ID   ECTB_ALKCK              Reviewed;         426 AA.
AC   Q5WL78;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
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; OrderedLocusNames=ABC0335;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD62877.1; -; Genomic_DNA.
DR   RefSeq; WP_011245196.1; NC_006582.1.
DR   AlphaFoldDB; Q5WL78; -.
DR   SMR; Q5WL78; -.
DR   STRING; 66692.ABC0335; -.
DR   EnsemblBacteria; BAD62877; BAD62877; ABC0335.
DR   KEGG; bcl:ABC0335; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   OMA; ELDQWKP; -.
DR   OrthoDB; 386839at2; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000001168; 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: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; Reference proteome; Transferase.
FT   CHAIN           1..426
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000120519"
FT   MOD_RES         268
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   426 AA;  46746 MW;  B890FD98EB331842 CRC64;
     MNETMSIFNE LESEVRSYCR SFPAVFTKAK GWKMWDEDGT EYIDFFAGAG ALNYGHNDEK
     MKRALIDYIA DDGITHSLDM ATKPKAAFLK KLNEVILKPR KLNYKVMFPG PTGTNTVESA
     LKLARKVTGR TEIISFTNGF HGMTIGSLSV TGNASKRKGA GIPLTNVVTM PYDKFGDEEV
     DTLRYLEQFL HDNGSGVDIP AAVILETVQG EGGINAARME WLQQLERICK KYDILMIIDD
     VQAGIGRTGT FFSFEEAGIT PDIVCLSKSI GGYGLPLALT LFKPELDIWA PGEHNGTFRG
     NNHAFITATA ALSYWEDPSF EQAIKDKSKK IHAFLTKLVD SYPEMDGCVK GRGFMAGIGS
     KVDGLAGKVA AEAFKRGLIM ETAGPEDEVF KLFPPLTISD EDLEKGFAII EESVRAVLGV
     KEPVTT