ID   A5FGT9_FLAJ1            Unreviewed;       339 AA.
AC   A5FGT9;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   SubName: Full=Threonine aldolase {ECO:0000313|EMBL:ABQ05581.1};
DE            EC=4.1.2.5 {ECO:0000313|EMBL:ABQ05581.1};
GN   OrderedLocusNames=Fjoh_2554 {ECO:0000313|EMBL:ABQ05581.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ05581.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ05581.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
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}.
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DR   EMBL; CP000685; ABQ05581.1; -; Genomic_DNA.
DR   RefSeq; WP_012024620.1; NZ_MUGZ01000022.1.
DR   AlphaFoldDB; A5FGT9; -.
DR   STRING; 376686.Fjoh_2554; -.
DR   KEGG; fjo:Fjoh_2554; -.
DR   eggNOG; COG2008; Bacteria.
DR   HOGENOM; CLU_029381_0_4_10; -.
DR   OrthoDB; 9774495at2; -.
DR   Proteomes; UP000006694; Chromosome.
DR   GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
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   Lyase {ECO:0000313|EMBL:ABQ05581.1}.
FT   DOMAIN          4..288
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   339 AA;  37333 MW;  E9F06E9FA6F03FF9 CRC64;
     MEINLISDTI TKPTYEMLQY MFNAHVGDDV YKQDPTVIEL ETRVAEFFGM EAGLFFPSGT
     MANQTAIKLH TQPGEQLIAD KYAHVFHYEG GGVSFNSGVS CCLLDGDRGM INAKQVAAAI
     NDPEFYHSPL TSLVCVENTT NKGGGACYEL QDLRDIKKVC DANNLKFHLD GARIWNALVA
     KRQNPKEFGA IFDTISVCLS KGLGAPIGSV LLGSKADIHR ALRIRKILGG GMRQVGYLAA
     AGLYALANNI ERLAEDHRRA KEIGAILSTK SWVASVEPVE TNILIFSLAE GYSDQLLIEK
     LKQKNILISS LGHNKLRIVT HLDYKEVMHT YVVETLSKI
//