ID A3SKR9_ROSNI Unreviewed; 411 AA.
AC A3SKR9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=ISM_06635 {ECO:0000313|EMBL:EAP77950.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP77950.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP77950.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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}.
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:EAP77950.1}.
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DR EMBL; AALY01000001; EAP77950.1; -; Genomic_DNA.
DR RefSeq; WP_009813351.1; NZ_CH724156.1.
DR AlphaFoldDB; A3SKR9; -.
DR STRING; 89187.ISM_06635; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OrthoDB; 9811476at2; -.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000005954; 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; 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; 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};
KW Lyase {ECO:0000256|RuleBase:RU362012, ECO:0000313|EMBL:EAP77950.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU362012};
KW Reference proteome {ECO:0000313|Proteomes:UP000005954}.
FT DOMAIN 329..402
FT /note="ACT-like"
FT /evidence="ECO:0000259|PROSITE:PS51672"
SQ SEQUENCE 411 AA; 44650 MW; E62A8799DF5CB40E CRC64;
MSDFIDKARA AERAMREVFP ETPLLRNEHL SERYGANILL KREDLTPVRS YKLRGAFNAM
RKVMARGEAP VFVCASAGNH AQGVAFMCQH FGVRGVIFMP VTTPQQKIGK TAKFGGESVE
IKLIGDYFDD TLAAAQAHCA QIGGHFLPPF DDEDVIEGQA SVAAEIEAQL GGLPDEIVMP
VGGGGLSSGV RSYFGDRVGI TLVEPEGGAC LNAALAAGEP VRLAQVNNFA DGAAVAQIGE
KTFARLRDLD PARSRLVCED RLCTTMIEML NIEGIVLEPA GALSVDVLKD MRDEIAGKTV
VCVTSGGNFD FERLPEVKER AQRHSGVKKY FILRMPQRPG ALKDFLSILG PEDDIARFEY
LKKSARNFGS VLIGIETGHA ENFARIEAAL KAQGFAYRDI TKDEVLAEFL I
//
