DAT_ACIBA
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 03-AUG-2022, entry version 93.
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; Proteobacteria; 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; 470.IX87_08930; -.
DR KEGG; ag:BAA21844; -.
DR eggNOG; COG0160; Bacteria.
DR BioCyc; MetaCyc:MON-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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR43552; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00709; dat; 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
