ID A0A090VEM8_9FLAO Unreviewed; 338 AA.
AC A0A090VEM8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=L-allo-threonine aldolase {ECO:0000313|EMBL:GAL63221.1};
DE EC=2.1.2.1 {ECO:0000313|EMBL:GAL63221.1};
GN ORFNames=JCM19300_1243 {ECO:0000313|EMBL:GAL63221.1};
OS Algibacter lectus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Algibacter.
OX NCBI_TaxID=221126 {ECO:0000313|EMBL:GAL63221.1, ECO:0000313|Proteomes:UP000029644};
RN [1] {ECO:0000313|EMBL:GAL63221.1, ECO:0000313|Proteomes:UP000029644}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19300 {ECO:0000313|EMBL:GAL63221.1,
RC ECO:0000313|Proteomes:UP000029644};
RA Takatani N., Nakanishi M., Meirelles P., Mino S., Suda W., Oshima K.,
RA Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L., Niwa A.,
RA Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Algibacter lectus Strains
RT SS8 and NR4.";
RL Genome Announc. 2:e01168-14(2014).
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:GAL63221.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BBNQ01000010; GAL63221.1; -; Genomic_DNA.
DR RefSeq; WP_042505026.1; NZ_FOLN01000015.1.
DR AlphaFoldDB; A0A090VEM8; -.
DR OrthoDB; 9774495at2; -.
DR Proteomes; UP000029644; Unassembled WGS sequence.
DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000029644};
KW Transferase {ECO:0000313|EMBL:GAL63221.1}.
FT DOMAIN 4..287
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 338 AA; 37343 MW; 16851671371B6D1C CRC64;
MIIDLRSDTV TKPTKPMLDA MMQAAVGDDV FREDPTVNAL EARIANMFGK ETALFFPSGT
MANQTAIKLH TNPGDQVICD KYAHIFNYES GGASFNSGVS CNLLDVNNGI FSAQDVKQAI
NPEAYYYSKT SLVEIENTAN RRGGSCWDYN EILKIRTVCD ENNLGFHLDG ARLWHALVAK
NETTEQYGKA FDTISVCLSK GLGCPVGSVL VGDKVIMENA IRIRKIFGGN MRQAGYLAAA
GLYALDNNIE RLAEDHQKAK EIGAVLAERS IVKSVEPIET NIVIFELNNN VNEKEFTQKL
ADKNIHIISM GGNKLRMVTH LDYTNAMHDK LLSELLKL
//