ID A0A2G5K641_9RHOB Unreviewed; 463 AA.
AC A0A2G5K641;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=BFP76_02790 {ECO:0000313|EMBL:PIB24174.1};
OS Amylibacter kogurei.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Amylibacter.
OX NCBI_TaxID=1889778 {ECO:0000313|EMBL:PIB24174.1, ECO:0000313|Proteomes:UP000231516};
RN [1] {ECO:0000313|EMBL:PIB24174.1, ECO:0000313|Proteomes:UP000231516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:PIB24174.1,
RC ECO:0000313|Proteomes:UP000231516};
RA Wong S.-K., Hamasaki K., Yoshizawa S.;
RT "Draft genome of Amylibacter sp. strain 4G11.";
RL Submitted (AUG-2016) 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:PIB24174.1}.
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DR EMBL; MDGM01000012; PIB24174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5K641; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000231516; 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:UP000231516};
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 99..329
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; 50568 MW; C8C490F2BD084843 CRC64;
MKYISTRGQA PELTFEDAML TGLARDGGLY VPETWPTLSF DEIAGFAGQK YEDVAFAVMK
PFIGDTFSDA EFREILAKSY ASFEHDARCP LVQLDENHFL LELFHGPTLA FKDVAMQLIG
QMFQVALKRR GETVTIVGAT SGDTGSAAME AFKGLDAVNL FIMYPHGRVS DVQRLQMTTP
AESNVHALAV DGDFDTCQAL LKDMFNDFEF RDGVKLAGVN SINWARVLAQ VVYYFTSAVA
LGAPHRKVSF TVPTGNFGDI FAGYVAKRMG LPIDRLVIAT NQNDILHRTM ESGDHAKTGV
TPSISPSMDI QVSSNFERLV FDLYDREGLA VAQLFDALKT DGNFALSQGA LGKLRDEFDS
GRCSENETSA TIKSMAARTG EILCPHSAVG VKVANEHRDG ATPMITLATA HPAKFPAAVK
DACGIHPELP PRMADLFDRE ERFTRVDGTL DAVTKLIKDR IGA
//
