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Database: UniProt
Entry: S3L1W1_TREMA
LinkDB: S3L1W1_TREMA
Original site: S3L1W1_TREMA 
ID   S3L1W1_TREMA            Unreviewed;       475 AA.
AC   S3L1W1;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE            EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN   ORFNames=HMPREF9194_01101 {ECO:0000313|EMBL:EPF30779.1};
OS   Treponema maltophilum ATCC 51939.
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=1125699 {ECO:0000313|EMBL:EPF30779.1, ECO:0000313|Proteomes:UP000014541};
RN   [1] {ECO:0000313|EMBL:EPF30779.1, ECO:0000313|Proteomes:UP000014541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51939 {ECO:0000313|EMBL:EPF30779.1,
RC   ECO:0000313|Proteomes:UP000014541};
RG   The Broad Institute Genomics Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Leonetti C., Blanton J.M.,
RA   Dewhirst F.E., Izard J., Walker B., Young S., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Treponema maltophilum ATCC 51939.";
RL   Submitted (APR-2013) 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}.
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:EPF30779.1}.
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DR   EMBL; ATFF01000006; EPF30779.1; -; Genomic_DNA.
DR   RefSeq; WP_016525390.1; NZ_KE332518.1.
DR   AlphaFoldDB; S3L1W1; -.
DR   STRING; 1125699.HMPREF9194_01101; -.
DR   PATRIC; fig|1125699.3.peg.1123; -.
DR   eggNOG; COG0498; Bacteria.
DR   HOGENOM; CLU_015170_0_0_12; -.
DR   OrthoDB; 9763107at2; -.
DR   UniPathway; UPA00050; UER00065.
DR   Proteomes; UP000014541; 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   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:UP000014541};
KW   Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT   DOMAIN          2..81
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          93..378
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         108
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   475 AA;  52287 MW;  57BA5DA45E679568 CRC64;
     MEYTDTRDNS IRTNLKEAVL SGMNPATGGL YIPVRIPKLS PSLLERGFSP SFRDIAFEIA
     KLYCAGEIPE NDLQAIIADC YPFNAPVVPV DPVTYVLELF HGPTCAFKDF GARFMARLMA
     YFNRGEKENL HILVATSGDT GSAVGSAFQG IDGISVTILY PKGKISRLQE KQLSTFTGNV
     RSLAVEGTFD DCQRLVKTAF IDQKLRKAFR LSSANSINIA RLLPQSFYYM YAALSVSCRS
     MHDNKIENPA IIAVVPSGNF GNLTSGFIAK EMGAPITGFI AATNSNKTVP DWMATGRYEP
     RPSVLTLSNA MDVGAPSNHE RITAMYTLDE IKKLLATYWT DDEGTLQGIA SCHERTGYIM
     DPHGAVGWKA WYDIRKDGML KLMSGFPNNP ENPGLTPNLP SWAQAVIDNK AVGILLETAH
     PAKFGETVKR AIGREPPMPD RLEKILNLPD NSVPMKNDYG EFSSWLHKNL PQNDA
//
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