GenomeNet

Database: UniProt
Entry: T2JHA0_CROWT
LinkDB: T2JHA0_CROWT
Original site: T2JHA0_CROWT 
ID   T2JHA0_CROWT            Unreviewed;       375 AA.
AC   T2JHA0;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679, ECO:0000256|PIRNR:PIRNR038945};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028, ECO:0000256|PIRNR:PIRNR038945};
GN   ORFNames=CWATWH0402_4576 {ECO:0000313|EMBL:CCQ65208.1};
OS   Crocosphaera watsonii WH 0402.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera.
OX   NCBI_TaxID=1284629 {ECO:0000313|EMBL:CCQ65208.1, ECO:0000313|Proteomes:UP000018130};
RN   [1] {ECO:0000313|EMBL:CCQ65208.1, ECO:0000313|Proteomes:UP000018130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0402 {ECO:0000313|EMBL:CCQ65208.1,
RC   ECO:0000313|Proteomes:UP000018130};
RA   Bench S.;
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCQ65208.1, ECO:0000313|Proteomes:UP000018130}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH 0402 {ECO:0000313|EMBL:CCQ65208.1,
RC   ECO:0000313|Proteomes:UP000018130};
RA   Bench S.R., Heller P., Frank I., Arciniega M., Shilova I.N., Zehr J.P.;
RT   "Whole genome comparison of six Crocosphaera watsonii strains with
RT   differing phenotypes.";
RL   Submitted (SEP-2013) 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|ARBA:ARBA00000051,
CC         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|ARBA:ARBA00004979,
CC       ECO:0000256|PIRNR:PIRNR038945}.
CC   -!- SIMILARITY: Belongs to the threonine synthase family.
CC       {ECO:0000256|ARBA:ARBA00005517, ECO:0000256|PIRNR:PIRNR038945}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCQ65208.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CAQN01000129; CCQ65208.1; -; Genomic_DNA.
DR   RefSeq; WP_007312086.1; NZ_CAQN01000129.1.
DR   AlphaFoldDB; T2JHA0; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000018130; Unassembled WGS sequence.
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; IPR001763; Rhodanese-like_dom.
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; 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.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR038945};
KW   Lyase {ECO:0000256|PIRNR:PIRNR038945, ECO:0000313|EMBL:CCQ65208.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRNR:PIRNR038945};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697,
KW   ECO:0000256|PIRNR:PIRNR038945}.
FT   DOMAIN          105..148
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   BINDING         212..216
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   BINDING         340
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-1"
FT   MOD_RES         86
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038945-2"
SQ   SEQUENCE   375 AA;  39745 MW;  8A2E360138B2AFAE CRC64;
     MIVQPLTSPP SAPNSKTITP SSDVKPWPGL IETYRPYLPV TENTPVFTLL EGNTPLIPVP
     YISQQVGKGV KVFVKYDGLN PTGSFKDRGM TMAISKAKEE GAKAVICAST GNTSAAAAAY
     ARRAGMRAFV IIPDGYVALG KLAQALLYGA EVIAVEGNFD DALTVVKNMA KDYPVTLVNS
     LNPYRLEGQK TAAFEVVDVL GNAPDWLCIP VGNAGNISAY WMGFCQYRSF GKSDKLPKMM
     GFQAAGAAPF MAGKPVPNPE TLATAIRIGN PANWDKAWGA KDASQGEFNA VTDEEILEAY
     RILAAHEGIF CEPASAASVA GLLKVSDRVP ANSTVVCVLT GNGLKDPDSA IKHSKNQVKS
     GIKPELSQVA KVMGF
//
DBGET integrated database retrieval system