ECTB_MARHA
ID ECTB_MARHA Reviewed; 427 AA.
AC O06060;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 93.
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 Marinococcus halophilus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Marinococcus.
OX NCBI_TaxID=1371;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 27964 / DSM 20408 / CIP 140819 / JCM 2479 / NBRC 102359 / NCIMB
RC 13496 / CCM 2706;
RX PubMed=9141677; DOI=10.1099/00221287-143-4-1141;
RA Louis P., Galinski E.A.;
RT "Characterization of genes for the biosynthesis of the compatible solute
RT ectoine from Marinococcus halophilus and osmoregulated expression in
RT Escherichia coli.";
RL Microbiology 143:1141-1149(1997).
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:0000305|PubMed:9141677}.
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; U66614; AAB57634.1; -; Genomic_DNA.
DR AlphaFoldDB; O06060; -.
DR SMR; O06060; -.
DR STRING; 1371.GCA_900166605_00960; -.
DR PRIDE; O06060; -.
DR KEGG; ag:AAB57634; -.
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..427
FT /note="Diaminobutyrate--2-oxoglutarate transaminase"
FT /id="PRO_0000120524"
FT MOD_RES 269
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 427 AA; 47193 MW; 907FE135B852EBEF CRC64;
MMQNDLSVFN EYESEVRSYV RGFPTVFHQA KGYKLWDLDG KEYVDFFSGA GALNYGHNDE
NMKQKLLTYI QEDGVTHSLD MATKAKGEFI DAFQNIILKP RNMDYKIMFP GPTGANSVES
ALKLARKVTG RTNVVSFTNG FHGMTIGALS VTGNKFKRNG AGMPLSNTST LPYDQFLKES
NNSIEYIENF LDNGGSGLDK PAAFIVETVQ GEGGLNAASS EWLRSIEKIC RERDIKLILD
DVQAGVGRTG TFFSFEPAGI KPDFVCLSKS IGGNGSPLAI TLVAPEYDKF APGEHNGTFR
GNNFAFVTGT EALNYWKDDR LEKNVQEKSE RITSFLDDMI KKHPEMKGVR KGRGFMQGIM
SPIEDLADNI AGRCFEHGLI METAGAEDEV FKLFPPITID DEGLERGLSI LQQAIEEVTA
ESNLVAK
