ID C4GEU3_9NEIS Unreviewed; 470 AA.
AC C4GEU3;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EEP68748.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:EEP68748.1};
GN Name=thrC {ECO:0000313|EMBL:EEP68748.1};
GN ORFNames=GCWU000324_00652 {ECO:0000313|EMBL:EEP68748.1};
OS Kingella oralis ATCC 51147.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Kingella.
OX NCBI_TaxID=629741 {ECO:0000313|EMBL:EEP68748.1, ECO:0000313|Proteomes:UP000003009};
RN [1] {ECO:0000313|EMBL:EEP68748.1, ECO:0000313|Proteomes:UP000003009}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51147 {ECO:0000313|EMBL:EEP68748.1,
RC ECO:0000313|Proteomes:UP000003009};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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:EEP68748.1}.
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DR EMBL; ACJW02000002; EEP68748.1; -; Genomic_DNA.
DR RefSeq; WP_003794215.1; NZ_GG665871.1.
DR AlphaFoldDB; C4GEU3; -.
DR STRING; 629741.GCWU000324_00652; -.
DR GeneID; 84906996; -.
DR HOGENOM; CLU_015170_1_0_4; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000003009; Unassembled WGS sequence.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
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; 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.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:EEP68748.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000003009}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 103..336
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 113
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 470 AA; 51710 MW; 049C14147F62540D CRC64;
MNYISTRGNT PAKTFSQALL MGLAPDGGLM LPEHYPQITP AQLTHWRTLS YAELAFEVIR
LFATDIPEAD LRDIINRTYT RETFGSAEIT PVRTLKDGIK IQALSNGPTL AFKDMAMQFL
GNAFEYVLAK ENQTLNILGA TSGDTGSAAE YALRGKRGIN VFMLSPDGKM SAFQRAQMYS
LQDDNIINIA VRGMFDDCQD IVKAVQNDAE FKQRYCISTV NSINWGRIVA QVVYYIAGYL
RATESNEQRV SFCVPSGNFG NICAGHIAKQ MGVPIHRLIV ATNENNVLDE FFRTGQYSPR
DAAHTYVTSS PSMDISKASN FERFIFDLVG RDADQVQSLW ANVAQGNGFN LQDKLDIIRQ
KYGFVSGSST HADRLATIKS VYQTDGELID PHTADGIKVA RQLRESGETI VCLETALAAK
FEATIHEAVG SVAVPRPAKL AGLEDLPQRV QVIDNDADVV KAIIRNKVGG
//
