ID   A0A0Q8QGN4_9SPHN        Unreviewed;       415 AA.
AC   A0A0Q8QGN4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:KRB82554.1};
GN   ORFNames=ASE00_10915 {ECO:0000313|EMBL:KRB82554.1};
OS   Sphingomonas sp. Root710.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736594 {ECO:0000313|EMBL:KRB82554.1, ECO:0000313|Proteomes:UP000051854};
RN   [1] {ECO:0000313|EMBL:KRB82554.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB82554.1,
RC   ECO:0000313|Proteomes:UP000051854};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRB82554.1, ECO:0000313|Proteomes:UP000051854}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root710 {ECO:0000313|EMBL:KRB82554.1,
RC   ECO:0000313|Proteomes:UP000051854};
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:KRB82554.1}.
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DR   EMBL; LMIB01000012; KRB82554.1; -; Genomic_DNA.
DR   RefSeq; WP_056380542.1; NZ_LMIB01000012.1.
DR   AlphaFoldDB; A0A0Q8QGN4; -.
DR   STRING; 1736594.ASE00_10915; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000051854; 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: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; 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; PF01842; ACT; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051854}.
FT   DOMAIN          338..415
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   415 AA;  44422 MW;  2EA782694C4AF01E CRC64;
     MASVHKQTGA DGVPVTIDDI RAAHARISPS IVRTPVLKSR TLSEITGANI WLKFENLQFT
     AAYKERGALN KLLLLTDEQR ARGVIAASAG NHAQGLAYHG KRLGIPVTIV MPKMTPTVKV
     QQTEGHGARV ILSGESFDDA YEAARALEAK EGLTFVHPFD DPDVIAGQGT VTLEMLEDAP
     EIDTLVVPIG GGGLISGAAV AARAAGKPMQ VFGVQAELYP SMYAKMKGLM LPCDGDTLAE
     GIAVKQPGVL TAEIVRALVD DIVLVAERDL ETAVSMLLQI EKTVAEGAGA AGLAALLAHP
     QKFRGRNVGV ILCGGNIDTR LLANVLLRDL ARLGRLARLR VRLQDRPGAL FHVARVFDEQ
     QVNIVEVYHQ RVFTTLPAKG LIAEIECETR GAEHLERLLK ALRAEGYDVT PIEAA
//