ID   DAT_ACIBA               Reviewed;         445 AA.
AC   P56744;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE            EC=2.6.1.76;
DE   AltName: Full=Diaminobutyrate transaminase;
DE   AltName: Full=L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase;
DE            Short=DABA aminotransferase;
DE            Short=DABA-AT;
DE   AltName: Full=L-diaminobutyric acid transaminase;
GN   Name=dat;
OS   Acinetobacter baumannii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC   STRAIN=ATCC 19606 / DSM 30007 / CCUG 19096 / CIP 70.34 / JCM 6841 / LMG
RC   1041 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81;
RX   PubMed=9260954; DOI=10.1128/jb.179.16.5118-5125.1997;
RA   Ikai H., Yamamoto S.;
RT   "Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-
RT   ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane
RT   production pathway in Acinetobacter baumannii.";
RL   J. Bacteriol. 179:5118-5125(1997).
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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; 1,3-diaminopropane
CC       biosynthesis; 1,3-diaminopropane from L-aspartate 4-semialdehyde: step
CC       1/2.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB001599; BAA21844.1; -; Genomic_DNA.
DR   PIR; T43804; T43804.
DR   AlphaFoldDB; P56744; -.
DR   SMR; P56744; -.
DR   STRING; 400667.A1S_2454; -.
DR   KEGG; ag:BAA21844; -.
DR   eggNOG; COG0160; Bacteria.
DR   BioCyc; MetaCyc:MONOMER-19; -.
DR   BRENDA; 4.1.1.86; 98.
DR   UniPathway; UPA00010; UER00731.
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   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..445
FT                   /note="Diaminobutyrate--2-oxoglutarate aminotransferase"
FT                   /id="PRO_0000120514"
FT   MOD_RES         289
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   445 AA;  47423 MW;  0DD756817A30D933 CRC64;
     MSVTSVNPAT NATNEYYLTR QSQMESNVRS YPRKLPLAIA KAQGCWVTDV EGTQYLDCLA
     GAGTLALGHN HPAVIQSIQD TLASGLPLHT LDLTTPLKDA FTEALLAYLP GGKEEYCLQF
     CGPSGADATE AAIKLAKTYT GRSSVISFSG GYHGMTHGSL AMTGNLSAKN AVNGLMPGVQ
     FMPYPHEYRC PLGLGGEAGV DALTYYFENF IEDVESGVTK PAAVILEAIQ GEGGVVTAPV
     KWLQKIREVT EKHNIVLILD EVQAGFARSG KMFAFEHAGI EPDVVVMSKA VGGGLPLAVL
     GIKRKFDAWQ PAGHTGTFRG NQLAMGTGLV VLETIKEQNL AQNAQERGEF PCIGNVRGRG
     LMIGVEIVDE RKPADRIGSH PADSQLAAAI QTACFNNNLL LEKGGRNGTV IRLLCPLIIT
     QEECVEVIAR FKKAVAEALV AVRGA
//