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Database: UniProt
Entry: C1A7S4_GEMAT
LinkDB: C1A7S4_GEMAT
Original site: C1A7S4_GEMAT 
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
//
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