ID V9VYI7_9RHOB Unreviewed; 306 AA.
AC V9VYI7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:AHD02779.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:AHD02779.1};
GN ORFNames=METH_20950 {ECO:0000313|EMBL:AHD02779.1};
OS Leisingera methylohalidivorans DSM 14336.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=999552 {ECO:0000313|EMBL:AHD02779.1, ECO:0000313|Proteomes:UP000018780};
RN [1] {ECO:0000313|EMBL:AHD02779.1, ECO:0000313|Proteomes:UP000018780}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14336 {ECO:0000313|EMBL:AHD02779.1,
RC ECO:0000313|Proteomes:UP000018780};
RG DOE Joint Genome Institute;
RA Klenk H.-P., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP006773; AHD02779.1; -; Genomic_DNA.
DR RefSeq; WP_024092305.1; NC_023135.1.
DR AlphaFoldDB; V9VYI7; -.
DR STRING; 999552.METH_20950; -.
DR KEGG; lmd:METH_20950; -.
DR PATRIC; fig|999552.6.peg.4148; -.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000018780; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:AHD02779.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 14..297
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 306 AA; 31375 MW; A12510A9288CAEDD CRC64;
MDWQVEIRDA AERISPYVQQ TPVMQTQGFG LGFPVALKLE HLQHTGSFKA RGAFNTLLSQ
PVPPAGLVAA SGGNHGAAAA FAAHQLGHKA RVYVPEMAGP AKISLIESNG ADLQVVPGAY
ANALEQAQSY EAATGAMQVH AYDAPATVAG QGTCFAEWQA QGLEADTLLI AVGGGGLIAG
ALAWFRGTKK IVAVEPGTSC ALHAALQARQ PVDVDVSGIA ANALGAKRIG AICFELASAQ
DLTSVTVPDS AIVKAQTALW RERRILAEPA GATALAALMC GAYRPAPGER VAVLICGGNI
APDPLG
//
