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Database: UniProt
Entry: A0A143HL90_9GAMM
LinkDB: A0A143HL90_9GAMM
Original site: A0A143HL90_9GAMM 
ID   A0A143HL90_9GAMM        Unreviewed;       464 AA.
AC   A0A143HL90;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=A3224_06270 {ECO:0000313|EMBL:AMX02240.1};
OS   Microbulbifer thermotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Microbulbiferaceae; Microbulbifer.
OX   NCBI_TaxID=252514 {ECO:0000313|EMBL:AMX02240.1, ECO:0000313|Proteomes:UP000076077};
RN   [1] {ECO:0000313|Proteomes:UP000076077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAU221 {ECO:0000313|Proteomes:UP000076077};
RA   Lee Y.-S., Choi Y.-L.;
RL   Submitted (MAR-2016) 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; CP014864; AMX02240.1; -; Genomic_DNA.
DR   RefSeq; WP_067152639.1; NZ_JAPHQC010000002.1.
DR   AlphaFoldDB; A0A143HL90; -.
DR   STRING; 252514.A3224_06270; -.
DR   GeneID; 76607658; -.
DR   KEGG; mthd:A3224_06270; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000076077; 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; 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.
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   Reference proteome {ECO:0000313|Proteomes:UP000076077};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..80
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          98..399
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         112
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   464 AA;  51639 MW;  3B2F9DACB8726971 CRC64;
     MKFISTRGRA PSLSFADTVL TGLASDGGLY VPESLPAFSR EEIASMAGLD YRELAFRIMQ
     PFVGSDVSEE ELRGIIDRSY STFRHSAIAP LVQTDTNEWI LELFHGPTLA FKDFALQFLG
     QLFDLLLKKR GERVVVMGAT SGDTGSAAIE GCRHCENIDI FILHPHNRVS EVQRRQMTTV
     LSDNVFNIAL EGNFDDCQNM VKASFAEQSF LPDGRRLVAV NSINWARIMA QIVYYFYAAL
     RLGAPQRTVN FSVPTGNFGD IFAGYLARQM GLPIGQLVIA TNANDILHRC ISDNDHSPRP
     LVHSLSPSMD IMVSSNFERL LFDLYGRDGA AVAALLADRS APMHLSKEAL DRARELFSSY
     RVDDTRTVEV IRAVYESSGY LLDPHTAIGV EAARQVRRAE DQPMVCLSTA HPAKFPQAVA
     RALPTQEIPL PPHMQDLFQR EERMKVLPND LKRVHEFMAM ALGG
//
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