ID A0A2S9KGH3_9BURK Unreviewed; 476 AA.
AC A0A2S9KGH3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:PRD69538.1};
GN ORFNames=C6P61_05570 {ECO:0000313|EMBL:PRD69538.1};
OS Malikia spinosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Malikia.
OX NCBI_TaxID=86180 {ECO:0000313|EMBL:PRD69538.1, ECO:0000313|Proteomes:UP000238326};
RN [1] {ECO:0000313|EMBL:PRD69538.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=83 {ECO:0000313|EMBL:PRD69538.1};
RA Suzuki S., Ishii S., Walworth N., Bird L., Kuenen J.G., Nealson K.H.;
RT "Comparative genomics illustrates the genes involved in a hyperalkaliphilic
RT mechanisms of Serpentinomonas isolated from highly-alkaline calcium-rich
RT serpentinized springs.";
RL Submitted (MAR-2018) 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:PRD69538.1}.
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DR EMBL; PVLR01000013; PRD69538.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9KGH3; -.
DR OrthoDB; 9763107at2; -.
DR Proteomes; UP000238326; Unassembled WGS sequence.
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};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51}.
FT DOMAIN 2..83
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 93..338
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 117
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 476 AA; 52444 MW; 48F422EAAE8C3BB6 CRC64;
MRYLSTRGHA ERKRFCEILL EGLAPDGGLY LPESYPQVDG ATLDAWRKIL REQGYAALAY
QVLSLYIDDI PADDLRALCA KTYTEQVFGT QEIVPLRKLE DGLLIEALSN GPTLAFKDMA
MQLLGNLFEY ELARRGEQLN ILGATSGDTG SAAEYAMRGK QGVRVFMTSP NGRMSPFQQA
QMFSLLDANI HNIAIDGVFD DCQDIVKAVS NDLEFKRQYK IGTVNSINWA RLLAQVVYYF
AGYLYATESN AQKVSFTVPS GNFGNVCAGH VARMMGLPID QLVVATNEND VLDEFFRTGI
YRVRGSADTF ETSSPSMDIS KASNFERFVF DLLGRDGARV KALFGDALNR DGRFDLSADP
QFAQAAARYG FVSGKSTHAN RLDTIRDTYQ RFGQMIDTHT ADGVKVAREH LSAGVPMIVL
ETALPIKFAG TIVEALGQEP SRPAKFDGIE ALPKRVLVMP ADVAQVKAYI VAHCAD
//