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Database: UniProt
Entry: A0A1F8N2Q7_9CHLR
LinkDB: A0A1F8N2Q7_9CHLR
Original site: A0A1F8N2Q7_9CHLR 
ID   A0A1F8N2Q7_9CHLR        Unreviewed;       347 AA.
AC   A0A1F8N2Q7;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   13-SEP-2023, entry version 19.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OGO05163.1};
GN   ORFNames=A2Y73_04530 {ECO:0000313|EMBL:OGO05163.1};
OS   Chloroflexi bacterium RBG_13_56_8.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797632 {ECO:0000313|EMBL:OGO05163.1, ECO:0000313|Proteomes:UP000180162};
RN   [1] {ECO:0000313|EMBL:OGO05163.1, ECO:0000313|Proteomes:UP000180162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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:OGO05163.1}.
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DR   EMBL; MGMZ01000107; OGO05163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8N2Q7; -.
DR   Proteomes; UP000180162; 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..288
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   347 AA;  36986 MW;  C8B193BD1E667758 CRC64;
     MKAIDLRSDT VTLPTPAMRK AMCDAELGDD VYGEDPTVNR LEEMTAERLG KEAALLVVSG
     TMGNLVSLLT HCGRGSEVIV GNKAHTFLYE QGGISALGSV HVHAIPNLPN GMLDPADVEN
     AIRGDNVHFP RSRVICLENT HNRCGGAVLS PGQMAIIKEI ANRHGLALHL DGARIFNAAV
     ALGIDVKEIA ALADSVQFCF SKGLAAPVGS AICGSREFIQ EARRNRKVVG GGMRQAGVIA
     AAAIVALEQM VDRLAEDHEN ARILAQGLAE IEGIEIDLAS VQSNIVIFSL ADLNVEAARV
     VEALWSEGVK MGAIDKTRIR AVTHYGIERE DITSALTAFR KVMGELI
//
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