ID Q161F5_ROSDO Unreviewed; 327 AA.
AC Q161F5;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Threonine dehydratase, putative {ECO:0000313|EMBL:ABG33388.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:ABG33388.1};
GN OrderedLocusNames=RD1_3931 {ECO:0000313|EMBL:ABG33388.1};
OS Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS (strain OCh 114)) (Roseobacter denitrificans).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=375451 {ECO:0000313|EMBL:ABG33388.1, ECO:0000313|Proteomes:UP000007029};
RN [1] {ECO:0000313|EMBL:ABG33388.1, ECO:0000313|Proteomes:UP000007029}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33942 / OCh 114 {ECO:0000313|Proteomes:UP000007029};
RX PubMed=17098896; DOI=10.1128/JB.01390-06;
RA Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA O'huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA Touchman J.W.;
RT "The complete genome sequence of Roseobacter denitrificans reveals a
RT mixotrophic rather than photosynthetic metabolism.";
RL J. Bacteriol. 189:683-690(2007).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000362; ABG33388.1; -; Genomic_DNA.
DR RefSeq; WP_011569999.1; NZ_FOOO01000010.1.
DR AlphaFoldDB; Q161F5; -.
DR STRING; 375451.RD1_3931; -.
DR KEGG; rde:RD1_3931; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000007029; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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.
PE 4: Predicted;
KW Lyase {ECO:0000313|EMBL:ABG33388.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000007029}.
FT DOMAIN 15..308
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 327 AA; 33814 MW; 933822753AB8DECA CRC64;
MNIDAIRAAE QRLKGHVRRT PLLCSPNLDA IAGCRVFVKA ECLQHTGSFK YRGALSAISA
LDADARKRGI IAFSSGNHAQ GIALAARQFD APAVIIMPQD APSTKIENTR TLGAEIVLYD
RVGGEDRDAI GAELSAKRNL TLIKPFDNAQ VIAGQGTAGL EIAAQAQARG IDDADVIVCC
GGGGFASGIA LALEADAPGF RVRPAEPAGF DDMARSLKAG ARLHNAQTSG SLCDAIITPT
PGVLTFPILQ RLAGPGLVVS DEEALHAMAL AFAHLKVVAE PGGAVALASA LFHTSEIDAD
TVIVTISGGN VDADVFQMAL KRCGDSA
//