ID Q493S8_BLOPB Unreviewed; 433 AA.
AC Q493S8;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:AAZ40757.1};
GN Name=thrC {ECO:0000313|EMBL:AAZ40757.1};
GN OrderedLocusNames=BPEN_117 {ECO:0000313|EMBL:AAZ40757.1};
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX NCBI_TaxID=291272 {ECO:0000313|EMBL:AAZ40757.1, ECO:0000313|Proteomes:UP000007794};
RN [1] {ECO:0000313|EMBL:AAZ40757.1, ECO:0000313|Proteomes:UP000007794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN {ECO:0000313|EMBL:AAZ40757.1,
RC ECO:0000313|Proteomes:UP000007794};
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40757.1; -; Genomic_DNA.
DR RefSeq; WP_011282664.1; NC_007292.1.
DR AlphaFoldDB; Q493S8; -.
DR STRING; 291272.BPEN_117; -.
DR KEGG; bpn:BPEN_117; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_015170_0_0_6; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000007794; Chromosome.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.90.1380.10; Threonine synthase, N-terminal domain; 1.
DR InterPro; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
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; PTHR42690; THREONINE SYNTHASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42690:SF1; THREONINE SYNTHASE-LIKE 2; 1.
DR Pfam; PF00291; PALP; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000007794}.
FT DOMAIN 10..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 96..366
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 433 AA; 48460 MW; 1B635AB3B30EE1D5 CRC64;
MKLYNIKQPS EQVTFTQALL QGLGKNQGLF FPKDLPKFSI FEINSLLEMS FIERSTHILS
TYIGSELSKN SILTCVKNAF NFPVPLVCIN NNVAILELFH GPTLAFKDFG SRLMAQMLNQ
TNHCSDKPMV ILTATSGDTG AAVAHAFFNL SNIHVIILYP RGKISALQEK LFCTLGGNIS
TISVNGDFDS CQRLVKKAFD DSVLRQKLNL NSANSINIGR LLAQICYYFE GVSQLPHQMR
NKLVIAVPSG NFGNLTAGLL AQSCGLPVKK FIAATNINDT VPRFLEFGYW EPRPTLSTFS
NAMDVSSPNN WSRIEELFRR ENKSIKELEY GCVNDFLTEK TVQEIADLGY LSEPHTAVAY
RLLCDKLHSD EFGICLGTAH PVKFKELVED FLKKKIQLIL PIVLKERMKL PVLSFKIPKC
FSSLRNLILS IMS
//