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Database: UniProt
Entry: A0A0Q5UH82_9FLAO
LinkDB: A0A0Q5UH82_9FLAO
Original site: A0A0Q5UH82_9FLAO 
ID   A0A0Q5UH82_9FLAO        Unreviewed;       341 AA.
AC   A0A0Q5UH82;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:KQS45773.1};
GN   ORFNames=ASG38_14235 {ECO:0000313|EMBL:KQS45773.1};
OS   Flavobacterium sp. Leaf359.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1736351 {ECO:0000313|EMBL:KQS45773.1, ECO:0000313|Proteomes:UP000051024};
RN   [1] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf359 {ECO:0000313|Proteomes:UP000051024};
RA   Vorholt J.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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:KQS45773.1}.
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DR   EMBL; LMPW01000015; KQS45773.1; -; Genomic_DNA.
DR   RefSeq; WP_056073304.1; NZ_LMPW01000015.1.
DR   AlphaFoldDB; A0A0Q5UH82; -.
DR   STRING; 1736351.ASG38_14235; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000051024; 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:UP000051024}.
FT   DOMAIN          5..286
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;  38015 MW;  410734D1FC33BDFE CRC64;
     MEINLVSDTV TKPTNEMLQQ MFSSKVGDDV YKQDPTVNEL EEMVASIFGM EAALFFPSGT
     MANQTAIKLH TNPGEQIICD KWSHIFHYEG GGASFNSGVS CCLVDGKRGM ITAEQVRESI
     NPPEFYHSPL TSLVSIENTT NKGGGACYEI EELAKIKEVC KENNLKYHLD GARLWNALVA
     KRQNPKHFGE LFDTISVCLS KGLGAPVGSV LLGSKETMDR ALRIRKMLGG GMRQAGYLAG
     AGIYALKHNV SRLQEDHNKA KELAYILKQL PWVESVEPLE TNILIFAVKP QYNEDVVIEK
     LKQKNIFISS LGKGKLRIVT HLDYRDVMHT YVIETLQKLT F
//
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