ID R5IXQ7_9CLOT Unreviewed; 498 AA.
AC R5IXQ7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Threonine synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN757_01714 {ECO:0000313|EMBL:CCY41491.1};
OS Clostridium sp. CAG:7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262832 {ECO:0000313|EMBL:CCY41491.1, ECO:0000313|Proteomes:UP000018268};
RN [1] {ECO:0000313|EMBL:CCY41491.1, ECO:0000313|Proteomes:UP000018268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:7 {ECO:0000313|Proteomes:UP000018268};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY41491.1}.
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DR EMBL; CAYE010000060; CCY41491.1; -; Genomic_DNA.
DR AlphaFoldDB; R5IXQ7; -.
DR STRING; 1262832.BN757_01714; -.
DR Proteomes; UP000018268; 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; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR604450-51};
KW Reference proteome {ECO:0000313|Proteomes:UP000018268}.
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 498 AA; 54335 MW; 736DBD57029520BB CRC64;
MALSYESTRG GQKGVTASQA ILKGLAEDGG LFMPTEIPKL DKTLEQLAGM TYQETAYEVM
KLFLTDYTEE ELKSCIANAY DDKFDTEEIA PLAKADGAYF LELYHGSTIA FKDMALSILP
HLMTTAAKKN HADKEIVILT ATSGDTGKAA MAGFADVPGT RIIVFYPKGG VSKVQELQMR
TQKGDNTSVV AIHGNFDDAQ TGVKKLFGNK ELEKEMAEAG FQFSSANSIN IGRLVPQVVY
YVYAYAKLLE NEQIENGEEI NVVVPTGNFG NILAAYFAKH MGVPIKTLIC ASNDNKVLYD
FFTTGTYDRK REFILTNSPS MDILISSNLE RLIYLSTGCD AAADAALMKD LSEKGSYTVT
ENMRQFMSDF RGGFATEAQN EATIRKIFED TGYLIDTHTG VAATVYNAYK AETGDQTKTV
IASTASPYKF SHSVLEAIKG KSAVEGKDEF AVVDELSEVS GTQVPKAVEE LRSAVIRHNT
ECDVDKMGET VKNILGIA
//
