ID A0A419RTA3_9SPHN Unreviewed; 416 AA.
AC A0A419RTA3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Threonine ammonia-lyase {ECO:0000313|EMBL:RJY09033.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:RJY09033.1};
GN ORFNames=D6201_06350 {ECO:0000313|EMBL:RJY09033.1};
OS Aurantiacibacter aquimixticola.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=1958945 {ECO:0000313|EMBL:RJY09033.1, ECO:0000313|Proteomes:UP000285232};
RN [1] {ECO:0000313|EMBL:RJY09033.1, ECO:0000313|Proteomes:UP000285232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSSK-14 {ECO:0000313|EMBL:RJY09033.1,
RC ECO:0000313|Proteomes:UP000285232};
RX PubMed=28820100; DOI=10.1099/ijsem.0.002055;
RA Park S., Jung Y.T., Choi S.J., Yoon J.H.;
RT "Erythrobacter aquimixticola sp. nov., isolated from the junction between
RT the ocean and a freshwater spring.";
RL Int. J. Syst. Evol. Microbiol. 67:2964-2969(2017).
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:RJY09033.1}.
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DR EMBL; RAHX01000001; RJY09033.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A419RTA3; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000285232; Unassembled WGS sequence.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:UniProtKB-EC.
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; 3.30.70.260; -; 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; 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; PF01842; ACT; 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:RJY09033.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 339..416
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 416 AA; 45047 MW; 8ACCA0B534291317 CRC64;
MTQVTQAKSA SRAEELTVQD VRDAAERIAG AVVRTPTMFS QTLSKITGAN IWLKFENLQF
TAAYKERGAL NALLQLTEEQ RQRGVIAASA GNHSQGLSYH GTRLGVPVTI VMPRTTPTVK
VMQTEQVGGN VMLEGETFDD AYAHARELEK ERGLTFVHPF DDPRVAAGAG TTALELFEDA
PEVDCIVTPI GGGGLISGMA TVAKDRDPPV EVIGVEARLF PSSYCAFKGE TLPKGGDTLA
EGIAVKEPGR FTQGVIDRLV DDILLVDEPC LEEAVSLLLQ IEKTVVEGAG AAGLAAILSY
PERFAGKNIG LVLCGGNIDT RLLANVLLRD LARSGRLARL QITLQDRPGA LFRVMREFDA
HNVNIIEIYH QRIFTNLPAK GLVTDIECEA RDKQQLDALV KALTQKGYRV SQVELN
//
