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Database: UniProt
Entry: A0A0J8VS73_9ENTR
LinkDB: A0A0J8VS73_9ENTR
Original site: A0A0J8VS73_9ENTR 
ID   A0A0J8VS73_9ENTR        Unreviewed;       461 AA.
AC   A0A0J8VS73;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000313|EMBL:KMV36026.1};
DE            EC=2.6.1.76 {ECO:0000313|EMBL:KMV36026.1};
GN   ORFNames=ACH50_04090 {ECO:0000313|EMBL:KMV36026.1};
OS   Franconibacter pulveris.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Franconibacter.
OX   NCBI_TaxID=435910 {ECO:0000313|EMBL:KMV36026.1, ECO:0000313|Proteomes:UP000037315};
RN   [1] {ECO:0000313|EMBL:KMV36026.1, ECO:0000313|Proteomes:UP000037315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ34 {ECO:0000313|EMBL:KMV36026.1,
RC   ECO:0000313|Proteomes:UP000037315};
RA   Pal S., Banerjee T.D., Roy A., Sar P., Kazy S.K.;
RT   "Genome sequencing of Cronobacter sp. strain DJ34 isolated from petroleum
RT   contaminated sludge of Duliajan Oil Fields, Assam, India.";
RL   Submitted (JUN-2015) 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 class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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:KMV36026.1}.
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DR   EMBL; LFEJ01000004; KMV36026.1; -; Genomic_DNA.
DR   RefSeq; WP_024555848.1; NZ_LFEJ01000004.1.
DR   AlphaFoldDB; A0A0J8VS73; -.
DR   STRING; 1121863.GCA_000621185_04167; -.
DR   PATRIC; fig|1656095.3.peg.2915; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000037315; Unassembled WGS sequence.
DR   GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 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; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR004637; Dat.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00709; dat; 1.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KMV36026.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:KMV36026.1}.
SQ   SEQUENCE   461 AA;  49650 MW;  9CE1CFF4FE62CF12 CRC64;
     MMTDKVRIDS LSANSLPQSN ESFLNRQAEF ESNVRSYPRK LPLAIAKAQG VWITDVENKE
     YLDCLAGAGT LALGHNHPEV IQSIQSVITS GLPLHTLDLT TPLKDEFSAY LLSLLPGQGK
     EYCLQFTGPS GADAVEAALK LAKKVTGRSG VISFSGGYHG MTHGALSVTG NLSPKEAVNG
     MMPEVQFMPY PHQYRCPLGI GGEAGVKALT YYFENLINDV ESGVRKPAAV ILEAVQGEGG
     VNPAPAEWLQ RIRKVTQEHG ILLILDEVQA GFARTGKFFA FEHAGIEPDI IVMSKAVGGG
     LPLAVLGIKK QFDAWAPGHH TGTFRGNQLA MATGLTTLKI LKEERIADKV AEQGEWLKGK
     LAEMQKRFPV IGHVRGLGLM IGIEIVKPHE AQDHMGCYPA DGELSALLQK KCFEAGLILE
     RGGRGGSVLR LLPSLLISNA ELDVFLDKFE SALLNAGVKP V
//
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