ID   ECTB_BORBR              Reviewed;         435 AA.
AC   Q7WHI8;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
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=BB3219;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640446; CAE33711.1; -; Genomic_DNA.
DR   RefSeq; WP_003810599.1; NC_002927.3.
DR   AlphaFoldDB; Q7WHI8; -.
DR   SMR; Q7WHI8; -.
DR   STRING; 257310.BB3219; -.
DR   EnsemblBacteria; CAE33711; CAE33711; BB3219.
DR   GeneID; 56479329; -.
DR   KEGG; bbr:BB3219; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   OMA; ELDQWKP; -.
DR   OrthoDB; 386839at2; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000001027; 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; Transferase.
FT   CHAIN           1..435
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000120520"
FT   MOD_RES         266
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   435 AA;  47707 MW;  983E0746A97B3111 CRC64;
     MDLKIFDRME SEVRGYIRSF PVIFSQARGS LLIDEEGNEY IDFFSGAGTL NYGHNNPVFK
     ERLLEYLHSD GVVHGLDMAT SAKKRFLETV DRVLLKPRNW QYTLQFTGPT GTNAVEAALK
     LARQVKGRSN IISFTHGFHG VSGGSLAATA NAKFRDAAGV SLGNTTFMPY DGYFGPDVDT
     IAYIERMLDD PSSGLDKPAA VIVETVQGEG GVNVATLRWL KDLQKLCRRH DMLMIVDDIQ
     VGCGRTGSFF SFEAAGIQPD IITLSKSLSG FGLPMSLVLM KPELDVWKPG AHSGTFRGNN
     LAFVTATQAL ETYWSSDAFS NEVQRKERLV RDWLENLAHS YPNAGLAVRG RGLIQGLVAT
     AEPELANRIA RKAFERGVVI ETSGAQDEVL KLLPALTIED ELLTRGLDLI EASVADALSE
     EQPAAQVLKF GGKRR