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Database: UniProt
Entry: A0A1F9KHC3_9DELT
LinkDB: A0A1F9KHC3_9DELT
Original site: A0A1F9KHC3_9DELT 
ID   A0A1F9KHC3_9DELT        Unreviewed;       359 AA.
AC   A0A1F9KHC3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:OGQ80048.1};
GN   ORFNames=A3F90_06005 {ECO:0000313|EMBL:OGQ80048.1};
OS   Deltaproteobacteria bacterium RIFCSPLOWO2_12_FULL_60_19.
OC   Bacteria; Deltaproteobacteria.
OX   NCBI_TaxID=1797894 {ECO:0000313|EMBL:OGQ80048.1, ECO:0000313|Proteomes:UP000177611};
RN   [1] {ECO:0000313|EMBL:OGQ80048.1, ECO:0000313|Proteomes:UP000177611}
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:OGQ80048.1}.
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DR   EMBL; MGSS01000107; OGQ80048.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F9KHC3; -.
DR   STRING; 1797894.A3F90_06005; -.
DR   Proteomes; UP000177611; 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          7..289
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   359 AA;  38611 MW;  EF09EC5CA2FEE81A CRC64;
     MAATPIDLRS DTVTKPSPEM RRAMAEAEVG DDVFMEDPTV NRLQARAAEI FGREAALFVP
     SGSMGNLVCL IAHTRPGQEV ICDENAHIYS YEMAAMAGVA GLLPRLVPGE DGILTWEQIS
     RAIRPRMYAR AQTALVCLEN THNMAGGTVY PTRLAQEICE RAHEAGLLVH LDGSRIFNAA
     TFLHEHVRGM TGKFDSVQFC LSKGLGAPVG SMIVGSGALI ERCRSIRKLL GGGMRQAGVL
     AAAGLIALEK GPQRLGIDHE NATLLAHELA RMPGIRLNPA KVQTNIVIYD VRETGLSSAE
     FLAESARRGV LGVPVDRDKI RMVTHLDVSR ADVERVAAAI CELAESLSLS RASAPMKNA
//
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