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Database: UniProt
Entry: A0A101IEY8_9CHLR
LinkDB: A0A101IEY8_9CHLR
Original site: A0A101IEY8_9CHLR 
ID   A0A101IEY8_9CHLR        Unreviewed;       348 AA.
AC   A0A101IEY8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   13-SEP-2023, entry version 24.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KUK93933.1};
GN   ORFNames=XE06_0899 {ECO:0000313|EMBL:KUK93933.1};
OS   Anaerolineaceae bacterium 46_22.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae.
OX   NCBI_TaxID=1635294 {ECO:0000313|EMBL:KUK93933.1, ECO:0000313|Proteomes:UP000054480};
RN   [1] {ECO:0000313|Proteomes:UP000054480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT   Other Microbial Community Members in Biogeochemical Transformations in Oil
RT   Reservoirs.";
RL   MBio 7:e01669-15(2015).
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}.
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:KUK93933.1}.
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DR   EMBL; LGHA01000092; KUK93933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101IEY8; -.
DR   PATRIC; fig|1635294.3.peg.499; -.
DR   Proteomes; UP000054480; Unassembled WGS sequence.
DR   GO; GO:0016829; F:lyase activity; IEA:InterPro.
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; IPR023603; Low_specificity_L-TA-like.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; NF041359; GntG_guanitoxin; 1.
DR   PANTHER; PTHR48097:SF9; L-THREONINE ALDOLASE; 1.
DR   PANTHER; PTHR48097; L-THREONINE ALDOLASE-RELATED; 1.
DR   Pfam; PF01212; Beta_elim_lyase; 1.
DR   PIRSF; PIRSF017617; Thr_aldolase; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
FT   DOMAIN          5..289
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         202
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   348 AA;  37509 MW;  46FB95E32AEC902E CRC64;
     MKWIDLRSDT VTLPTHRMRE AMANAELGDD VYGEDPTVNR LQRMAAERLG KEDALFVPSG
     TMGNLIAVLA NCGRGDEVIM GDCAHTFLYE AGGISALGGV HPHLIPNNPD GTLSIQDIKD
     AVRKDDIHFP KSKLLILENT HNRCGGVSLS RDYMLEAADT AHQSSLSVHL DGARIFNAAV
     DQGISAHELT EMVDSVTFCL SKGLCAPVGS VLCGSKAFIQ EALRLRKQLG GGMRQAGVLA
     AAGIVALEEM VDRLAEDHHR AEMLAEALSS IPDVALDKGS PNTNMVYINL DPALGISAKA
     CSENLKKQGV LAGITGSYHF RMVCHYWIKD EDIPVVRSAL EKSIKSPQ
//
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