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Database: UniProt
Entry: A0A095C3Y0_9SPHN
LinkDB: A0A095C3Y0_9SPHN
Original site: A0A095C3Y0_9SPHN 
ID   A0A095C3Y0_9SPHN        Unreviewed;       416 AA.
AC   A0A095C3Y0;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:KGB58026.1};
DE            EC=4.3.1.19 {ECO:0000313|EMBL:KGB58026.1};
GN   ORFNames=FG95_01349 {ECO:0000313|EMBL:KGB58026.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB58026.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB58026.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB58026.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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:KGB58026.1}.
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DR   EMBL; JNFC01000013; KGB58026.1; -; Genomic_DNA.
DR   RefSeq; WP_037554848.1; NZ_JNFC01000013.1.
DR   AlphaFoldDB; A0A095C3Y0; -.
DR   STRING; 1120705.FG95_01349; -.
DR   PATRIC; fig|1120705.3.peg.1362; -.
DR   eggNOG; COG1171; Bacteria.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000029625; 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   Lyase {ECO:0000313|EMBL:KGB58026.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029625}.
FT   DOMAIN          339..416
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   416 AA;  44851 MW;  DF2592723ADACA60 CRC64;
     MTDQLTLTPA ADFPAITLDD VRAAAGRING AVVRTPTLHS QTLSELVGAE VWLKFENLQF
     TAAYKERGAL NALLLLDDEA KARGVIAASA GNHAQGLAYH GKRLGVPVTI VMPKTTPQVK
     VSQTASHGAE IVLFGEKFDD ASAHARVLEK ERGLTFVHPF DHPHIAAGQG TVALEMLEDV
     PELDTMIVPI GGGGLLTGMG TAARGIKNDM RLIGVQAELY PSMYAELNGV DMACEGDTLA
     EGIAVKEPGV YTRKIVAELN DDIVLVAERH LERAVSLLLQ IEKTVVEGAG AAGLAAMLAH
     PEEFKGRKVG LVLTGGNIDT RLLANVLLRD LARSGRIARL RIRLQDRPGA LFKVMKLFDE
     KQVNIIEIYH QRIFTTLPAK GLITDIECEA RDREHLDSLV ASLRDAGYMV TTVELA
//
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