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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//