ID A0A099BU89_9BACT Unreviewed; 397 AA.
AC A0A099BU89;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN ORFNames=HMPREF0671_09410 {ECO:0000313|EMBL:KGI59836.1};
OS Prevotella sp. S7 MS 2.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1287488 {ECO:0000313|EMBL:KGI59836.1, ECO:0000313|Proteomes:UP000029732};
RN [1] {ECO:0000313|EMBL:KGI59836.1, ECO:0000313|Proteomes:UP000029732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S7 MS 2 {ECO:0000313|EMBL:KGI59836.1,
RC ECO:0000313|Proteomes:UP000029732};
RA McCorrison J., Sanka R., Torralba M., Gillis M., Haft D.H., Methe B.,
RA Sutton G., Nelson K.E.;
RL Submitted (JUL-2014) 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 -!- 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:KGI59836.1}.
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DR EMBL; JRPT01000054; KGI59836.1; -; Genomic_DNA.
DR RefSeq; WP_036899749.1; NZ_JRPT01000054.1.
DR AlphaFoldDB; A0A099BU89; -.
DR eggNOG; COG1171; Bacteria.
DR UniPathway; UPA00047; UER00054.
DR Proteomes; UP000029732; 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:0006567; P:threonine catabolic process; IEA:InterPro.
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; PF13291; ACT_4; 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 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000029732}.
FT DOMAIN 325..397
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 397 AA; 42983 MW; 651DA5F21B11AC1E CRC64;
MLELENFRKA RKVLSEVIRP TNLVHAYNVN PECDVYLKPE CLQKTGSFKI RGAYYMISQL
SEAERQKGVI SCSAGNHAQG VVLGASAMGV KSLICLPEGA PFSKVEATRQ MGAEICLVPG
VYDDAYQRAL QLRDELGYTF VHPFNDENVI AGQGTVGLEI LDQLPDVEAV IVPVGGGGLI
SGIAYAVKSL RPDIKVYGVQ AEGAASMVQS LRNGKPERLA SVSTVADGIA VKEPGSLTFD
ICSKYVDDVV TVNEDEICAA ILHLIEREKL VAEGAGAVSV AAVMYNKVPV KGKKTICIVS
GGNIDLTILN RVIYRGQVKT GRLCTFDIEL DDQPGKLVEV SSIIANLGAN VTGVQHDRSI
NRQKVNACIL RVTIETRNHE QIEQIMNALR ERGYKLI
//
