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Database: UniProt
Entry: A0A3N0BX49_9SPHI
LinkDB: A0A3N0BX49_9SPHI
Original site: A0A3N0BX49_9SPHI 
ID   A0A3N0BX49_9SPHI        Unreviewed;       413 AA.
AC   A0A3N0BX49;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   SubName: Full=Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme {ECO:0000313|EMBL:RNL54251.1};
GN   ORFNames=D7004_09170 {ECO:0000313|EMBL:RNL54251.1};
OS   Pedobacter jejuensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=1268550 {ECO:0000313|EMBL:RNL54251.1, ECO:0000313|Proteomes:UP000274046};
RN   [1] {ECO:0000313|EMBL:RNL54251.1, ECO:0000313|Proteomes:UP000274046}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TNB23 {ECO:0000313|EMBL:RNL54251.1,
RC   ECO:0000313|Proteomes:UP000274046};
RA   Cho Y.-J., Cho A., Kim O.-S.;
RT   "Genome sequencing of Pedobacter jejuensis TNB23.";
RL   Submitted (OCT-2018) 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|RuleBase:RU003693};
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003693}.
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:RNL54251.1}.
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DR   EMBL; RBEE01000012; RNL54251.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N0BX49; -.
DR   OrthoDB; 9807157at2; -.
DR   Proteomes; UP000274046; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic 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; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:RNL54251.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003693}; Transferase {ECO:0000313|EMBL:RNL54251.1}.
FT   DOMAIN          46..392
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   413 AA;  46172 MW;  D3336A33440D9788 CRC64;
     MDIFDKITKH MGPLGQHQKW SHGYFSFPKL EGEIAPHMQF NGKEHLVWSL NNYLGLANHP
     EVRKADEEAA AKFGMAYPMG ARMMSGNSKY HEQLEQELAE FVGKPDAFLL NFGYQGMVSI
     IDTLVDRNDV VVYDAESHAC IVDGLRLHMG KRFVYKHNDV DSARKQLERA TKLVEETGGG
     ILLITEGVFG MSGAQGKLKE LIELKKEFTF RILVDDAHGF GTMGKTGAGT HEAQDCIEDI
     DVYFSTFAKS MAGIGAFVAS TVDITNFLRY NMRSQTFAKA LPMPMVIGLL KRLELLKTKP
     ELKDKLWEIA MALQKGLRER GLDLGITDTV VTPVFLKGEL SDATAITYDL RENYGIFCSI
     VIFPVIPKGL IELRLIPTAV HTLEDVQRTL DAFSEVAEKL ESGYYKENQF AAV
//
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