ID A0A3D8PFC7_9RHOB Unreviewed; 462 AA.
AC A0A3D8PFC7;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:RDW14157.1};
GN ORFNames=DIE28_04255 {ECO:0000313|EMBL:RDW14157.1};
OS Paracoccus thiocyanatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34006 {ECO:0000313|EMBL:RDW14157.1, ECO:0000313|Proteomes:UP000256679};
RN [1] {ECO:0000313|EMBL:RDW14157.1, ECO:0000313|Proteomes:UP000256679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST {ECO:0000313|EMBL:RDW14157.1,
RC ECO:0000313|Proteomes:UP000256679};
RA Ghosh W., Rameez M.J., Roy C.;
RT "Whole genome sequencing of Paracoccus thiocyanatus SST.";
RL Submitted (MAY-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:RDW14157.1}.
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DR EMBL; QFCQ01000013; RDW14157.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8PFC7; -.
DR Proteomes; UP000256679; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000256679}.
FT DOMAIN 2..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 101..398
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 112
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 462 AA; 50128 MW; D8FC84C69F4BFF97 CRC64;
MRYVSTRGRA PALDFEQAMM TGLARDGGLY LPEAMPMFSA DEIARFEGLP YEEVARRVVS
PFVGDSFSDA ELREAVARAY AGFDHVARAP LVQLAPGHHL LELFHGPTLA FKDFAMQLIG
QLFQLALARS GQRVTILGAT SGDTGSAAIE AFKGLSNVDV FIMYPHGRVS EVQRRQMSTP
ADANVHALAV DGTFDDCQAR LKDLFNDHDF RDAVGLAGVN SINWARVLAQ IVYYFSAAVS
LGAPQREVDF TVPTGNFGDV FAGSIARTMG LPIGKLVVAT NQNDILHRAL SGGEYRVGTA
RPSISPSMDI QVSSNFERAL WLAYGQDGKA VSRLMEELQS GGFAISQGAL QALRETYVSG
RASEEETMAM IATIRAETGE VICPHTAVAV KVAREHLRPG VPMISLSTAH PAKFPDAVEA
AIGIRPALPP HMADLFEREE RITRIENDVD AIKSLILERR TV
//