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Database: UniProt
Entry: R8QGZ6_BACCE
LinkDB: R8QGZ6_BACCE
Original site: R8QGZ6_BACCE 
ID   R8QGZ6_BACCE            Unreviewed;       333 AA.
AC   R8QGZ6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000256|ARBA:ARBA00022248, ECO:0000256|RuleBase:RU363083};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096, ECO:0000256|RuleBase:RU363083};
DE   AltName: Full=Threonine deaminase {ECO:0000256|RuleBase:RU363083};
GN   ORFNames=IIQ_01366 {ECO:0000313|EMBL:EOP70082.1};
OS   Bacillus cereus VD118.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053231 {ECO:0000313|EMBL:EOP70082.1, ECO:0000313|Proteomes:UP000014019};
RN   [1] {ECO:0000313|EMBL:EOP70082.1, ECO:0000313|Proteomes:UP000014019}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VD118 {ECO:0000313|EMBL:EOP70082.1,
RC   ECO:0000313|Proteomes:UP000014019};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus VD118.";
RL   Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC       ammonia from threonine in a two-step reaction. The first step involved
CC       a dehydration of threonine and a production of enamine intermediates
CC       (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC       Both intermediates are unstable and short-lived. The second step is the
CC       nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC       ketobutyrate and free ammonia. In the low water environment of the
CC       cell, the second step is accelerated by RidA.
CC       {ECO:0000256|ARBA:ARBA00025527, ECO:0000256|RuleBase:RU363083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC         ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC         Evidence={ECO:0000256|RuleBase:RU363083};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU363083};
CC   -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC       pathway; propanoate from L-threonine: step 1/4.
CC       {ECO:0000256|ARBA:ARBA00004958, ECO:0000256|RuleBase:RU363083}.
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, ECO:0000256|RuleBase:RU363083}.
CC   -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC       {ECO:0000256|RuleBase:RU363083}.
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:EOP70082.1}.
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DR   EMBL; AHEZ01000045; EOP70082.1; -; Genomic_DNA.
DR   RefSeq; WP_016104862.1; NZ_KB976798.1.
DR   AlphaFoldDB; R8QGZ6; -.
DR   PATRIC; fig|1053231.3.peg.2585; -.
DR   HOGENOM; CLU_021152_4_2_9; -.
DR   UniPathway; UPA00052; UER00507.
DR   Proteomes; UP000014019; Unassembled WGS sequence.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR   CDD; cd01562; Thr-dehyd; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   Lyase {ECO:0000256|RuleBase:RU363083};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU363083};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU363083}.
FT   DOMAIN          22..311
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   333 AA;  35709 MW;  03ADB12350653732 CRC64;
     MITSKLPLHI ADIKKAQKIL DRNVRKTPLV KSFYLTSKTG GEIHLKLENM QLTGSFKFRG
     AFNKMSQLTE QEKEKGVIAC SAGNHAQGVA LSAHLLGIKS KIVMPISAPL AKVEATRGYG
     SEVVLYGETF DDAKAKCEEI IRETGETYLH PYDDVEVMAG QGTIGLDILD DMWDVDTVIV
     PIGGGGIISG IAVALKSFNP SINIIGVQAE NVHGMKASYD KGTIVEHYEA PTIADGCAVK
     IPGNLTFEVV KELVDDIVTV SEEELEVAMK DLLQRGKAVV EGAGALATAA LLAGKVDQYI
     KGKKVVAVIS GGNVDLQRIS SVCEHFFVAN EVK
//
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