ID D3Q4K0_STANL Unreviewed; 418 AA.
AC D3Q4K0;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:ADD40160.1};
GN OrderedLocusNames=Snas_0445 {ECO:0000313|EMBL:ADD40160.1};
OS Stackebrandtia nassauensis (strain DSM 44728 / CIP 108903 / NRRL B-16338 /
OS NBRC 102104 / LLR-40K-21).
OC Bacteria; Actinomycetota; Actinomycetes; Glycomycetales; Glycomycetaceae;
OC Stackebrandtia.
OX NCBI_TaxID=446470 {ECO:0000313|EMBL:ADD40160.1, ECO:0000313|Proteomes:UP000000844};
RN [1] {ECO:0000313|EMBL:ADD40160.1, ECO:0000313|Proteomes:UP000000844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44728 / CIP 108903 / NRRL B-16338 / NBRC 102104 /
RC LLR-40K-21 {ECO:0000313|Proteomes:UP000000844};
RX PubMed=21304662; DOI=10.4056/sigs.47643;
RA Munk C., Lapidus A., Copeland A., Jando M., Mayilraj S.,
RA Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H., Cheng J.F.,
RA Han C., Detter J.C., Bruce D., Goodwin L., Chain P., Pitluck S., Goker M.,
RA Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Stackebrandtia nassauensis type strain (LLR-
RT 40K-21).";
RL Stand. Genomic Sci. 1:292-299(2009).
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}.
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DR EMBL; CP001778; ADD40160.1; -; Genomic_DNA.
DR RefSeq; WP_013015731.1; NC_013947.1.
DR AlphaFoldDB; D3Q4K0; -.
DR STRING; 446470.Snas_0445; -.
DR KEGG; sna:Snas_0445; -.
DR eggNOG; COG0498; Bacteria.
DR HOGENOM; CLU_028142_4_1_11; -.
DR OrthoDB; 9778118at2; -.
DR Proteomes; UP000000844; Chromosome.
DR GO; GO:1901605; P:alpha-amino acid metabolic process; IEA:UniProt.
DR CDD; cd01563; Thr-synth_1; 1.
DR Gene3D; 3.40.50.1100; -; 2.
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; PTHR48078:SF6; ACT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48078; THREONINE DEHYDRATASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000000844}.
FT DOMAIN 81..387
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT MOD_RES 118
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR604450-51"
SQ SEQUENCE 418 AA; 44125 MW; CE7B6C17BCF16752 CRC64;
MTTTSVFTDS PAVGLVCRGC SATYPLAAQH ACWECFGPLE VDYDATALAK VTREQIESGP
DNIWRYAALL PAGVDAATRV TLNPGMTPLV KADNLAAELG MKALWVKDDS ANPTHSFKDR
VVSVALTAAS QLGFDRFACA STGNLANSVA AHAARAGKPS IVFIPYDLEP GKVITTAVYG
GQLVAIEGSY DDVNRLCSEL TETDEFENTA FVNVNVRPFY AEGSKTLGYE VAEQLGWRLP
RQVVIPMASG ELLTKVDKAF TEMGEIGLVD PSEVKVFGAQ SSGCNPIATA LRAGTDEITP
VKPTGIAKSL NIGDPAAGPY AIESVRRTGG WMADVDDDEI REGIRLLART TGVFAETAGG
VVVATLKKLL AEGRLDPEAE TVIYNTGEGL KTLDAVTAGP THQVKPSLKS VKEAGLLS
//
