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Database: UniProt
Entry: A0A1N7MHK9_9RHOB
LinkDB: A0A1N7MHK9_9RHOB
Original site: A0A1N7MHK9_9RHOB 
ID   A0A1N7MHK9_9RHOB        Unreviewed;       463 AA.
AC   A0A1N7MHK9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=SAMN05421795_107135 {ECO:0000313|EMBL:SIS85557.1};
OS   Phaeovulum vinaykumarii.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Phaeovulum.
OX   NCBI_TaxID=407234 {ECO:0000313|EMBL:SIS85557.1, ECO:0000313|Proteomes:UP000186098};
RN   [1] {ECO:0000313|Proteomes:UP000186098}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18714 {ECO:0000313|Proteomes:UP000186098};
RA   Varghese N., Submissions S.;
RL   Submitted (JAN-2017) 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; FTOM01000007; SIS85557.1; -; Genomic_DNA.
DR   RefSeq; WP_076366880.1; NZ_OBMN01000007.1.
DR   AlphaFoldDB; A0A1N7MHK9; -.
DR   STRING; 407234.SAMN05421795_107135; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000186098; 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:0000256|ARBA:ARBA00023239};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186098};
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          100..332
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   463 AA;  49885 MW;  79C953CC7746226B CRC64;
     MRYISTRGRA PELGFKDAML TGLARDGGLY VPAEIPRLSP DEIAALAGQS YEEVAYRVMA
     PFTGDAFSEA DLRGAIERAY AGFGHAARAP LVQLAPGHFL LELFHGPTLA FKDFAMQVIG
     QLFQLALARE GRRITIVGAT SGDTGSAAIE AFRGLDNVDV FILFPHGRVS EVQRRQMTTP
     VEANVHALAL QGDFDDCQAR LKDMFNDHDF RDSVGLAGVN SINWARVLAQ VVYYFTAAVS
     LGAPGRPVDF TVPTGNFGDI FAGYIARRMG LPIRRLVVAT NQNDILHRCL STGEYRTDGV
     KPSISPSMDI QVSSNFERAL FEVLGRDGAA VTQLMDELRS AGGFSVPQGA LEALREIFGS
     GRASEDETSA TIAAQLAATG ELLCPHSAVG VKVAQEHLAP PVPMITLATA HPAKFPDAVE
     AATGRRPGLP PRMADLFDRS ERMRVVENDL AALQALIHEG RRA
//
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