ID   ECTB_VIRPA              Reviewed;         416 AA.
AC   Q6PR32;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase;
DE            EC=2.6.1.76;
DE   AltName: Full=DABA aminotransferase;
DE   AltName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase;
DE   AltName: Full=L-2,4-diaminobutyric acid transaminase;
GN   Name=ectB;
OS   Virgibacillus pantothenticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX   NCBI_TaxID=1473;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kuhlmann A.U., Gimpel S., Hoffmann T., Bremer E.;
RT   "Synthesis of compatible solute ectoine in Virgibacillus pantothenticus is
RT   induced by high osmolality and growth in the cold.";
RL   Submitted (MAR-2004) 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:0000250}.
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC       ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AY585263; AAS93807.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6PR32; -.
DR   SMR; Q6PR32; -.
DR   PRIDE; Q6PR32; -.
DR   UniPathway; UPA00067; UER00121.
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:UniProtKB-UniPathway.
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; IPR012773; Ectoine_EctB.
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   PANTHER; PTHR43552:SF2; PTHR43552:SF2; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00709; dat; 1.
DR   TIGRFAMs; TIGR02407; ectoine_ectB; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..416
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000120532"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   416 AA;  45890 MW;  0B3026F9E7018B91 CRC64;
     MQIFEELESA VRSYSRGWPT IFEKAKGYKL WDIDGNMYID FFAGAGALNY GHNHDTMQEK
     LIAYIQDDHI IHSLDMGTTP RKTFLETFHN TILKPRNLDY KIMFPGPTGT NTVESALKIA
     RKVTGRDTVI SFTNAFHGMT IGSLSVTGNS FKRHGAGVPL HHSVSMPYDK YVNDQDSIAY
     LERFLEDSGS GVALPAAIIL ETVQGEGGIN AASIEWLQKI ASICERWDIL LIIDDVQAGC
     GRTGTFFSFE PAGIAPDIVC LSKSIGGIGL PMAITLIKPE YDQWGPGEHN GTFRGNNLAF
     IAATEALTAF WQDNTFSKSI IQKSKLVRQR IDRIIDKFPS LQGEARGRGL MQGIVIPEPN
     CASEICKAAF DIGLIVETSG PNDEVVKFLP PLIIDKEGIN QGFDILEVSM EHVLKK