ID A0A271IVD3_9BACT Unreviewed; 427 AA.
AC A0A271IVD3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, 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=BSZ37_01355 {ECO:0000313|EMBL:PAP75183.1};
OS Rubrivirga marina.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubrivirga.
OX NCBI_TaxID=1196024 {ECO:0000313|EMBL:PAP75183.1, ECO:0000313|Proteomes:UP000216339};
RN [1] {ECO:0000313|EMBL:PAP75183.1, ECO:0000313|Proteomes:UP000216339}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC-28 {ECO:0000313|EMBL:PAP75183.1,
RC ECO:0000313|Proteomes:UP000216339};
RA Yoshizawa S., Kumagai Y., Kogure K.;
RT "Study of marine rhodopsin-containing bacteria.";
RL Submitted (NOV-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:PAP75183.1}.
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DR EMBL; MQWD01000001; PAP75183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A271IVD3; -.
DR OrthoDB; 9763107at2; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000216339; 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:UP000216339};
KW Threonine biosynthesis {ECO:0000256|ARBA:ARBA00022697}.
FT DOMAIN 6..63
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 94..375
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 427 AA; 44621 MW; 407C88B0FBF29B22 CRC64;
MSAPLYVSTR GGADPVPFRE ALLDGLAPDG GLYVPTHVPA LPAGWQSATA LADLGGRVLA
EWLPEVDRLD ALVMDALSFP IPLVPLRGGG WDGVHVLELF HGPTLSFKDV GARTMARLMG
AALGGEPVTI LAATSGDTGS AVASGFEGVE GVRVVLLYPM GQVSAVQERQ LIVERDNVQA
LAVEGTFDDC QRLVKQAFSE ARPAKGRLSS ANSINIGRLL PQTLYYLWAG RELAVAGAEG
PPAFVVPSGN LGNLTAGTLA MRGGLDVAGF LAAHNANDGF PRFLDGGDPP AGDSVRTLSN
AMDVGVPSNL ERLRSLFSDD QLRSLVRGEA VTDEETTASM RRVHDETGYL ADPHTAVGLE
AARRARGRGE AGPMIVLSTA HPAKFPEAVE AAAGVAPEAP ERLASLWDAP VSVETIPSTL
DALRAHL
//
