ID A0A0Q7T8R4_9CAUL Unreviewed; 402 AA.
AC A0A0Q7T8R4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:KQY93240.1};
GN ORFNames=ASD21_10740 {ECO:0000313|EMBL:KQY93240.1};
OS Caulobacter sp. Root1455.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736465 {ECO:0000313|EMBL:KQY93240.1, ECO:0000313|Proteomes:UP000051447};
RN [1] {ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|Proteomes:UP000051447};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQY93240.1, ECO:0000313|Proteomes:UP000051447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1455 {ECO:0000313|EMBL:KQY93240.1,
RC ECO:0000313|Proteomes:UP000051447};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KQY93240.1}.
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DR EMBL; LMFQ01000023; KQY93240.1; -; Genomic_DNA.
DR RefSeq; WP_056443418.1; NZ_LMFQ01000023.1.
DR AlphaFoldDB; A0A0Q7T8R4; -.
DR Proteomes; UP000051447; Unassembled WGS sequence.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR CDD; cd04886; ACT_ThrD-II-like; 1.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR044561; ACT_ThrD-II-like.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR01127; ilvA_1Cterm; 1.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51671; ACT; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 328..402
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 402 AA; 43131 MW; 4CC29FC03FE0B337 CRC64;
MSRTLDIDSI RAAAARLAGQ IERTPCRYSR TLSKITGAEV WVKFENLQFT AAYKERGALN
KLMLLSNSEK ARGVIAASAG NHAQGLAYHG ARLGVPVTIV MPKTTPFIKV QHTRDFGATV
VIEGETYDDA STHARKLQVE QDLTFVHPFD DYDIMAGQGT IALEMLEDAP DLEVLPVPIG
GGGLISGVAT AAKAVKPDIR IIGCEPAMYP SFTAKMRGVA AHCGGQTIAE GVAVKQVGEL
TYGVARPLID DVLLLEEPHI EQAVALYCNV EKTIAEGAGA ASLAALLAYP ERFRGKKCGL
ILCGGNIDTR LLASVLTREL VRAQRLVSLR IVGDDRPGLL STVANVIGTM GANIIEVNHN
RLALDVPAKG AEFDITIETR DAQHTQEVMD ALREKGYPPR TV
//