ID A0A0F0KAB9_9MICO Unreviewed; 473 AA.
AC A0A0F0KAB9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:KJL17334.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:KJL17334.1};
GN Name=thrC {ECO:0000313|EMBL:KJL17334.1};
GN ORFNames=RL72_03578 {ECO:0000313|EMBL:KJL17334.1};
OS Microbacterium azadirachtae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=582680 {ECO:0000313|EMBL:KJL17334.1, ECO:0000313|Proteomes:UP000033448};
RN [1] {ECO:0000313|EMBL:KJL17334.1, ECO:0000313|Proteomes:UP000033448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23848 {ECO:0000313|EMBL:KJL17334.1,
RC ECO:0000313|Proteomes:UP000033448};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-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:KJL17334.1}.
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DR EMBL; JYIT01000086; KJL17334.1; -; Genomic_DNA.
DR RefSeq; WP_045252432.1; NZ_JYIT01000086.1.
DR AlphaFoldDB; A0A0F0KAB9; -.
DR PATRIC; fig|582680.7.peg.3636; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000033448; 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:KJL17334.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000033448}.
FT DOMAIN 2..79
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 105..349
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 111
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 473 AA; 50813 MW; 8371BD32BAF5B1E3 CRC64;
MQYISTRGGG DPKTYSEALL EGLAVDGGLL VPEQLPTVDA ATLESWRDLG YADLATEVLG
LFATDIPRDD LAALCAAAYS PDTFAAPVPL TPIGGGITLV GLSEGPTLAF KDMAMQFLGQ
ALEYALECTG GVLNIVGATS GDTGSAAEHA LRGKERISVF MLSPQGRMSA FQRAQMYSLQ
DANVHNIAVE GVFDDCQNLV KDLAGDLDFK RAQHLGAVNS INLARITAQV VYYFWAWLRA
TDSLAPAERE GFEVSFAVPS GNFGNILSGF FARGMGLPIR RLVLAANENN VLDEFFRTGV
YRPRSAAQTL ATSSPSMDIS KASNLERFIF ELVGREPQRV VAAWDQLTLA GAFDFAADLP
RFADEFGIVS GTSTHDDRLS TIRAVYEQSG TVIDPHTADG VKVAREFLED GVPMLVLETA
KPEKFGETIT EALGIELPLS DELKALLAAP QRVTEIPNDE SALRTIIETS ALH
//
