ID A0A1W1Y0P5_9NEIS Unreviewed; 477 AA.
AC A0A1W1Y0P5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=SAMN02745857_04110 {ECO:0000313|EMBL:SMC29769.1};
OS Andreprevotia lacus DSM 23236.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Andreprevotia.
OX NCBI_TaxID=1121001 {ECO:0000313|EMBL:SMC29769.1, ECO:0000313|Proteomes:UP000192761};
RN [1] {ECO:0000313|EMBL:SMC29769.1, ECO:0000313|Proteomes:UP000192761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23236 {ECO:0000313|EMBL:SMC29769.1,
RC ECO:0000313|Proteomes:UP000192761};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-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; FWXD01000043; SMC29769.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W1Y0P5; -.
DR STRING; 1121001.SAMN02745857_04110; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000192761; 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:UP000192761};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 94..339
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 120
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 477 AA; 52383 MW; E72EF0426941C060 CRC64;
MRYISTRGGM APQAFSDILL GGLAPDGGLS IPETYPQFDL AQLQALAGLN YRDLAFAVIS
RFVDDIPAAD LKALIDKTYT PAVYCNGRSK AQSEHITPLI KLDNTLFIQE LSNGPTLAFK
DMAMQLLGNL FEYVLNQRGE QVNIVGATSG DTGSAAEYAM RGKHGVNVFM LSPYGKMSPF
QRAQMFSLQD ANIFNLSVKG FFDACQDIVK AINNDAAFKA QYKIGAVNSI NWGRIVAQVV
YYFKGYFSAA KTVGDPVDFV VPSGNFGNIC AGHIARQMGL PIRRLIVATN ENDVLDEFFK
TGGYFPRGVD KTYETTSPSM DISKASNLER FVFDLVGRDS NKLAELWRSV DKGEGFKLSE
SEFALLHDTY GFRSEASTHA DRIASIREVF DKYGVQIDPH TADGYKAAKA HRDSNVVTVI
METALPAKFE DTMREALGIN PARPAGLAGL EQLPQRFDAL EADAEAIKAY LRERIAV
//
