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Database: UniProt
Entry: A0A0Q1BML7_9SPHI
LinkDB: A0A0Q1BML7_9SPHI
Original site: A0A0Q1BML7_9SPHI 
ID   A0A0Q1BML7_9SPHI        Unreviewed;       341 AA.
AC   A0A0Q1BML7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KQC02348.1};
GN   ORFNames=AQF98_01865 {ECO:0000313|EMBL:KQC02348.1};
OS   Pedobacter sp. Hv1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1740090 {ECO:0000313|EMBL:KQC02348.1, ECO:0000313|Proteomes:UP000050543};
RN   [1] {ECO:0000313|EMBL:KQC02348.1, ECO:0000313|Proteomes:UP000050543}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hv1 {ECO:0000313|EMBL:KQC02348.1,
RC   ECO:0000313|Proteomes:UP000050543};
RA   Ott B.M., Beka L., Graf J., Rio R.;
RT   "Draft Genome Sequence of a Pedobacter sp. Strain Hv1, an Isolate From
RT   Medicinal Leech Mucosal Castings.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KQC02348.1}.
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DR   EMBL; LLWP01000001; KQC02348.1; -; Genomic_DNA.
DR   RefSeq; WP_055130217.1; NZ_LLWP01000001.1.
DR   AlphaFoldDB; A0A0Q1BML7; -.
DR   STRING; 1740090.AQF98_01865; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000050543; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000050543}.
FT   DOMAIN          5..289
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         201
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   341 AA;  36663 MW;  74792BE5E96C5E0B CRC64;
     MDKIDFRSDT VTKPTPGMLD AMMNAKVGDD VFGEDETVNA LEEKLAGLFN MEAALFCPSG
     TMSNQIAIKC FTQPMDEVIC DQTAHVYRYE GGGIAYNSLA SVRLLNGERG ILTPELIEPE
     INADNVHYPN SSLVVLENTV NKGGGKCYQL SQIEPIHHLC AIKGIKLHLD GARIFNALVA
     TGDKAANYGK YFDGISVCLS KGLGAPVGSV LLSSKETINK ARRIRKVLGG GMRQAGFLAA
     AGIYALDHHV TRLATDHQHA KALATALTQT NYVSAVTPVE TNIVLFDVRN GLKSDQVVKA
     LGAKGILCNS TSDKTIRFVT HLDLSSSLID RAITTISQLN L
//
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