ID   ECTB_STRCO              Reviewed;         423 AA.
AC   Q93RW1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
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=SCO1865; ORFNames=SCI39.12;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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; AL939110; CAC38800.1; -; Genomic_DNA.
DR   RefSeq; NP_626132.1; NC_003888.3.
DR   RefSeq; WP_003976955.1; NZ_VNID01000001.1.
DR   AlphaFoldDB; Q93RW1; -.
DR   SMR; Q93RW1; -.
DR   STRING; 100226.SCO1865; -.
DR   PRIDE; Q93RW1; -.
DR   GeneID; 1097299; -.
DR   KEGG; sco:SCO1865; -.
DR   PATRIC; fig|100226.15.peg.1890; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   InParanoid; Q93RW1; -.
DR   OMA; ELDQWKP; -.
DR   PhylomeDB; Q93RW1; -.
DR   UniPathway; UPA00067; UER00121.
DR   Proteomes; UP000001973; 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..423
FT                   /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT                   /id="PRO_0000120529"
FT   MOD_RES         271
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   423 AA;  46720 MW;  611FBAEEDB8C5BC2 CRC64;
     MTITQPDLSV FETVESEVRS YCRGWPTVFD RAVGSRMYDE DGHEYLDFFA GAGSLNYGHN
     NAVLKRALID YLERDGVTHG LDMSTTAKRR FLETFQNTIL RPRDLPYKVM FPGPTGTNAV
     ESALKLARKV KGRESIVSFT NAFHGMSLGS LAVTGNAFKR AGAGIPLVHG TPMPFDNYFD
     GTVEDFIWFE RLLEDQGSGL NKPAAVIVET VQGEGGINVA RAEWLRALAD LCERQDMLLI
     VDDIQMGCGR TGAFFSFEEA GITPDIVTVS KSISGYGMPM ALTLFKPELD VWEPGEHNGT
     FRGNNPAFVT ATATLEAYWA DGSAMEKQTR KRGEQVEQHM IAITEENLAD VKEYRGRGLV
     WGLEFHDKDR AGRVAKRAFE LGLLIETSGP ESEVVKLLPA LTITPDELDE GMKTLARAVR
     ETA