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Database: UniProt
Entry: A0A164GEH8_9NOCA
LinkDB: A0A164GEH8_9NOCA
Original site: A0A164GEH8_9NOCA 
ID   A0A164GEH8_9NOCA        Unreviewed;       406 AA.
AC   A0A164GEH8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE            EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN   ORFNames=A2J03_14440 {ECO:0000313|EMBL:KZE98424.1};
OS   Rhodococcus sp. EPR-157.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZE98424.1, ECO:0000313|Proteomes:UP000077673};
RN   [1] {ECO:0000313|EMBL:KZE98424.1, ECO:0000313|Proteomes:UP000077673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPR-157 {ECO:0000313|EMBL:KZE98424.1,
RC   ECO:0000313|Proteomes:UP000077673};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:KZE98424.1}.
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DR   EMBL; LVCV01000676; KZE98424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A164GEH8; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000077673; Unassembled WGS sequence.
DR   GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
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; 3.40.50.1100; -; 2.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR044561; ACT_ThrD-II-like.
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; PS51671; ACT; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KZE98424.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077673}.
FT   DOMAIN          331..406
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   406 AA;  41522 MW;  80D7AD2B9B44C8F7 CRC64;
     MSGGLLTAQD IADAEALLGP VMRRARVVAS RILSDLTGVE VRLKCENLQR TGSFKPRGAY
     NRIAKLSAAD RENGVVAASA GNHAQGVAWA ASELGIPSTV FMPTGVSLPK LVATKAYGAE
     ITLVGSTVDE ALGHAREFAA RTGAVLIHPF DHADIVAGQA TLGTELLAQM PNVGTIVVPT
     GGGGLLAGVA AAVHLHKPGV RVVGVQAEGA AAWPASLKAG HPIAAESMST MADGIAVGLP
     GSVPFDHVVD LVDDIVTVSE DALSRALLLC VERAKLIVEP AGAAAVAALM SRDDLMLDGP
     VCAILSGGNI DPLLLTHVIT HGLRAAGRYL AVRVTISDRP GGLLSLLDVV KKLGASVVDV
     VHSRTGGQLG LEEVDVMLTV ETRGPTHRQD VLDALAASGY AVTVES
//
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