ID K9SC48_9CYAN Unreviewed; 434 AA.
AC K9SC48;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=GEI7407_2878 {ECO:0000313|EMBL:AFY67349.1};
OS Geitlerinema sp. PCC 7407.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Geitlerinematales;
OC Geitlerinemataceae; Geitlerinema.
OX NCBI_TaxID=1173025 {ECO:0000313|EMBL:AFY67349.1, ECO:0000313|Proteomes:UP000010383};
RN [1] {ECO:0000313|EMBL:AFY67349.1, ECO:0000313|Proteomes:UP000010383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7407 {ECO:0000313|EMBL:AFY67349.1,
RC ECO:0000313|Proteomes:UP000010383};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished genome of Geitlerinema sp. PCC 7407.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR038945};
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|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; CP003591; AFY67349.1; -; Genomic_DNA.
DR RefSeq; WP_015172913.1; NC_019703.1.
DR AlphaFoldDB; K9SC48; -.
DR STRING; 1173025.GEI7407_2878; -.
DR KEGG; gei:GEI7407_2878; -.
DR PATRIC; fig|1173025.3.peg.3221; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_4_1_3; -.
DR OrthoDB; 9778118at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000010383; Chromosome.
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; 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; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF038945; Thr_synthase; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|PIRNR:PIRNR038945};
KW Lyase {ECO:0000256|PIRNR:PIRNR038945, ECO:0000313|EMBL:AFY67349.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRNR:PIRNR038945};
KW Reference proteome {ECO:0000313|Proteomes:UP000010383};
KW Threonine biosynthesis {ECO:0000256|PIRNR:PIRNR038945}.
FT DOMAIN 86..388
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT BINDING 148
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT BINDING 387
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT MOD_RES 122
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ SEQUENCE 434 AA; 47069 MW; 6FE888DD2C1C6A97 CRC64;
MTQTADRQAQ TRTATFSGLK CKECGAEYEP QAIHVCEQCF GPLEVAYDYN AIRSLVSRES
IQAGPNSIWR YRAFLPVETD TPIDVGTGMT PLLQANRLAR RLGLKKLYIK NDAVNMPTLS
FKDRVVSVAL TRARELGFST VSCASTGNLA NSTAAIAAHA GLECCVFIPA DLEAGKVLGT
VIYGPTVMAV EGNYDQVNRL CSEVANTHGW GFVNINLRPY YSEGSKTLGY EVAEQLGWEL
PDHIVAPLAS GSLFTKIYKG FREFVEVGLV EDKHVRFSGA QAEGCSPIAQ AFQEGRDFIK
PVKPNTIAKS IAIGNPADGV YAVDIAQKTN GNIESVTDAE IIEGMKLLAE TEGIFTETAG
GTTIATLKKL VEAGKISPDE TTVVYITGNG LKTQEAVQGY VGEPLTIEPK LESFERALER
AQTLDRLEWQ QVLV
//
