ID A0A3M7LEC1_9FLAO Unreviewed; 367 AA.
AC A0A3M7LEC1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=DegT/DnrJ/EryC1/StrS family aminotransferase {ECO:0000313|EMBL:RMZ61051.1};
GN ORFNames=D1632_03530 {ECO:0000313|EMBL:RMZ61051.1};
OS Chryseobacterium nematophagum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2305228 {ECO:0000313|EMBL:RMZ61051.1, ECO:0000313|Proteomes:UP000267524};
RN [1] {ECO:0000313|EMBL:RMZ61051.1, ECO:0000313|Proteomes:UP000267524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JUb275 {ECO:0000313|EMBL:RMZ61051.1,
RC ECO:0000313|Proteomes:UP000267524};
RA Page A., Roberts M., Felix M.-A., Weir W.;
RT "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT nematodes.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC {ECO:0000256|RuleBase:RU004508}.
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:RMZ61051.1}.
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DR EMBL; QWIV01000005; RMZ61051.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7LEC1; -.
DR Proteomes; UP000267524; Unassembled WGS sequence.
DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR30244:SF36; 3-OXO-GLUCOSE-6-PHOSPHATE:GLUTAMATE AMINOTRANSFERASE; 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 Aminotransferase {ECO:0000313|EMBL:RMZ61051.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW ECO:0000256|RuleBase:RU004508}; Transferase {ECO:0000313|EMBL:RMZ61051.1}.
FT ACT_SITE 189
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT MOD_RES 189
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ SEQUENCE 367 AA; 41456 MW; CACEBBA4546E367F CRC64;
MIKFLDLQQI NLQYQEEIEA KLLEVFRSGW YLMGGALSNF EKKLSQYTGA KHAIGVANGL
DALRLILRAY IEMGFMEPGD EIIVPSNTYI ASILAISDNG LVPILVEPDI DNYNIDILKI
EEKITSKTKG ILIVHLYGRV VFSEVLTSLA TQYNLKVIED NAQAIGAEWN DKKSGNLGDA
AGFSFYPGKN LGALGDAGGI TTNDEKLAQT IRALANYGSN QKYVNIYKGL NSRLDEIQAA
VLDVKLNYID EENNKRREVA KQFIQGISNP KITLPEYPDK EKEHVWHLFV IRTNDRDRLQ
QYLTENGIQT LIHYPIPPHK QEAYKEWNEL SFPISEKIHE EVLSLPISSI IKKEDIEKII
SVLNGFE
//
