ID A0A089WLM3_9PSED Unreviewed; 465 AA.
AC A0A089WLM3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=2,4-diaminobutyrate 4-aminotransferase {ECO:0000313|EMBL:AIR90165.1};
GN ORFNames=LK03_13045 {ECO:0000313|EMBL:AIR90165.1};
OS Pseudomonas cremoricolorata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR90165.1, ECO:0000313|Proteomes:UP000029493};
RN [1] {ECO:0000313|EMBL:AIR90165.1, ECO:0000313|Proteomes:UP000029493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND07 {ECO:0000313|EMBL:AIR90165.1,
RC ECO:0000313|Proteomes:UP000029493};
RA Chan K.-G.;
RL Submitted (SEP-2014) 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; CP009455; AIR90165.1; -; Genomic_DNA.
DR RefSeq; WP_038412781.1; NZ_CP009455.1.
DR AlphaFoldDB; A0A089WLM3; -.
DR STRING; 157783.LK03_13045; -.
DR KEGG; psw:LK03_13045; -.
DR eggNOG; COG0160; Bacteria.
DR OrthoDB; 9801052at2; -.
DR Proteomes; UP000029493; Chromosome.
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 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 Aminotransferase {ECO:0000313|EMBL:AIR90165.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000029493};
KW Transferase {ECO:0000313|EMBL:AIR90165.1}.
SQ SEQUENCE 465 AA; 49918 MW; C3381B316BAE4459 CRC64;
MSSASSLAQV LPATAPQPLY EFSDSPLLLR QQQQESNARS YPRRIPLALK RARGIYVEDV
EGRQFIDCLA GAGTLALGHN HPVVIEAIQR VLADELPLHT LDLTTPVKDR FVQDLFGVLP
DALRREAKVQ FCGPTGTDAV EAALKLARIA TGRSNVLAFH GAYHGMSQGA LSLMGSLGPK
KALGALLNNN VQFLPFPYDY RCPFGLGGAA GVRANLHYLE NLFNDPESGV QLPAAVIVEA
VQGEGGMIPA DVEWLRGLRR ITEQHGVALI VDEIQSGFAR TGKLFAFEHA GIVPDVVTLS
KAIGGSLPLA VVVYREWLDQ WGPGAHAGTF RGNQMAMAAG SAVIDYLLEH DLASHAAAMG
ERLCGHLRQL QRDYPQLGDI RGRGLMLGVE LVDPAGAADA QGHPPACRQL APKVQRECLR
RGLIVELGGR HGAVVRFLPP LIISAEQIDE VAERFAQAVR AALAA
//
