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Database: UniProt
Entry: U5T3S9_9GAMM
LinkDB: U5T3S9_9GAMM
Original site: U5T3S9_9GAMM 
ID   U5T3S9_9GAMM            Unreviewed;       378 AA.
AC   U5T3S9;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE            EC=4.2.3.1 {ECO:0000256|PIRNR:PIRNR038945};
GN   ORFNames=SPICUR_04845 {ECO:0000313|EMBL:AGY91946.1};
OS   Spiribacter curvatus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Spiribacter.
OX   NCBI_TaxID=1335757 {ECO:0000313|EMBL:AGY91946.1, ECO:0000313|Proteomes:UP000017640};
RN   [1] {ECO:0000313|EMBL:AGY91946.1, ECO:0000313|Proteomes:UP000017640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAH-SP71 {ECO:0000313|EMBL:AGY91946.1,
RC   ECO:0000313|Proteomes:UP000017640};
RX   PubMed=24225341; DOI=10.1186/1471-2164-14-787;
RA   Lopez-Perez M., Ghai R., Leon M.J., Rodriguez-Olmos A., Copa-Patino J.L.,
RA   Soliveri J., Sanchez-Porro C., Ventosa A., Rodriguez-Valera F.;
RT   "Genomes of "Spiribacter", a streamlined, successful halophilic
RT   bacterium.";
RL   BMC Genomics 14:787-787(2013).
CC   -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L-
CC       phosphohomoserine and the beta-addition of water to produce L-
CC       threonine. {ECO:0000256|ARBA:ARBA00003648,
CC       ECO:0000256|PIRNR:PIRNR038945}.
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         ECO:0000256|PIRNR:PIRNR038945};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|ARBA:ARBA00000298};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRNR:PIRNR038945, ECO:0000256|PIRSR:PIRSR038945-1};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine
CC       from L-aspartate: step 5/5. {ECO:0000256|ARBA:ARBA00004979,
CC       ECO:0000256|PIRNR:PIRNR038945}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
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DR   EMBL; CP005990; AGY91946.1; -; Genomic_DNA.
DR   RefSeq; WP_023366613.1; NC_022664.1.
DR   AlphaFoldDB; U5T3S9; -.
DR   STRING; 1335757.SPICUR_04845; -.
DR   KEGG; spiu:SPICUR_04845; -.
DR   PATRIC; fig|1335757.3.peg.943; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_028142_0_0_6; -.
DR   OrthoDB; 9778118at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000017640; 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; cd01563; Thr-synth_1; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR004450; Thr_synthase-like.
DR   InterPro; IPR026260; Thr_Synthase_bac/arc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00260; thrC; 1.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF5; THREONINE SYNTHASE 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF038945; Thr_synthase; 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   ECO:0000256|PIRNR:PIRNR038945}; Lyase {ECO:0000256|PIRNR:PIRNR038945};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR038945};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017640};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW   ECO:0000256|PIRNR:PIRNR038945}.
FT   DOMAIN          26..342
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   BINDING         91
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   BINDING         191..195
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   BINDING         341
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   MOD_RES         65
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ   SEQUENCE   378 AA;  39671 MW;  6339249C3E93B0DC CRC64;
     MKGNRYTGLI GAYGSRLPLD AGARPISLGE GNTPLIRLDN LPLARERDIE LYVKYEGLNP
     TGSFKDRGMT VAVTQAVAEG SEAIICASTG NTSASAAAYA ARAGIKAFVL IPDGKIAMGK
     LAQAIMHGAD VLQIRGNFDD GMRIVKEMAQ QAPVSLVNSV NPYRLQGQKT AAFEICEALG
     EAPDYHCLPV GNAGNITAYW MGYSEMALSP GDPGTEACGF CGGDCAFHEG LVRNRPVMLG
     YQASGSAPFL RGGPVSHPET LATAIRIGAP QSWDYARTAS QESGGWFDEF TDEAILDAQF
     QLASHEGIFC EPASIVSVAG AMQDIEQGRI PPGSRVVCTL TGHGLKDTDV AQRHAGSAVT
     TVDADGSSVR QAILGKMG
//
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