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Database: UniProt
Entry: R5EBJ2_9CLOT
LinkDB: R5EBJ2_9CLOT
Original site: R5EBJ2_9CLOT 
ID   R5EBJ2_9CLOT            Unreviewed;       405 AA.
AC   R5EBJ2;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|ARBA:ARBA00022248};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=BN724_01230 {ECO:0000313|EMBL:CCX86137.1};
OS   Clostridium sp. CAG:590.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX86137.1, ECO:0000313|Proteomes:UP000017939};
RN   [1] {ECO:0000313|EMBL:CCX86137.1, ECO:0000313|Proteomes:UP000017939}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939};
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   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004810}.
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC       pathway; propanoate from L-threonine: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004958}.
CC   -!- SUBUNIT: In the native structure, TdcB is in a dimeric form, whereas in
CC       the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).
CC       {ECO:0000256|ARBA:ARBA00011447}.
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:CCX86137.1}.
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DR   EMBL; CAXF010000050; CCX86137.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5EBJ2; -.
DR   STRING; 1262825.BN724_01230; -.
DR   UniPathway; UPA00047; UER00054.
DR   UniPathway; UPA00052; UER00507.
DR   Proteomes; UP000017939; Unassembled WGS sequence.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR   CDD; cd04886; ACT_ThrD-II-like; 1.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.30.70.260; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR045865; ACT-like_dom_sf.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR044561; ACT_ThrD-II-like.
DR   InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR   InterPro; IPR005789; Thr_deHydtase_catblc.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01127; ilvA_1Cterm; 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; SSF55021; ACT-like; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51671; ACT; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   4: Predicted;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW   Isoleucine biosynthesis {ECO:0000256|ARBA:ARBA00022624};
KW   Lyase {ECO:0000313|EMBL:CCX86137.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017939}.
FT   DOMAIN          325..405
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   405 AA;  44162 MW;  EEBCC9643A2F93B6 CRC64;
     MLTLEKFEEA YNTVQKVVKP TPLIYSDYFS EASDNKIYFK PENLQVTGAY KIRGAYYKIS
     TLSEEDRNKG LITASAGNHA QGVAFAAKAY GVKATIVMPT TTPLIKVNRT KSYGAEVILY
     GDVYDESCQY ALELAEDKGY TFIHPFDDED VACGQGSIAM EIIKELPTVD YIMVPIGGGG
     LATGVSTLAK MLNPNIKVIG VEPAGAACMK ESLKNGKVTT LPSVDTIADG TAVKTPGSKI
     FPYIQKNIDE IITVEDSELV VAFLDMMENH KLLVENSGLL TAAACKHLNV KDKKVVCILS
     GGNMDVITLA SVVQHGLFAR SRIFTVSVLL PDKPGELKNV SSIIAEMQGN IIKLEHNQFV
     SLNRNSAVEL IITLEAFGPE HKERIIQVLS EKGYRPVEKS PKNIF
//
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