ID   ECTB_WOLSU              Reviewed;         427 AA.
AC   Q7M9K2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   25-MAY-2022, entry version 98.
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=WS0855;
OS   Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS   11488 / FDC 602W) (Vibrio succinogenes).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=273121;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC   11488 / FDC 602W;
RX   PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX571659; CAE09965.1; -; Genomic_DNA.
DR   RefSeq; WP_011138762.1; NC_005090.1.
DR   AlphaFoldDB; Q7M9K2; -.
DR   SMR; Q7M9K2; -.
DR   STRING; 273121.WS0855; -.
DR   EnsemblBacteria; CAE09965; CAE09965; WS0855.
DR   KEGG; wsu:WS0855; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_7; -.
DR   OMA; ELDQWKP; -.
DR   OrthoDB; 386839at2; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000000422; 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..427
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000120533"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   427 AA;  47222 MW;  2A659C16E6712D2C CRC64;
     MRIFEQLESQ VRSYIRSFPV IFERSKGAYL YDEQGKAYID FFAGAGTLNY GHNHPKIIEA
     MIAYLQNDGI LHGLDKATSA KKAFLQTLSE TILEPRHMDY KVQFTGPTGT NAIESALKLA
     RMVKGRSNVI AFTNAFHGLT MGSMAVTGNA FYRDEAFVNR ANVSFMPFDG YFGEEVDTSL
     YLRRFLEDGS SGVDLPAAII LETIQAEGGV NVARDEWLRS VEKVCRDFDI LLIVDEIQVG
     NGRTGRFFSF EESGIRPDII TLSKSIGGGL PLALVLLRPE LDQWKPGEHT GTFRGNNLAF
     VAAKEALEYW SDSVLGEWVK HNSAILKEGL EALVQAFPEL GMSARGRGLI YGLEIPLSGM
     AKEVSANCFQ KGLVIELAGA SDTVLKFLPP LIIEEETLRE GLGIIKEAIG EVLREREARM
     GEVFGDR