ID   A0A2K4G560_9PSED        Unreviewed;       465 AA.
AC   A0A2K4G560;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:POA18643.1};
GN   ORFNames=C1886_15890 {ECO:0000313|EMBL:POA18643.1};
OS   Pseudomonas sp. FW300-N1A1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA18643.1, ECO:0000313|Proteomes:UP000236411};
RN   [1] {ECO:0000313|EMBL:POA18643.1, ECO:0000313|Proteomes:UP000236411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA18643.1,
RC   ECO:0000313|Proteomes:UP000236411};
RA   Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA   Alm E.J.;
RT   "Whole genome sequencing of deep branching strains shows evolution and
RT   exchange across a contaminated watershed.";
RL   Submitted (JAN-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   -!- 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:POA18643.1}.
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DR   EMBL; PPSF01000036; POA18643.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K4G560; -.
DR   Proteomes; UP000236411; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   465 AA;  49607 MW;  45E6D4F2E664EFEE CRC64;
     MSVATSLVNV QSAPAEVLYQ FNESPLLARQ SRQESNARSY PRRIPLALKR AKGLYVEDVE
     GRRFIDCLAG AGTLALGHNH PVVIEAIQQV LADELPLHTL DLTTPVKDQF VQDLFGLLPA
     ALAGEAKIQF CGPTGTDAVE AALKLVRTAT GRSMVLSFQG GYHGMSQGAL SLMGSLGPKK
     PLGALLGNGV QFMPFPYDYR CPFGLGGELG VKANLHYLEN LLNDPEAGVQ LPAAVIVEAV
     QGEGGVIPAD LDWLRGLRRI TEQAGVALIV DEIQSGFART GKMFAFEHAG IIPDVVVMSK
     AIGGSLPLAV VVYRDWLDTW LPGAHAGTFR GNQMAMAAGS AVMRYLIEHK VADHAAAMGE
     RLAAHLRLLQ QDFPQLGDIR GRGLMLGVEL VNPAGEADAQ GHPPAFGQLA PRVQRECLKR
     GLILELGGRH GCVVRFLPPL IITAAEIDRV AEIFGRALGA AVADL
//