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
//