ID C1A7S4_GEMAT Unreviewed; 330 AA.
AC C1A7S4;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:BAH38284.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:BAH38284.1};
GN OrderedLocusNames=GAU_1242 {ECO:0000313|EMBL:BAH38284.1};
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC Gemmatimonadaceae; Gemmatimonas.
OX NCBI_TaxID=379066 {ECO:0000313|EMBL:BAH38284.1, ECO:0000313|Proteomes:UP000002209};
RN [1] {ECO:0000313|Proteomes:UP000002209}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505
RC {ECO:0000313|Proteomes:UP000002209};
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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; AP009153; BAH38284.1; -; Genomic_DNA.
DR RefSeq; WP_012682731.1; NC_012489.1.
DR AlphaFoldDB; C1A7S4; -.
DR STRING; 379066.GAU_1242; -.
DR KEGG; gau:GAU_1242; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_0; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000002209; 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 CDD; cd01562; Thr-dehyd; 1.
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:BAH38284.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000002209}.
FT DOMAIN 22..315
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 330 AA; 34244 MW; 8B6D34A1F53AA3E0 CRC64;
MTASALIAPS IDDIRAAAAR IAPHAAVTPL LESPALDAAA GGRVLLKAEV LQHTGSFKLR
GALNRLLQLS PEERTRGVVA FSSGNHAQAV AYSATLLGMR STIVMPKDAP SLKIERTRAF
GAEVVLYDRY TEDRVAIGRA IAAKTDATVV PPFEDPHVVA GQGTLALEAL QQATARGATP
DRLYVNCGGG GLTAGCAIAA EAVSPGTVVH PCEPEHFDDT ARSLELGYRV ANEPGHRSIC
DAIVTDIPGE FTFSINQPRV GEGLRVSEDE VLAAIAFAVR ELKLVVEPGG AAALAALLSG
RLDTRGRTTL VVVTGGNIDP KILARAVGAG
//