ID   A0A059MS24_9NOCA        Unreviewed;       426 AA.
AC   A0A059MS24; A0A0F6YB62; N1M8K9;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|RuleBase:RU365034};
DE            EC=2.6.1.76 {ECO:0000256|RuleBase:RU365034};
DE   AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN   Name=ectB {ECO:0000313|EMBL:UYF92345.1};
GN   ORFNames=OCS65_17820 {ECO:0000313|EMBL:UYF92345.1};
OS   Rhodococcus aetherivorans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=191292 {ECO:0000313|EMBL:UYF92345.1, ECO:0000313|Proteomes:UP001163947};
RN   [1] {ECO:0000313|EMBL:UYF92345.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=N1 {ECO:0000313|EMBL:UYF92345.1};
RA   Jiang W.;
RT   "The genome sequence of Rhodococcus aetherivorans N1.";
RL   Submitted (SEP-2022) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes reversively the conversion of L-aspartate beta-
CC       semialdehyde (ASA) to L-2,4-diaminobutyrate (DABA) by transamination
CC       with L-glutamate. {ECO:0000256|RuleBase:RU365034}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-2,4-diaminobutanoate = L-aspartate 4-
CC         semialdehyde + L-glutamate; Xref=Rhea:RHEA:11160, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58761, ChEBI:CHEBI:537519;
CC         EC=2.6.1.76; Evidence={ECO:0000256|RuleBase:RU365034};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU365034};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC       {ECO:0000256|RuleBase:RU365034}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP106982; UYF92345.1; -; Genomic_DNA.
DR   RefSeq; WP_006937215.1; NZ_JAWLKG010000001.1.
DR   GeneID; 83622315; -.
DR   KEGG; rav:AAT18_11170; -.
DR   Proteomes; UP001163947; Chromosome.
DR   GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047307; F:diaminobutyrate-pyruvate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0019491; P:ectoine 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; IPR012773; Ectoine_EctB.
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   NCBIfam; TIGR02407; ectoine_ectB; 1.
DR   PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43552:SF2; DIAMINOBUTYRATE--2-OXOGLUTARATE TRANSAMINASE; 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:0000256|RuleBase:RU365034,
KW   ECO:0000313|EMBL:UYF92345.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:UYF92345.1}.
SQ   SEQUENCE   426 AA;  46452 MW;  81992FC9EF1E625F CRC64;
     MTILEHPETP AKHSVFDYLE SEVRSYSRGW PTVFETASGS WLRDENGKDY LDFFAGAGAL
     NYGHNNPVLK TALVDYIMGD GITHGLDMST VAKRELLESF ESHILAPRGL DYKVQFPGPT
     GTNSVEAALK LARKVTGRES IINFTNAFHG MTLGALSVTG NSMKRAGAGV PLVHATPMPF
     DNYFDGVTED FHWFSRVLDD SGSGLNRPAA VIVETVQGEG GVNVARPEWL RALADLCAER
     DILLIVDDVQ MGCGRTGPFF SFEVAGITPD IVTLSKSIGG YGLPLALTLF KRDLDVWGPG
     EHNGTFRGNN PAFVTAAKAL QHYWADDHLE RETLRKGERI RQTFMNLSDM FDGVSTRGRG
     MVQGLVFDEP NDAQKVCALA FEQGLLAETS GPSDEVVKLL PPLTISDDEL EHGLNILCEA
     TSVVRA
//