ID A0A0M2M2Y9_9MICO Unreviewed; 475 AA.
AC A0A0M2M2Y9;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KKI22147.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:KKI22147.1};
GN ORFNames=XM48_02780 {ECO:0000313|EMBL:KKI22147.1};
OS Leucobacter sp. Ag1.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=1642040 {ECO:0000313|EMBL:KKI22147.1, ECO:0000313|Proteomes:UP000033836};
RN [1] {ECO:0000313|EMBL:KKI22147.1, ECO:0000313|Proteomes:UP000033836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ag1 {ECO:0000313|EMBL:KKI22147.1,
RC ECO:0000313|Proteomes:UP000033836};
RA Pei D., Kukutla P., Yu W., Xu J.;
RT "Draft Genome Sequences of Leucobacter sp. Ag1 from Mosquito Anopheles
RT gambiae.";
RL Submitted (APR-2015) 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:KKI22147.1}.
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DR EMBL; LAYO01000068; KKI22147.1; -; Genomic_DNA.
DR RefSeq; WP_046454261.1; NZ_LAYO01000068.1.
DR AlphaFoldDB; A0A0M2M2Y9; -.
DR STRING; 1642040.XM48_02780; -.
DR PATRIC; fig|1642040.3.peg.1570; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000033836; Unassembled WGS sequence.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
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:KKI22147.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000033836}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 107..341
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 475 AA; 51328 MW; 4F07E13DD1095F3C CRC64;
MQFISTRGGL EPSEFSAILL EGLAPDGGLV VPAELPRVDA ATLESWRSLD YAGLATEVIS
RFATDIPRAD LEAMCRAAYS AENFPTEGVV PLTELDGGIT LVGLSEGPTF AFKDMAMQFL
GQSLEYVLAR TGRALNVLGA TSGDTGSAAE YALRGKDRVA VFMLSPQGRM SAFQRAQMYS
LTDDNIHNIA VEGVFDDCQN LVKELSGDLA FKQQHQLGTV NSINLGRITA QTVYYVWSWL
RASDAVAPEQ RAGFEISITV PSGNFGNILS GWYAKQLGVP LRRLVLAANE NNVLDDFFRT
GVYRPRSAAN THATSSPSMD ISKASNLERF IFELVGRDAD RLRGLWTELS ERGEFDLSHE
QARFADEFGF ASGTSTHADR VATIRAVHEA TGVTIDPHTA DGVKVAREHQ EAGVPMLVLE
TAKPAKFPEI VVEALGSAAP LPADLAAMLE LPQHVTEMAD DAEALRAFIA ERATA
//
