ID A0A1T1HGA4_OCELI Unreviewed; 463 AA.
AC A0A1T1HGA4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Threonine synthase {ECO:0000256|ARBA:ARBA00018679};
DE EC=4.2.3.1 {ECO:0000256|ARBA:ARBA00013028};
GN ORFNames=BTA35_0204645 {ECO:0000313|EMBL:OOV88770.1};
OS Oceanospirillum linum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Oceanospirillum.
OX NCBI_TaxID=966 {ECO:0000313|EMBL:OOV88770.1, ECO:0000313|Proteomes:UP000190064};
RN [1] {ECO:0000313|EMBL:OOV88770.1, ECO:0000313|Proteomes:UP000190064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11336 {ECO:0000313|EMBL:OOV88770.1,
RC ECO:0000313|Proteomes:UP000190064};
RA Trachtenberg A.M., Carney J.G., Linnane J.D., Rheaume B.A., Pitts N.L.,
RA Mykles D.L., Maclea K.S.;
RT "Draft Genome Sequence of the Salt Water Bacterium Oceanospirillum linum
RT ATCC 11336.";
RL Submitted (FEB-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}.
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:OOV88770.1}.
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DR EMBL; MTSD02000001; OOV88770.1; -; Genomic_DNA.
DR RefSeq; WP_077243218.1; NZ_MTSD02000001.1.
DR AlphaFoldDB; A0A1T1HGA4; -.
DR STRING; 966.BTA35_0204645; -.
DR UniPathway; UPA00050; UER00065.
DR Proteomes; UP000190064; 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:UP000190064};
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 88..330
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; 51249 MW; 25F049410A10ECAA CRC64;
MRYISTRGQA PALNFEDVVL TGLASDGGLY VPETIPQFSA EEIASWAGLP YTDIAYKVMH
AFIGDEIPAD TLKSMIEDTY GTFKHDAVTP LKQLDSNHYL LELFHGPTLA FKDVALQMLG
RLLDHFLGKR NEHAVIMGAT SGDTGSAAIE GCKPCDHVDI FILHPYNRVS EVQRRQMTTV
LADNVFNIAV EGNFDDCQAI VKESFNNQDF LGGKTRLVAV NSINWARIMA QVVYYFVSAV
AVGSPHRKVS FSVPSANFGD VFAGYIAYKM GLPVNQFVVA TNANDILHRV ISKNDFSKQP
LLHTLSPSMD IVVSSNFERL LFDLYDNDGA AVEDLLKRFN NEPVHIEQPR WDKARELFDS
LSVDDDTTIE VIKEAFERTG ELLDPHTATG YRAAETCNRD KAVPMITLAT AHPAKFEDAI
VKAGFKGAPL PAHMADLMER EERFSVLPAD AEAIQAFVVG NKR
//
