ID   W0DWR0_9GAMM            Unreviewed;       492 AA.
AC   W0DWR0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=THIAE_05380 {ECO:0000313|EMBL:AHF01301.1};
OS   Thiomicrospira aerophila AL3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Thiomicrospira.
OX   NCBI_TaxID=717772 {ECO:0000313|EMBL:AHF01301.1, ECO:0000313|Proteomes:UP000005380};
RN   [1] {ECO:0000313|EMBL:AHF01301.1, ECO:0000313|Proteomes:UP000005380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AL2 {ECO:0000313|Proteomes:UP000005380};
RG   DOE Joint Genome Institute;
RA   Kappler U., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-homoserine = L-threonine + phosphate;
CC         Xref=Rhea:RHEA:10840, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57590, ChEBI:CHEBI:57926; EC=4.2.3.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000051};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR604450-51};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517}.
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DR   EMBL; CP007030; AHF01301.1; -; Genomic_DNA.
DR   RefSeq; WP_006460367.1; NZ_CP007030.1.
DR   AlphaFoldDB; W0DWR0; -.
DR   STRING; 717772.THIAE_05380; -.
DR   KEGG; tao:THIAE_05380; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_015170_3_1_6; -.
DR   InParanoid; W0DWR0; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000005380; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway.
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; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR   PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          3..76
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          101..339
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         115
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   492 AA;  54261 MW;  4CEDCA68A0443908 CRC64;
     MNFIETRGND GHFPPQFTFS QAILSPMSSY GGLYSPESLP SLDQAFLQAH LDSDYKTLAK
     AVLMKFEVDI PEEVIDRALA LYDQFDDPKH PVPVVKVTDR IFVSELFHGP TRAFKDMALQ
     PFGTLLSAVA QARQEQFLIL AATSGDTGPA ALDTFRDKPN VQVVCMYPEG GTSDVQRLQM
     VTEAGKNLKV IGIKGDFDDA QSALKTLLTS DEFKATLQQK GISVSAANSV NFGRIIFQTL
     YHIHSYLELV RMGEISLGEP VYLNVPSGNF GNALGGYYAY KMGLPVAKIL IASNDNNVLT
     QFINQGVYDL RGAQVQPTKS PAMDILKSSN IERILFDMLG AKRTRELMLA LDKDKFYQLT
     PAELAKVQAI FAADYCTDEE GAHYIKQHFE QGYLMDPHTA TSFKVDATQV DNPAIKSIIY
     STAEWTKFSP TIVASVFGED VANDEAALQK MAATGQACIP KQIAALFTKP AVQDKVIDKN
     DIEAEILRFF EV
//