ID A0A0Q4C8Z8_9SPHN Unreviewed; 419 AA.
AC A0A0Q4C8Z8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:KQM22120.1};
GN ORFNames=ASE49_02100 {ECO:0000313|EMBL:KQM22120.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM22120.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM22120.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM22120.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM22120.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM22120.1,
RC ECO:0000313|Proteomes:UP000050893};
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:KQM22120.1}.
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DR EMBL; LMJY01000001; KQM22120.1; -; Genomic_DNA.
DR RefSeq; WP_056768264.1; NZ_LMJY01000001.1.
DR AlphaFoldDB; A0A0Q4C8Z8; -.
DR STRING; 1735670.ASE49_02100; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000050893; 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; PF01842; ACT; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050893}.
FT DOMAIN 342..419
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 419 AA; 44684 MW; 67A6A8BC6FFB4D1D CRC64;
MDQTLLNTDT GTAAGDAPLT AADVRAAAQR IAGNVVRTPT LYSATLSAIT GADIWLKFEN
LQFTAAYKER GALNALLQLP EERKARGVIA ASAGNHAQGL SYHGTRLGVP VTIVMPKTTP
TVKIMQTESV GGKVVLEGES FDEASAHALK LQVERGLTYV HPFDDPHVAA GQGTVALEML
EDVPQIDTLV LPVGGGGLSS GMGTIARDIN PDIRLIAVEA QLYPSMYNLL KGTNLPIGGD
TLAEGIAVIA PGQMTSKVLR PLLDEFLLVS EPQIESALAL LLQIEKTLVE GAGATGLAAV
LANRELFVGR KVGLVLCGGN IDTRLLANVL LRDLARSGRL ARLRIGLQDR AGALFKVAKV
FHEHNVNIIE VFHQRIFTHL PAKGLVTEIE CEARDRAQLQ ALVAGLRREG YEVKLVETE
//
