ID G5KF99_9STRE Unreviewed; 497 AA.
AC G5KF99;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EHJ56406.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:EHJ56406.1};
GN Name=thrC {ECO:0000313|EMBL:EHJ56406.1};
GN ORFNames=STRUR_2243 {ECO:0000313|EMBL:EHJ56406.1};
OS Streptococcus urinalis 2285-97.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ56406.1, ECO:0000313|Proteomes:UP000005388};
RN [1] {ECO:0000313|EMBL:EHJ56406.1, ECO:0000313|Proteomes:UP000005388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2285-97 {ECO:0000313|EMBL:EHJ56406.1};
RX PubMed=24625962; DOI=10.1093/gbe/evu048;
RA Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT "Phylogenomics and the dynamic genome evolution of the genus
RT Streptococcus.";
RL Genome Biol. Evol. 6:741-753(2014).
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:EHJ56406.1}.
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; AEUZ02000001; EHJ56406.1; -; Genomic_DNA.
DR RefSeq; WP_006739166.1; NZ_AEUZ02000001.1.
DR AlphaFoldDB; G5KF99; -.
DR STRING; 764291.STRUR_2243; -.
DR eggNOG; COG0498; Bacteria.
DR Proteomes; UP000005388; Unassembled WGS sequence.
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:EHJ56406.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000005388}.
FT DOMAIN 5..80
FT /note="Threonine synthase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF14821"
FT DOMAIN 104..423
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 497 AA; 55524 MW; C2B85B5F2C735025 CRC64;
MPMLYQSTRQ ENNKVSASQA ILQGLAQDGG LFTPLEMPKL NLDFDKLKKA SYQEVAQFIL
KAFFDDFTEE EINFCVQSAY GSSFDDERIA PMTSFGQEHY LELYHGETIA FKDMALSILP
YLMTTAAKKQ GVDRKIVILT ATSGDTGKAA MAGFEDVPNT EIIVFYPKNG VSNIQELQMT
TQTGTNTHVI AIEGNFDDAQ TEVKRLFSDN TLKSTLLANN IQFSSANSMN IGRLVPQIVY
YVYAYAQLIK SNAITKGQEI NIVVPTGNFG NILASYYAKE IGLPVAKLIC ASNENNVLTD
FFKSHTYNKK RDFKLTLSPS MDILVSSNLE RLVFHLMGND AKATKKLMDQ LINDNQYQIQ
ALKQEIFDLF DAGFATEEAT KEEIKRVFKK YGYTIDPHTA VASAVYQDYL KKTKDNTPTL
IVSTASPYKF PSVVVTAIEN ERPNDDFEAV DLLNKISQVS VPKAVDSIEK REIKHHTTCA
ISEMQKAVET ILLGESN
//
