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Database: UniProt
Entry: A0A0P1FCQ2_9RHOB
LinkDB: A0A0P1FCQ2_9RHOB
Original site: A0A0P1FCQ2_9RHOB 
ID   A0A0P1FCQ2_9RHOB        Unreviewed;       462 AA.
AC   A0A0P1FCQ2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   Name=thrC {ECO:0000313|EMBL:CUH52864.1};
GN   ORFNames=SHM7688_02311 {ECO:0000313|EMBL:CUH52864.1};
OS   Shimia marina.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=321267 {ECO:0000313|EMBL:CUH52864.1, ECO:0000313|Proteomes:UP000054823};
RN   [1] {ECO:0000313|EMBL:CUH52864.1, ECO:0000313|Proteomes:UP000054823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7688 {ECO:0000313|EMBL:CUH52864.1,
RC   ECO:0000313|Proteomes:UP000054823};
RG   Swine Surveillance;
RL   Submitted (SEP-2015) 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; CYPW01000024; CUH52864.1; -; Genomic_DNA.
DR   RefSeq; WP_058240057.1; NZ_FOMU01000003.1.
DR   AlphaFoldDB; A0A0P1FCQ2; -.
DR   STRING; 321267.SHM7688_02311; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000054823; 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; 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   Lyase {ECO:0000313|EMBL:CUH52864.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054823};
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          89..330
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   462 AA;  50252 MW;  2E3F91E4670EC77F CRC64;
     MKYISTRGNA PELSFEEAML TGLARDGGLY VPETIPTLSR EEIAALAGKS YEEAAFTVMR
     PFVGDAFSDE EFKGIIARAY ANFRHEARAP LVQLAPNHYL LELFHGPTLA FKDFAMQLIG
     QLFQFSLARR NERVTIVGAT SGDTGSAAIE AFRGLDNVDV FILFPHGRVS PIQRKQMTTP
     TDSNVHALAL DGDFDDCQAR LKDMFNDFEF RDGVKLAGVN SINWARVLAQ VVYYFTSAVS
     LGAPDRKVSF TVPTGNFGDI FAGYIAKKMG LPIERLVIAT NQNDILHRTM ESGAYTKEGV
     TPSISPSMDI QVSSNFERAL FDAYGRDGGA VAQLMEELKD GAFAISQGAM ETLRDHFASG
     RASEEETTAT IAGAFTSCGE VLCPHSAVGV KVANAYLGDV PMVTLATAHP AKFPDAVETA
     MGARPALPPH MADMMDKDER VTRVPNDLGA LETLIKERIA QR
//
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