ID A0A0J9E760_9RHOB Unreviewed; 325 AA.
AC A0A0J9E760;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Threonine dehydratase, catabolic {ECO:0000313|EMBL:KMW58541.1};
DE EC=4.3.1.19 {ECO:0000313|EMBL:KMW58541.1};
GN ORFNames=AIOL_003518 {ECO:0000313|EMBL:KMW58541.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW58541.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW58541.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW58541.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-2015) 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:KMW58541.1}.
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DR EMBL; LFTY01000002; KMW58541.1; -; Genomic_DNA.
DR RefSeq; WP_049644135.1; NZ_LFTY01000002.1.
DR AlphaFoldDB; A0A0J9E760; -.
DR STRING; 1675527.AIOL_003518; -.
DR PATRIC; fig|1675527.3.peg.3678; -.
DR OrthoDB; 9811476at2; -.
DR Proteomes; UP000037178; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd01562; Thr-dehyd; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
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 4: Predicted;
KW Lyase {ECO:0000313|EMBL:KMW58541.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT DOMAIN 17..307
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 325 AA; 33408 MW; 0D965EB9775BF6EE CRC64;
MNIEMIEAAA ARLDGVARRT PLLSSPFLDE IAGRRVLIKP ECLQHTGSFK FRGGYNSVAA
IDPETRARGV IAYSSGNHAQ GAALGARLHG VPAVIVMPQD APAIKLANTA ALGAEVVTYD
RVGGESREAI GEALATERGL TLIRPYDHPE VIAGQGTTGL EIAAQATEHG VTEADVLVCC
GGGGLTSGIA LALEAKAPGL KVRPVEPEGF DDVKRSLASG QVVTNNTQTG SLCDAVLTPA
PGELTFPIMQ RLCGPGMAVT DEDALRAMAE AFNRLKIVAE PGGAVALAAA LYHAAEVEGD
AVIVVVSGGN VDPAVFQRAL AGFSD
//
