ID A0A1C3SB76_9BACI Unreviewed; 448 AA.
AC A0A1C3SB76;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|ARBA:ARBA00014798};
DE EC=2.6.1.76 {ECO:0000256|ARBA:ARBA00013155};
DE AltName: Full=DABA aminotransferase {ECO:0000256|ARBA:ARBA00030665};
DE AltName: Full=Diaminobutyrate--2-oxoglutarate aminotransferase {ECO:0000256|ARBA:ARBA00031476};
DE AltName: Full=L-2,4-diaminobutyric acid transaminase {ECO:0000256|ARBA:ARBA00029744};
GN ORFNames=BGLY_1214 {ECO:0000313|EMBL:SCA85037.1}, EQZ20_06400
GN {ECO:0000313|EMBL:QAT64570.1};
OS Bacillus glycinifermentans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1664069 {ECO:0000313|EMBL:SCA85037.1, ECO:0000313|Proteomes:UP000093092};
RN [1] {ECO:0000313|Proteomes:UP000093092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SCA85037.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BGLY {ECO:0000313|EMBL:SCA85037.1};
RA Schneider J.;
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QAT64570.1, ECO:0000313|Proteomes:UP000288675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRCM103574 {ECO:0000313|EMBL:QAT64570.1,
RC ECO:0000313|Proteomes:UP000288675};
RA Kong H.-J., Jeong S.-Y., Jeong D.-Y.;
RT "Genome sequence of Bacillus glycinifermentans SRCM103574.";
RL Submitted (JAN-2019) 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:0000256|ARBA:ARBA00002189}.
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; Evidence={ECO:0000256|ARBA:ARBA00001487};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC {ECO:0000256|ARBA:ARBA00004946}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP035232; QAT64570.1; -; Genomic_DNA.
DR EMBL; LT603683; SCA85037.1; -; Genomic_DNA.
DR RefSeq; WP_046131263.1; NZ_LT603683.1.
DR AlphaFoldDB; A0A1C3SB76; -.
DR GeneID; 82852309; -.
DR KEGG; bgy:BGLY_1214; -.
DR PATRIC; fig|1664069.6.peg.1276; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000093092; Chromosome 1.
DR Proteomes; UP000288675; Chromosome.
DR GO; GO:0045303; F:diaminobutyrate-2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR004637; Dat.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00709; dat; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF1; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:SCA85037.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SCA85037.1}.
SQ SEQUENCE 448 AA; 48944 MW; 7871B0205C816BE4 CRC64;
MSVQTSSKNR VFLEQQNRRE SNARSYPRRF PLAMQTAEGI FVTDADGKQY YDCLAGAGTL
VLGHNHPVVI EAIQKMIDEK RPLHTLDITS EIKEEFISEV FASLPESFAK RAKIQFCGPT
GGDAIEAAIK LVKTATGRRS ILSFQGGYHG ATHGTMALSG NLSPKENVQG LMPDVHFLPY
PYEYRCPFGA GGEETHRLSS AYIENMLDDP ESGILPPAGM IFEAVQGEGG SVPARAEWIR
EMRRITKERG IPLIIDEVQT GIGRTGKMFA FEHAGIIPDV IVLSKAIGGS LPLSVVVYDR
DLDQWAPGAH IGTFRGNQMA MAAGTATLKY MKENGILLHV EKAGAKFMQH LQDIQRHIPE
IGDVRGRGLM IGAEIVSPLQ KQSAAGTPPA DPELAAKIQR KCFEKGLIVE TGGRHGSVIR
FLPPLIVTEE QIADITAIFK EAVYEALK
//
