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Database: UniProt
Entry: A0A117IVM3_9ACTN
LinkDB: A0A117IVM3_9ACTN
Original site: A0A117IVM3_9ACTN 
ID   A0A117IVM3_9ACTN        Unreviewed;       448 AA.
AC   A0A117IVM3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=2,4-diaminobutyrate 4-aminotransferase {ECO:0000313|EMBL:KUH37443.1};
GN   ORFNames=ATE80_18095 {ECO:0000313|EMBL:KUH37443.1};
OS   Streptomyces kanasensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=936756 {ECO:0000313|EMBL:KUH37443.1, ECO:0000313|Proteomes:UP000054011};
RN   [1] {ECO:0000313|EMBL:KUH37443.1, ECO:0000313|Proteomes:UP000054011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZX01 {ECO:0000313|EMBL:KUH37443.1,
RC   ECO:0000313|Proteomes:UP000054011};
RA   Zhang G., Han L., Feng J., Zhang X.;
RT   "Genome-wide analysis reveals the secondary metabolome in Streptomyces
RT   kanasensis ZX01.";
RL   Submitted (NOV-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:KUH37443.1}.
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DR   EMBL; LNSV01000046; KUH37443.1; -; Genomic_DNA.
DR   RefSeq; WP_058943264.1; NZ_LNSV01000046.1.
DR   AlphaFoldDB; A0A117IVM3; -.
DR   STRING; 936756.ATE80_18095; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000054011; Unassembled WGS sequence.
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   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; IPR004637; Dat.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00202; Aminotran_3; 2.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:KUH37443.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054011};
KW   Transferase {ECO:0000313|EMBL:KUH37443.1}.
FT   REGION          180..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  45956 MW;  E3E9454279E376B1 CRC64;
     MAATEPAPAG PTAGHEGIMR RQALREPAAR TYARSLPVVP VRARGVTIEG ADGRRYLDCT
     SGAGILVLGH NHPVVLEAIK RVIDSGAPLD VHGLATPVRD AFTTELFTTL PAALAADARV
     RFCGPAPGDA VAAALALART ATGRSRVLAC AGYGPHAPAA PGRPAGPGPD GDVPVTWLPY
     PRDGRHPPDG DGGAPHGPRG AEGGIATPAA VIVEPVRGAR DVVPAPDDWL RRVRGLTAES
     SVPLIADERL TGLGRTGSFW AVGHSGVVPD VMVMPEALGA SLPLSVIVYR AGLDHGRRDR
     PAGAPRGNQL AMAAGTATLA YVRGNRLAER AATLGARLLA DLRGLAAAHP CVAGVRGRGL
     MIGVELAAPS PTGDTPPRAT TPFLRTAADR AEAVRRECLD RGLIVTTGGR ASGVVRLLPP
     LTLTDGQAAA VLDRFADAVA ATERTQPH
//
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