ID A0A098R0K6_9SPIO Unreviewed; 469 AA.
AC A0A098R0K6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KGE73484.1};
GN ORFNames=DC28_03260 {ECO:0000313|EMBL:KGE73484.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE73484.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE73484.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE73484.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KGE73484.1}.
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DR EMBL; JNUP01000024; KGE73484.1; -; Genomic_DNA.
DR RefSeq; WP_037545841.1; NZ_JNUP01000024.1.
DR AlphaFoldDB; A0A098R0K6; -.
DR STRING; 1480694.DC28_03260; -.
DR eggNOG; COG0498; Bacteria.
DR Proteomes; UP000029692; Unassembled WGS sequence.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
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 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029692}.
FT DOMAIN 2..82
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 98..203
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 242..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 469 AA; 50071 MW; 3803AA1DB9C520D5 CRC64;
MQFVSTRGGG KDAPVGFRQA VFQGLAPDGG LYHPLEEPDL SGIIRGFSPS TSFTELAFRM
TRALFSQELT EDQADQLCRR AFPFEPALSR LGPGHLLLEL FHGPSCAFKD FGASYLANVM
QTFLDGRSQR AIILTATSGD TGSAVAQAFH GKDAIDVVIL YPSGRVSPSQ EQQLTTLGGN
VHALEVQGSF DDCQSLVKQA FTDPALSKDL PLTSANSINL GRLIPQSFYY LWAASRDLES
LDPGSSAPGT SVRSASASGA SSSSPAAPRP GKSGPGTFCV PSGNFGNLTA GILARRWGMA
ADGFIAATNA NDVVPQYLET GDYQPRPSIP THANAMDVGS PSNFERMSAL FQGDFHAMAR
LIRGESSNNQ QILDTMKDYY QRQGVYLCPH TAAGVRAGDR ALKEGTAQRV ITLATAHPAK
FPEIARLATG TEPAMPQRLA DVMSRTKQAT LIDPTLEALG AFLRDSFRS
//
