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Database: UniProt
Entry: A0A316AAF7_9BACT
LinkDB: A0A316AAF7_9BACT
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ID   A0A316AAF7_9BACT        Unreviewed;       335 AA.
AC   A0A316AAF7;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=L-threonine aldolase {ECO:0000313|EMBL:PWJ54532.1};
GN   ORFNames=CLV98_11770 {ECO:0000313|EMBL:PWJ54532.1};
OS   Dyadobacter jejuensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC   Dyadobacter.
OX   NCBI_TaxID=1082580 {ECO:0000313|EMBL:PWJ54532.1, ECO:0000313|Proteomes:UP000245880};
RN   [1] {ECO:0000313|EMBL:PWJ54532.1, ECO:0000313|Proteomes:UP000245880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100346 {ECO:0000313|EMBL:PWJ54532.1,
RC   ECO:0000313|Proteomes:UP000245880};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (MAR-2018) 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:PWJ54532.1}.
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DR   EMBL; QGDT01000017; PWJ54532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316AAF7; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000245880; 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:UP000245880}.
FT   DOMAIN          3..288
FT                   /note="Aromatic amino acid beta-eliminating lyase/threonine
FT                   aldolase"
FT                   /evidence="ECO:0000259|Pfam:PF01212"
FT   MOD_RES         200
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ   SEQUENCE   335 AA;  36944 MW;  904712DECCD9B50F CRC64;
     MIDLRSDTVT RPTPAMKEAM WSASVGDDVY GEDPTVNALE QKVANMFGME KALFCASGTM
     TNQLAIRVHC EPGSDVICEK DSHIYLYEGG GVMVNAQASV RLLTGDKGRL NAGQIAETIS
     PENDIHNTYT RLVSLENTMN KGGGSYYDFD EILKIQKVCN ERRVALHLDG ARLFNAIVET
     NTPLKDYGQA FDSISICLSK GLGCPVGSLL LGTEAFIHKA LRFRKMMGGG WRQAGMLAAA
     GIYALDHHVE RLKDDHRRAL ALAELFSRQP EVSYIYPVQT NIVILKLQDG LDAQAYVDSL
     AKRGVLAIDF GKNLVRLVTH LDFSDDQLNW LSDQL
//
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