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Database: UniProt
Entry: A0A136MCS4_9BACT
LinkDB: A0A136MCS4_9BACT
Original site: A0A136MCS4_9BACT 
ID   A0A136MCS4_9BACT        Unreviewed;       462 AA.
AC   A0A136MCS4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Threonine synthase {ECO:0000313|EMBL:KXK31673.1};
DE            EC=4.2.3.1 {ECO:0000313|EMBL:KXK31673.1};
GN   Name=thrC {ECO:0000313|EMBL:KXK31673.1};
GN   ORFNames=UZ16_OP3001002781 {ECO:0000313|EMBL:KXK31673.1};
OS   Candidatus Hinthialibacteria bacterium OLB16.
OC   Bacteria; Candidatus Hinthialibacterota.
OX   NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK31673.1, ECO:0000313|Proteomes:UP000070296};
RN   [1] {ECO:0000313|EMBL:KXK31673.1, ECO:0000313|Proteomes:UP000070296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB16 {ECO:0000313|EMBL:KXK31673.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-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:KXK31673.1}.
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DR   EMBL; LMZT01000141; KXK31673.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136MCS4; -.
DR   STRING; 1617433.UZ16_OP3001002781; -.
DR   PATRIC; fig|1617433.3.peg.2985; -.
DR   Proteomes; UP000070296; Unassembled WGS sequence.
DR   GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
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:KXK31673.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR604450-51}.
FT   DOMAIN          6..83
FT                   /note="Threonine synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14821"
FT   DOMAIN          95..386
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   MOD_RES         110
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ   SEQUENCE   462 AA;  50648 MW;  6EE0701979305F5C CRC64;
     MKPLLFYSTN GHSPQVDLRT ALIQGQAPDR GLYLPVSIPT LPQEEIREFA SLSYAEIASR
     ILSRYTGGIL DESVLQDLCW DAYDYPVPVE KVYGRVHVLR LDRGPTASFK ELAARMMARL
     IGRFVQEEGG SLNILTATSG DTGSAVASAF HNVPGIRVLV LFPIDEVSDR QRKQMTTLGG
     NIATLAVDGK FDDCQALVKQ AFADPSLSEI PLSSANSINI GRLLPQSVYY FYAASRAAEP
     AEPVVFSVPS GNFGNMMGAV LAWRMGLPVR KLVVPVNAND EFPVFLASSD YHRIEPSKNC
     LSNAMNVGHP SNLARLVAVY GGCMDEKGFI HRPPDMGKMK NDLFSISVDD LETARTIRQA
     WDEHRLLLEP HGAVGWRGLQ AFLEESSDPQ TPCVSLETAT RPNFLMKSNA SWVSFLRFPS
     PFHALMACRK SMKKWMSIIR PSGTACWPIT VPGSVSPVAG VT
//
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