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Database: UniProt
Entry: Q1N800_SPHSS
LinkDB: Q1N800_SPHSS
Original site: Q1N800_SPHSS 
ID   Q1N800_SPHSS            Unreviewed;       415 AA.
AC   Q1N800;
DT   30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   30-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:EAT07161.1};
GN   ORFNames=SKA58_11593 {ECO:0000313|EMBL:EAT07161.1};
OS   Sphingomonas sp. (strain SKA58).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=314266 {ECO:0000313|EMBL:EAT07161.1, ECO:0000313|Proteomes:UP000005395};
RN   [1] {ECO:0000313|EMBL:EAT07161.1, ECO:0000313|Proteomes:UP000005395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SKA58 {ECO:0000313|EMBL:EAT07161.1,
RC   ECO:0000313|Proteomes:UP000005395};
RA   Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
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};
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:EAT07161.1}.
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DR   EMBL; AAQG01000025; EAT07161.1; -; Genomic_DNA.
DR   RefSeq; WP_009822076.1; NZ_CH959306.1.
DR   AlphaFoldDB; Q1N800; -.
DR   STRING; 314266.SKA58_11593; -.
DR   eggNOG; COG1171; Bacteria.
DR   HOGENOM; CLU_021152_4_1_5; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000005395; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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; IPR045865; ACT-like_dom_sf.
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; PF00291; PALP; 1.
DR   SUPFAM; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51671; ACT; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005395}.
FT   DOMAIN          338..415
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   415 AA;  44729 MW;  EEC416FB2FE9A844 CRC64;
     MNTLAKIESA LPLPVTVDDI LAARTRIAGA IVKTPTLISQ TLSDMLGCKV YLKFENLQFT
     AAYKERGALN RLLQLDDASK AKGVIAASAG NHAQGLAYHG KRLGVPVTIV MPTTTPIIKV
     TQTRSHGATV VQFGEKFDDA YAHARELEAQ QGLTFVHPFD EPDIIAGQGT VALEMLEDAP
     EIDTLVVPIG GGGLFSGMGT AARAMKPDIR LIGVQAELYP SMYGFMKSTD LACDGDTLAE
     GIAVKQPGSV TRRFVERLAD DILLVNERRL EESLSLLLQI EKTVVEGAGA AGLAALLTHR
     DQFAGRRVGL VLTGGNIDTR LLANVLLRDL ARSGRLARLR IILQDRPGAL FNVARIFDQE
     AVNILELSHQ RIFTNLPAKG LSLDVECETR DRDHLQNLLG ALRAAGYEVA PIEVA
//
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