ID C1CAB2_STRP7 Unreviewed; 494 AA.
AC C1CAB2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:ACO17180.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:ACO17180.1};
GN Name=thrC {ECO:0000313|EMBL:ACO17180.1};
GN OrderedLocusNames=SP70585_2157 {ECO:0000313|EMBL:ACO17180.1};
OS Streptococcus pneumoniae (strain 70585).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=488221 {ECO:0000313|EMBL:ACO17180.1, ECO:0000313|Proteomes:UP000002211};
RN [1] {ECO:0000313|Proteomes:UP000002211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70585 {ECO:0000313|Proteomes:UP000002211};
RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107;
RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J.,
RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R.,
RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D.,
RA Rappuoli R., Moxon E.R., Masignani V.;
RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and
RT closely related species.";
RL Genome Biol. 11:R107.1-R107.19(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000918; ACO17180.1; -; Genomic_DNA.
DR RefSeq; WP_000177173.1; NC_012468.1.
DR AlphaFoldDB; C1CAB2; -.
DR KEGG; snm:SP70585_2157; -.
DR HOGENOM; CLU_015170_3_1_9; -.
DR Proteomes; UP000002211; Chromosome.
DR GO; GO:0004795; F:threonine synthase activity; IEA:UniProtKB-EC.
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; PTHR43515; THREONINE SYNTHASE-LIKE 1; 1.
DR PANTHER; PTHR43515:SF1; THREONINE SYNTHASE-LIKE 1; 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:0000313|EMBL:ACO17180.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51}.
FT DOMAIN 5..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 101..413
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 494 AA; 53752 MW; F346CB538CE698BA CRC64;
MTLVYQSTRD ANNTVTASQA ILQGLATDGG LFTPVTYPKV DLNFDKLKDA SYQEVAKLVL
SAFLDDFTVE ELDYCINNAY DSKFDTPAIA PLVKLDGQYN LELFHGSTIA FKDMALSILP
YFMTTAAKKH GLENKIVILT ATSGDTGKAA MAGFANVPGT EIIVFYPKDG VSKIQELQMT
TQTGDNTHVI AIDGNFDDAQ TNVKHMFNDV ALREKLTTNK LQFSSANSMN IGRLVPQIVY
YVYAYAQLVK TGEIVAGEKV NFTVPTGNFG NILAAFYAKQ IGLPVGKLIC ASNDNNVLTD
FFKTRVYDKK REFKVTTSPS MDILVSSNLE RLIFHLLGNN AEKTTELMNA LNTQGQYKLT
DFDAEILDLF AAEYATEEET AAEIKRVCEL DSYIEDPHTA VASAVYKKYQ SATGDVTKTV
IASTASPYKF PVVAVEAVTG KAGLTDFEAL AQLHEISGVA VPPAVDGLEI APIRHKTTVA
AADMQAAVEA YLGL
//
