ID   A0A0F7HE39_SERFO        Unreviewed;       461 AA.
AC   A0A0F7HE39;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000313|EMBL:AKG71383.1};
DE            EC=2.6.1.76 {ECO:0000313|EMBL:AKG71383.1};
GN   ORFNames=WN53_20890 {ECO:0000313|EMBL:AKG71383.1};
OS   Serratia fonticola.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG71383.1, ECO:0000313|Proteomes:UP000034699};
RN   [1] {ECO:0000313|EMBL:AKG71383.1, ECO:0000313|Proteomes:UP000034699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG71383.1,
RC   ECO:0000313|Proteomes:UP000034699};
RA   Chan K.-G., Ee R.;
RT   "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL   Submitted (APR-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}.
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DR   EMBL; CP011254; AKG71383.1; -; Genomic_DNA.
DR   RefSeq; WP_024486749.1; NZ_CP011254.1.
DR   AlphaFoldDB; A0A0F7HE39; -.
DR   STRING; 47917.AV650_16685; -.
DR   GeneID; 30322638; -.
DR   KEGG; sfw:WN53_20890; -.
DR   PATRIC; fig|47917.8.peg.4357; -.
DR   Proteomes; UP000034699; Chromosome.
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:AKG71383.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034699};
KW   Transferase {ECO:0000313|EMBL:AKG71383.1}.
SQ   SEQUENCE   461 AA;  49615 MW;  27D4D4AAD8386767 CRC64;
     MMTDKVRIDT LSASSLPQSN DTFLARQAEF ESNVRSYPRK LPLAIAKAQG VWITDVENNQ
     YLDCLAGAGT LALGHNHPDV LQSIQSVISS GLPLHTLDLT TPLKDEFSSY LLSLLPSQGK
     EYCLQFTGPS GADAVEAALK LAKKVTGRSS IISFSGGYHG MTHGALSVTG NLSPKEAVSN
     MMPEVQFMPY PNQYRCPLGI GGDAGVKALT YYFDNLINDV ESGVRKPAAV ILEAVQGEGG
     VNPAPAEWLQ RIRKVTQEHG ILLIIDEVQA GFARTGKLFA FEHAGIEPDI IVMSKAVGGG
     LPLAVLGIKK QFDAWAPGHH TGTFRGNQLA MATGLTTLKH LKDNAIADKV AAQGEWLKGK
     LAELQKRYPV IGHVRGLGLM IGIEIVKPNE AQDHMGCYPA DGELSALLQK KCFESGLILE
     RGGRHGCVLR LLPSLLITDA ELEIFLDKFE NALLATGMEP V
//