ID D0Z4P1_PHODD Unreviewed; 334 AA.
AC D0Z4P1;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=Low-specificity L-threonine aldolase {ECO:0000313|EMBL:EEZ39479.1};
DE EC=4.1.2.5 {ECO:0000313|EMBL:EEZ39479.1};
GN ORFNames=VDA_000499 {ECO:0000313|EMBL:EEZ39479.1};
OS Photobacterium damselae subsp. damselae CIP 102761.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=675817 {ECO:0000313|EMBL:EEZ39479.1, ECO:0000313|Proteomes:UP000003579};
RN [1] {ECO:0000313|EMBL:EEZ39479.1, ECO:0000313|Proteomes:UP000003579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102761 {ECO:0000313|EMBL:EEZ39479.1,
RC ECO:0000313|Proteomes:UP000003579};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R., Huq A., Grim C.J., Hasan N.A., Vonstein V.,
RA Bartels D.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the threonine aldolase family.
CC {ECO:0000256|ARBA:ARBA00006966}.
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DR EMBL; ADBS01000002; EEZ39479.1; -; Genomic_DNA.
DR RefSeq; WP_005304539.1; NZ_ADBS01000002.1.
DR AlphaFoldDB; D0Z4P1; -.
DR eggNOG; COG2008; Bacteria.
DR Proteomes; UP000003579; Unassembled WGS sequence.
DR GO; GO:0004793; F:threonine aldolase activity; IEA:UniProtKB-EC.
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 Lyase {ECO:0000313|EMBL:EEZ39479.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003579}.
FT DOMAIN 2..283
FT /note="Aromatic amino acid beta-eliminating lyase/threonine
FT aldolase"
FT /evidence="ECO:0000259|Pfam:PF01212"
FT MOD_RES 196
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR017617-1"
SQ SEQUENCE 334 AA; 36286 MW; 42AB9B1B80C89950 CRC64;
MDFRSDTVTQ PTPAMREAMF SAPVGDDVYG DDPTVNELEA FAAHLAGFEA ALFTTSGTQA
NLLGIMSHCD RGDEYLCGQQ AHNYRYEAGG AAVLGSIQPQ PIENNPDGTL PFDKLAAAIK
PDDFHFARTK LLSLENTING KVLPLAYLAQ AREFTQQHNL QLHLDGARVF NAAVALDVPV
KEIAQYFDSM TICLSKGLSA PVGSLLLGSK EFIAKARRIR KMLGGGMRQA GILAAAGKLA
LTEQVKQLSV DHDNAKYLAQ ELSQLSGFHV KPELVQTNIV FAKLDENIDI SLIANQLKEN
GILVSPSNPI RFVTHKDISR DNITTLITQL KSVL
//
