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Database: UniProt
Entry: A0A261VJZ1_9BORD
LinkDB: A0A261VJZ1_9BORD
Original site: A0A261VJZ1_9BORD 
ID   A0A261VJZ1_9BORD        Unreviewed;       469 AA.
AC   A0A261VJZ1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:OZI74395.1};
GN   ORFNames=CAL22_07890 {ECO:0000313|EMBL:OZI74395.1};
OS   Bordetella genomosp. 12.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463035 {ECO:0000313|EMBL:OZI74395.1, ECO:0000313|Proteomes:UP000216429};
RN   [1] {ECO:0000313|EMBL:OZI74395.1, ECO:0000313|Proteomes:UP000216429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU6712 {ECO:0000313|EMBL:OZI74395.1,
RC   ECO:0000313|Proteomes:UP000216429};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OZI74395.1}.
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DR   EMBL; NEVU01000002; OZI74395.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261VJZ1; -.
DR   OrthoDB; 9763107at2; -.
DR   Proteomes; UP000216429; Unassembled WGS sequence.
DR   CDD; cd01560; Thr-synth_2; 1.
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}.
FT   DOMAIN          2..79
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          107..344
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         113
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   469 AA;  50963 MW;  486F5AF44364DF6C CRC64;
     MKYVSTRGGM AAQAFSDILL EGLAPDGGLA VPQQLPQVDA ATLESWRPLS YADLAVEVLS
     LFATDIPRED LSRLAHAAYN EQVFSSEQIV PLRPLAGGLQ LLGLSEGPTL AFKDMAMQFL
     GQVFEYVLTK RGTTLNIVGA TSGDTGSAAE YALRGKQGVG VFMLSPHGRM SSFQRAQMYS
     LQDENIHNIA VKGVFDQAQD IVKALAADLT FKSRYRIGAV NSINWARIAA QVVYYFHGWL
     RATTGAGQQV SFAVPSGNFG NILSGHIARR MGLPVRRLVL ATNENNVLEE FFRTGIYRPR
     APEQTYATSS PSMDISRASN FERFIYDLVG GDGERVRALW QELADKGSFD LSAQRASFGE
     QYGFASGVST HDDRLSTIRA VFDETGVLID PHTADGVHVA RSFVEEGIPM LVLETALPAK
     FSDTIQEALG RPVPPPAELA GLESLPQRVT VMDCDAAQVR AFIEAHAKI
//
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