ID A0A257K791_9FLAO Unreviewed; 423 AA.
AC A0A257K791;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Aspartate aminotransferase family protein {ECO:0000313|EMBL:OYU83233.1};
GN ORFNames=CFE24_12205 {ECO:0000313|EMBL:OYU83233.1};
OS Flavobacterium sp. BFFFF2.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=2015558 {ECO:0000313|EMBL:OYU83233.1, ECO:0000313|Proteomes:UP000216176};
RN [1] {ECO:0000313|EMBL:OYU83233.1, ECO:0000313|Proteomes:UP000216176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BFFFF2 {ECO:0000313|EMBL:OYU83233.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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:OYU83233.1}.
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DR EMBL; NKJD01000044; OYU83233.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257K791; -.
DR Proteomes; UP000216176; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic 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; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:OYU83233.1};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000216176};
KW Transferase {ECO:0000313|EMBL:OYU83233.1}.
FT MOD_RES 262
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 423 AA; 47599 MW; BC6F4C878525D230 CRC64;
MYWQKRTPDE RMARIQQALT ENVNFSTDAS LGYPASRLDS RVFYEEAPFL RDAPVLQTYV
ANPNHIGCHT MGTSEKAFGG TQALEREVLD IVGVDIFKAI PDSLDGYISP GGTEANIQAL
WMYRNYFMHE HHALPHQIAI MASEDTHYSI AKGANLLQLE WICTPVERDH RTLIPEQIAQ
LIADAMQRGI KYLIVVGNMG TTMFGSVDDV AVYTSLLDHY KMHYKMHIDG AYGGFVHPFS
QADHSLTFLN PAISSVTIDA HKMLQAPYGT GIFLCRKNLI HHVMTQEAAY VEGMDVTLCG
SRSGANAVAV WMILATYGPH GWYEKISILQ MRTQFLCREL ALVGVRFFRN PSMNIVTIDA
SFISTELAEK YTLVPQTHTP DNRWYKIVVM DHVEIEHLHT FIQDLKAALY AEKGLSAAIY
SST
//
