ID U5QBY8_9BACT Unreviewed; 345 AA.
AC U5QBY8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Low specificity L-threonine aldolase {ECO:0000313|EMBL:AGY54935.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:AGY54935.1};
GN Name=ltaE {ECO:0000313|EMBL:AGY54935.1};
GN ORFNames=BRDCF_p2308 {ECO:0000313|EMBL:AGY54935.1};
OS Bacteroidales bacterium CF.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1400053 {ECO:0000313|EMBL:AGY54935.1, ECO:0000313|Proteomes:UP000017642};
RN [1] {ECO:0000313|EMBL:AGY54935.1, ECO:0000313|Proteomes:UP000017642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF {ECO:0000313|EMBL:AGY54935.1};
RX PubMed=24356833;
RA Tang S., Edwards E.A.;
RT "Complete Genome Sequence of Bacteroidales Strain CF from a Chloroform-
RT Dechlorinating Enrichment Culture.";
RL Genome Announc. 1:e01066-13(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; CP006772; AGY54935.1; -; Genomic_DNA.
DR AlphaFoldDB; U5QBY8; -.
DR STRING; 1400053.BRDCF_p2308; -.
DR KEGG; bacc:BRDCF_p2308; -.
DR HOGENOM; CLU_049619_0_0_10; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000017642; Chromosome.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06502; TA_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001597; ArAA_b-elim_lyase/Thr_aldolase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR PANTHER; PTHR48097:SF5; LOW SPECIFICITY L-THREONINE ALDOLASE; 1.
DR Pfam; PF01212; Beta_elim_lyase; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000313|EMBL:AGY54935.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017642}.
FT DOMAIN 5..292
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
SQ SEQUENCE 345 AA; 38402 MW; 3D6E1E25E102B99D CRC64;
MLHSFGSDNH SGAAPEIIEA IINANKDFSE AYGEDKTTKQ ANILFKKILG DKAESFFVFN
GTGANVVALK ALTKTHNSIL CPETAHINVD ECGAPEKATG CKLIPLTAKD GKVTPEEVKK
ELKNFGFQHH SQVKVLSISQ PTELGTLYTP QEIKELADLM HEHNCYLHID GSRISNASAA
LGLPIKNFTA DAGVDALSFG GTKNGLLIGE AVIFFKKELS EDFLYIRKQN TQLFSKNRFI
AAQFIAYLKD GLNIRLAAHS NTMAKYLEST LKEIPEIEIS RPVETNAVFA IIPQYLCNEL
LKKHLFYVWD ETTNEVRWMC SFNTTREDID TFVNDIIRIV TANKI
//