06127 {ECO:0000313|EMBL:CCH56741.1};
OS Fibrisoma limi BUZ 3.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Fibrisoma.
OX NCBI_TaxID=1185876 {ECO:0000313|EMBL:CCH56741.1, ECO:0000313|Proteomes:UP000009309};
RN [1] {ECO:0000313|EMBL:CCH56741.1, ECO:0000313|Proteomes:UP000009309}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BUZ 3T {ECO:0000313|Proteomes:UP000009309};
RX PubMed=22843583; DOI=10.1128/jb.00869-12;
RA Filippini M., Qi W., Jaenicke S., Goesmann A., Smits T.H., Bagheri H.C.;
RT "Genome Sequence of the Filamentous Bacterium Fibrisoma limi BUZ 3T.";
RL J. Bacteriol. 194:4445-4445(2012).
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}.
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:CCH56741.1}.
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DR EMBL; CAIT01000009; CCH56741.1; -; Genomic_DNA.
DR AlphaFoldDB; I2GS63; -.
DR STRING; 1185876.BN8_06127; -.
DR eggNOG; COG1171; Bacteria.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000009309; 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; cd04907; ACT_ThrD-I_2; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR011820; IlvA.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001721; TD_ACT-like.
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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009309}.
FT DOMAIN 340..414
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 423 AA; 47044 MW; BE0D700CE81F3E52 CRC64;
MVVEAEKKIT FPDLDNIYLA AERLRGVATH TPLQENMNLS DRYQANIFLK REDLQVVRSY
KIRGAYNKMA SLPQEALAKG VVCASAGNHA QGLAYACRKM GVKGRIFMPT TTPAQKVKQV
RMFGKEFVEV VLTGDTYDDA YHAAIEYVNT HDSTFVHPFD DVQVMEGQGT VGLEIFKDSN
FKIDYLLMAI GGGGLASGVS TVFRQLSPKT KLIGVEPLGS PSMKVSIDEG HVVALDEIDK
FVDGAAVKRV GDMTFEVCRQ NLDRVVLVPE GKVCTTILQL YNEEAIVAEP AGALTIAALD
FLKDEIKGKN VVCLVGGGNN DITRTEEIKE RSLLYEGLKH YFIIRFAQRA GAMREFLSDV
LGPNDDITLF EYSKKTNRER GPALVGIELK SKADFEPLLI RMQDARIHFE YLNDKPDLFE
FLI
//
