ID A0A0D3L927_9BACT Unreviewed; 386 AA.
AC A0A0D3L927;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative PLP-dependent enzyme possibly involved in cell wall biogenesis {ECO:0000313|EMBL:AHM58418.1};
GN ORFNames=D770_00720 {ECO:0000313|EMBL:AHM58418.1};
OS Flammeovirgaceae bacterium 311.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM58418.1, ECO:0000313|Proteomes:UP000064112};
RN [1] {ECO:0000313|EMBL:AHM58418.1, ECO:0000313|Proteomes:UP000064112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=311 {ECO:0000313|EMBL:AHM58418.1,
RC ECO:0000313|Proteomes:UP000064112};
RA Fang C.;
RT "Complete bacteria genome obtained just from illumina data.";
RL Submitted (NOV-2012) 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 DegT/DnrJ/EryC1 family.
CC {ECO:0000256|ARBA:ARBA00037999, ECO:0000256|RuleBase:RU004508}.
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DR EMBL; CP004371; AHM58418.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D3L927; -.
DR STRING; 1257021.D770_00720; -.
DR KEGG; fbt:D770_00720; -.
DR PATRIC; fig|1257021.3.peg.165; -.
DR OrthoDB; 9810913at2; -.
DR Proteomes; UP000064112; Chromosome.
DR CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR InterPro; IPR026385; LegC-like.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR04181; NHT_00031; 1.
DR PANTHER; PTHR30244:SF43; PYRIDOXAL PHOSPHATE-DEPENDENT AMINOTRANSFERASE EPSN-RELATED; 1.
DR PANTHER; PTHR30244; TRANSAMINASE; 1.
DR Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR PIRSF; PIRSF000390; PLP_StrS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR000390-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000064112}.
FT ACT_SITE 219
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 219
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 386 AA; 43137 MW; 0FF872B21AAC7749 CRC64;
MGQSSKFSHI ITFIKSLFPG QDFIPLHEPR FVGNEKKYVA DAIDSTFVSS VGAYVNRFEE
MMQEITGAKY AVATVNGTAA LHMALLVAGV KQGDEVLSQD LSFIATANAI SYLGAKPVFL
DIDQKTLGLS AAKLEAFLEQ WGQKTAKGTI NKKTTKRIAA CVPMHSFGFP CEIDKIASIC
RQWQIPLVED AAESLGSYYK KKHTGTFGLL GTYSFNGNKT ITCGGGGAIV TNDEQLARLA
KHLTTQAKVP HAWEFNHDYI GYNYRMPNLN AALACAQLEQ LHHFVENKRQ LAQTYQAFFE
QMTGMEFFKE EQDAKANYWL NVLLLESREE RDAFLTEANQ NGVMVRPAWT LMHKLPMFRD
SQHDDVAVSQ WAEDRLVNIP SSVRLT
//