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Database: UniProt
Entry: A0A1G3R0D0_9SPIR
LinkDB: A0A1G3R0D0_9SPIR
Original site: A0A1G3R0D0_9SPIR 
ID   A0A1G3R0D0_9SPIR        Unreviewed;       350 AA.
AC   A0A1G3R0D0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OHD72308.1};
GN   ORFNames=A2V99_13925 {ECO:0000313|EMBL:OHD72308.1};
OS   Spirochaetes bacterium RBG_16_67_19.
OC   Bacteria; Spirochaetota.
OX   NCBI_TaxID=1802196 {ECO:0000313|EMBL:OHD72308.1, ECO:0000313|Proteomes:UP000177018};
RN   [1] {ECO:0000313|EMBL:OHD72308.1, ECO:0000313|Proteomes:UP000177018}
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:OHD72308.1}.
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DR   EMBL; MIBK01000189; OHD72308.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G3R0D0; -.
DR   STRING; 1802196.A2V99_13925; -.
DR   Proteomes; UP000177018; 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          8..290
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         203
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   350 AA;  37654 MW;  CA6CFF0EFBBA474C CRC64;
     MSAVLPIDLR SDTVTRPTQA MRRAMSEAEV GDDVLGEDPT VNTLEAEAAE RLGKEAALLV
     PSGTFGNQLA LFTHCPRGSE VVLSDDSHIV QHEAGASAII AGVQLRVFNP ADGLPRWEEI
     RARIRYSDDI HVPPTSLVAL ENALSNGMVM SLEEMEKIGG GARACGVPVH VDGARIFNAA
     TSLGLEASAL AAPADSVMFC LSKGLCAPVG SLLTGRRAFI ALARRRRKIM GGGMRQAGVL
     AAAGLVALRQ MTLRLAEDHE KARLLGEAFA KTGLFEVAPY PVRINMLFVR FRGEHAGREA
     RLVEELARRG VWSYPPFDGW IRFVTHHDVP PERLQKACRI VEEAAAAAVA
//
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