ID A0A0B7HZQ3_9FLAO Unreviewed; 419 AA.
AC A0A0B7HZQ3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-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 ECO:0000313|EMBL:CEN44900.1};
GN ORFNames=CCAND38_200027 {ECO:0000313|EMBL:CEN44900.1}, CKY20_03905
GN {ECO:0000313|EMBL:RIY37243.1};
OS Capnocytophaga canis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN44900.1, ECO:0000313|Proteomes:UP000045051};
RN [1] {ECO:0000313|EMBL:CEN44900.1, ECO:0000313|Proteomes:UP000045051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CcD38 {ECO:0000313|EMBL:CEN44900.1,
RC ECO:0000313|Proteomes:UP000045051};
RA MANFREDI Pablo;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RIY37243.1, ECO:0000313|Proteomes:UP000265497}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-158 {ECO:0000313|EMBL:RIY37243.1,
RC ECO:0000313|Proteomes:UP000265497};
RA Gulvik C.A.;
RT "Capnocytophaga canis 17-158 assembly.";
RL Submitted (AUG-2017) 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|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; CDOI01000113; CEN44900.1; -; Genomic_DNA.
DR EMBL; NSDI01000003; RIY37243.1; -; Genomic_DNA.
DR RefSeq; WP_013996708.1; NZ_NSDI01000003.1.
DR AlphaFoldDB; A0A0B7HZQ3; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000045051; Unassembled WGS sequence.
DR Proteomes; UP000265497; 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};
KW Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:CEN44900.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012};
KW Reference proteome {ECO:0000313|Proteomes:UP000045051}.
FT DOMAIN 336..410
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 419 AA; 46389 MW; 9FE43FCD7C812555 CRC64;
MEVTTYIPQV QEVQKAMLRI KSVINTTPLS KSVRLSNLFG AEIYFKREDL QQVRSYKIRG
AYNKISSLSE QDKQQGIVCA SAGNHAQGVA LSCQILNIKG DIYMPVTTPQ QKIEQVQMFG
GENVTIVLEG DTFDDSNNAA IKFATENAKT FVPPFDDEKV IEGQATIGLE ILDQANEPID
YVFVPIGGGG LSAGLSSVFK TLSPQTKIIG VEPLGAPSMK EALKAGKPVE LTEIDKFVDG
ASVKKVGSLN FEICNRFLDD VVLVPEGKVC QTILDLYNRD AIVVEPAGAL SISALDFYKE
KIKGKKVVCV ISGSNNDITR TAEIKERALL YANLKHYFIV RFPQRAGALK EFVVEILGKT
DDITYFEYSK KHNRENGPAV VGIELKNEAD LQPLIDRMKQ RNFYGDYLNN KPDLFQFLV
//
