ID C3KNE1_SINFN Unreviewed; 334 AA.
AC C3KNE1;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Threonine dehydratase {ECO:0000313|EMBL:ACP23771.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:ACP23771.1};
GN Name=ilvA1 {ECO:0000313|EMBL:ACP23771.1};
GN OrderedLocusNames=NGR_b23270 {ECO:0000313|EMBL:ACP23771.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234b {ECO:0000313|Proteomes:UP000001054}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23771.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=14702322; DOI=10.1128/JB.186.2.535-542.2004;
RA Streit W.R., Schmitz R.A., Perret X., Staehelin C., Deakin W.J., Raasch C.,
RA Liesegang H., Broughton W.J.;
RT "An evolutionary hot spot: the pNGR234b replicon of Rhizobium sp. strain
RT NGR234.";
RL J. Bacteriol. 186:535-542(2004).
RN [2] {ECO:0000313|EMBL:ACP23771.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000874; ACP23771.1; -; Genomic_DNA.
DR RefSeq; WP_015888384.1; NC_012586.1.
DR RefSeq; YP_002824524.1; NC_012586.1.
DR AlphaFoldDB; C3KNE1; -.
DR KEGG; rhi:NGR_b23270; -.
DR PATRIC; fig|394.7.peg.2755; -.
DR HOGENOM; CLU_021152_4_2_5; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234b.
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; IPR014333; Ectoine_EutB.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR02991; ectoine_eutB; 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; 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:ACP23771.1}; Plasmid {ECO:0000313|EMBL:ACP23771.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT DOMAIN 20..310
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 334 AA; 34691 MW; 481195E102A55FFF CRC64;
MSAFLTVTIE DIEAAARRIS GRVLRTPLVT STSLSKLCGV PVGLKLEHHQ TTGSFKLRGA
TNAVLSLSAE ARARGVIAAS TGNHGRALAH AARTQGSVAT ICMSHLVPEN KVSEIRRLGA
DVRIVGSSQD EAQDEVERLV AEKGLVMVPP FDDAAVVAGQ GTLGLEIVEQ MPDLTAVLVP
LSGGGLAAGV AAAVKARKPA TRVIGLTMER GAAMKASVVA GRPVLVEEYQ SLADSLGGGI
GLDNRLTFRM CSELLDEIIL LTEAEIAAGM RHAYAEEREI VEGAGAVGMA ALLAGKIKIA
GGPIAVILSG RNVDMGLHLR VMNGETDPFR EEAA
//