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
//