ID C0CU22_9FIRM Unreviewed; 497 AA.
AC C0CU22;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Threonine synthase {ECO:0000313|EMBL:EEG57411.1};
DE EC=4.2.3.1 {ECO:0000313|EMBL:EEG57411.1};
GN Name=thrC {ECO:0000313|EMBL:EEG57411.1};
GN ORFNames=CLOSTASPAR_00471 {ECO:0000313|EMBL:EEG57411.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG57411.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG57411.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57411.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG57411.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG57411.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) 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:EEG57411.1}.
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DR EMBL; ACCJ01000021; EEG57411.1; -; Genomic_DNA.
DR RefSeq; WP_007706207.1; NZ_GG657587.1.
DR AlphaFoldDB; C0CU22; -.
DR HOGENOM; CLU_015170_3_1_9; -.
DR Proteomes; UP000004756; 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:EEG57411.1};
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 98..421
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; 54303 MW; 955F0C28A2BBBD9B CRC64;
MSLSYQSTRG GEAGVTASQA ILKGLADDGG LFMPTTIPAL DVPVERLAGM TYQETAYEVM
KLFLTDFTEE ELKGCIEKAY DSKFDTEEIA PLAKADGAYF LELYHGSTIA FKDMALSILP
HLMTTAAKKN HVDQEIVILT ATSGDTGKAA MAGFADVPGT RIIVFYPKDG VSKVQELQMR
TQKGENTSVV AIHGNFDDAQ TGVKKIFADK DLAAELADRG FQFSSANSIN IGRLVPQIVY
YVYAYAKLFE NGEIEKDETI NVTVPTGNFG NILAAYFAKR MGLPIKTLIC ASNDNKVLYD
FFTTGTYDRK REFILTNSPS MDILISSNLE RLIYLSAGCD ASVSAALMRE LSENGSYTVT
DEMRRFMEDF VGGYADQKQN ADTIRRIFKD TGYLVDTHTG VAAAVYYDYA NRTGDTAKTV
IASTASPFKF SRSVMEAVQG ADETGAMDEF AVVDALSSLS GVPVPQAVEE IRTAPVRHNL
ECDVDRMKDT VKGILKI
//
