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Database: UniProt
Entry: A0A0Q9YQ15_9COXI
LinkDB: A0A0Q9YQ15_9COXI
Original site: A0A0Q9YQ15_9COXI 
ID   A0A0Q9YQ15_9COXI        Unreviewed;       311 AA.
AC   A0A0Q9YQ15;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=L-threonine dehydratase catabolic TdcB {ECO:0000313|EMBL:KRG18136.1};
DE            EC=4.3.1.19 {ECO:0000313|EMBL:KRG18136.1};
GN   Name=tdcB_2 {ECO:0000313|EMBL:KRG18136.1};
GN   ORFNames=CC99x_01848 {ECO:0000313|EMBL:KRG18136.1};
OS   Candidatus Berkiella cookevillensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Berkiella.
OX   NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG18136.1, ECO:0000313|Proteomes:UP000051494};
RN   [1] {ECO:0000313|EMBL:KRG18136.1, ECO:0000313|Proteomes:UP000051494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC99 {ECO:0000313|EMBL:KRG18136.1,
RC   ECO:0000313|Proteomes:UP000051494};
RA   Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT   "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT   Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT   aquae.";
RL   Submitted (SEP-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:KRG18136.1}.
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DR   EMBL; LKHV01000009; KRG18136.1; -; Genomic_DNA.
DR   RefSeq; WP_057624960.1; NZ_LKHV02000001.1.
DR   AlphaFoldDB; A0A0Q9YQ15; -.
DR   STRING; 437022.CC99x_01848; -.
DR   PATRIC; fig|1590042.3.peg.1879; -.
DR   OrthoDB; 9811476at2; -.
DR   Proteomes; UP000051494; 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   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:SF2; CATABOLIC L-SERINE_THREONINE DEHYDRATASE; 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:KRG18136.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051494}.
FT   DOMAIN          7..292
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   311 AA;  33544 MW;  FF3D20774BBD6DF7 CRC64;
     MTSALHIHTP LLKSHPLSEL IERNVYVKMD AMQPSGSFKD RGIGKLCIHY AKQGKKGLVS
     SSAGNAGIAV AYAGHQLGLD VKVIVPTSAL LLSVSKMLSE GADVITHGHV WNDADIYARQ
     LAKELDYAYI PPFDHPIIWQ GYESIIDEFK KDKIKPDAII TSVGGGGLFT GLIQGLIKHK
     WSKVALITAE TEGAASLATS FQKKQRITLD SINTVATTLG AKQICEQAFD YLNTHPVYPQ
     VLSDKAAIHA VAAFADHHRV LVEPACGAAL AVAYQNLPVL KQFKNIAIII CGGNGVSVEL
     LNGWKQQFQV G
//
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