ID Q0S4B3_RHOJR Unreviewed; 410 AA.
AC Q0S4B3;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=threonine ammonia-lyase {ECO:0000256|ARBA:ARBA00012096};
DE EC=4.3.1.19 {ECO:0000256|ARBA:ARBA00012096};
GN OrderedLocusNames=RHA1_ro05846 {ECO:0000313|EMBL:ABG97623.1};
OS Rhodococcus jostii (strain RHA1).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG97623.1, ECO:0000313|Proteomes:UP000008710};
RN [1] {ECO:0000313|Proteomes:UP000008710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA Eltis L.D.;
RT "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT catabolic powerhouse.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR EMBL; CP000431; ABG97623.1; -; Genomic_DNA.
DR RefSeq; WP_011597945.1; NC_008268.1.
DR AlphaFoldDB; Q0S4B3; -.
DR KEGG; rha:RHA1_ro05846; -.
DR PATRIC; fig|101510.16.peg.5886; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_1_11; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000008710; Chromosome.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
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; IPR045865; ACT-like_dom_sf.
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; SSF55021; ACT-like; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR PROSITE; PS51671; ACT; 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 Lyase {ECO:0000313|EMBL:ABG97623.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000008710}.
FT DOMAIN 335..410
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 410 AA; 42399 MW; F94118346503C161 CRC64;
MLARVEPVTL DQIRAARKLL DPVMRRTPVI ASRALSERCG HVVSLKCENL QRTGSFKPRG
AYNRIANLSV AERACGVVAA SAGNHAQGVA WAATELGIPS TVFMPTGAPL PKLVATKAYG
ATVHLTGDTV DDALVAAKEF ANETGAVLIH PFDHVDIVAG QGTVGLEILE QEPDVGTLVV
PTGGGGLIAG IAAAVKATRP DVRIVGVQAE QAAAWPRSLA EGRPIPLETM STMADGIAVG
RPGDVPFAHV GSQVDAIVTV SEDALSRALL LCLERAKLIV EPAGAAAVAA LISCSTDELG
LTGKVCAVLS GGNIDPLLLT HVVNHGLRAA GRYLGVHVTI PDRPGGLVSL LGVISGNGAS
VVDVVHSRTG GALALDEVEV FLTVETRGPG HRQDLLDALR DAQYTIRLQE
//
