ID U5WEG7_9ACTN Unreviewed; 383 AA.
AC U5WEG7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:AGZ46435.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:AGZ46435.1};
GN ORFNames=AFR_40905 {ECO:0000313|EMBL:AGZ46435.1};
OS Actinoplanes friuliensis DSM 7358.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ46435.1, ECO:0000313|Proteomes:UP000017746};
RN [1] {ECO:0000313|EMBL:AGZ46435.1, ECO:0000313|Proteomes:UP000017746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ46435.1,
RC ECO:0000313|Proteomes:UP000017746};
RX PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL J. Biotechnol. 178:41-42(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
CC -!- SIMILARITY: Belongs to the threonine synthase family.
CC {ECO:0000256|ARBA:ARBA00005517}.
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DR EMBL; CP006272; AGZ46435.1; -; Genomic_DNA.
DR AlphaFoldDB; U5WEG7; -.
DR STRING; 1246995.AFR_40905; -.
DR KEGG; afs:AFR_40905; -.
DR PATRIC; fig|1246995.3.peg.8281; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_4_1_11; -.
DR Proteomes; UP000017746; Chromosome.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AGZ46435.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000017746}.
FT DOMAIN 41..350
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 79
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 383 AA; 40001 MW; 9A176DC7C4BF2BD9 CRC64;
MAYDAAALAS VTREQIEAGP QNIWRYAALL PTGQDPATRV TLDPGLTPLV SATALAAEVG
LRAPLWVKDD SANPTHSFKD RVVSVALTAA RELGFTRFAC ASTGNLANSV AAHAARAGVP
SIVFIPGDLE QGKVITTAVY GGELVAIDGS YDDVNRLCGE LVETDEFEDT AFVNVNVRPF
YAEGSKTLGY EVAEQLGWRI PAQVVVPMAS GELLTKIDKA FSELVEIGLV EAPEGGWTVF
GAQSAGCNPI ATALHNGTDQ IIPVKPTGIA KSLNIGDPAA GSYAIEAVTR TGGWMDYADD
DEIRDAIQLL ARTTGVFAET AGGVTVAVLK KLVASGKLDP DKETVVYNTG EGLKTLDAVA
GQVGPTHRIK PSLRGARDAG LLG
//
