ID A0A1G3PSN6_9SPIR Unreviewed; 494 AA.
AC A0A1G3PSN6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:OHD57404.1};
GN ORFNames=A2Y33_07935 {ECO:0000313|EMBL:OHD57404.1};
OS Spirochaetes bacterium GWF1_51_8.
OC Bacteria; Spirochaetota.
OX NCBI_TaxID=1802190 {ECO:0000313|EMBL:OHD57404.1, ECO:0000313|Proteomes:UP000177109};
RN [1] {ECO:0000313|EMBL:OHD57404.1, ECO:0000313|Proteomes:UP000177109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR604450-51};
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:OHD57404.1}.
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DR EMBL; MIBE01000006; OHD57404.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G3PSN6; -.
DR STRING; 1802190.A2Y33_07935; -.
DR Proteomes; UP000177109; Unassembled WGS sequence.
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; IPR029144; Thr_synth_N.
DR InterPro; IPR037158; Thr_synth_N_sf.
DR InterPro; IPR004450; Thr_synthase-like.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00260; thrC; 1.
DR PANTHER; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 1.
DR Pfam; PF14821; Thr_synth_N; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51}.
FT DOMAIN 2..76
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT MOD_RES 110
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 494 AA; 55632 MW; 457D62481ED52398 CRC64;
MRYVSTRGNY PPVPSAETIR LGMVPKGGLF CPESVPEVDL FSLRGLSYHE TAFEILKLFL
TDYTDNELQY AIAEAYSPER FETMNPAPLK LLRDNLAVLE LWHGPTAAFK DLALQIMPHL
LTIAVQKQKT EKEIVILVAT SGDTGKAALE GYKDVPGTKI IVFYPKNGVS RVQELQMVTT
GGSNTYTIGV QGNFDDCQTM VKDIFGDREF NRELSDAGME FSSANSINWG RLAPQIVYYF
WAYFQMVDRR KVFMGDPVNF NVPTGNFGNI LAGYYAQQMG LPVNKFVCSS NKNKILTDFI
ADGIYDKNRQ FFSTVSPSMD ILISSNLERY LYAISGNNPE KIVRWYDDLK TKGKFKVDES
TRERVFGSLY GGFADEEQTI AEIKRVYTEE RYLVDTHTAV GFHVHRQYTA ETGDTTPTVI
DSTASPFKFN KAVYQAVTGD KSIDDEFVLL EKLQDQTGVP VHRSLAGLDK LPVRHDKVIR
IEEGRSAIKS ILKI
//
