ID A0A1X6XHV9_9MICO Unreviewed; 428 AA.
AC A0A1X6XHV9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Diaminobutyrate--2-oxoglutarate transaminase {ECO:0000256|RuleBase:RU365034};
DE EC=2.6.1.76 {ECO:0000256|RuleBase:RU365034};
DE AltName: Full=DABA aminotransferase {ECO:0000256|RuleBase:RU365034};
GN ORFNames=FM105_09425 {ECO:0000313|EMBL:SLM98708.1};
OS Brevibacterium yomogidense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=946573 {ECO:0000313|EMBL:SLM98708.1, ECO:0000313|Proteomes:UP000196581};
RN [1] {ECO:0000313|EMBL:SLM98708.1, ECO:0000313|Proteomes:UP000196581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B Co 03.10 {ECO:0000313|EMBL:SLM98708.1,
RC ECO:0000313|Proteomes:UP000196581};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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|RuleBase:RU365034}.
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|RuleBase:RU365034};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU365034};
CC -!- PATHWAY: Amine and polyamine biosynthesis; ectoine biosynthesis; L-
CC ectoine from L-aspartate 4-semialdehyde: step 1/3.
CC {ECO:0000256|RuleBase:RU365034}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FWFF01000017; SLM98708.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6XHV9; -.
DR UniPathway; UPA00067; UER00121.
DR Proteomes; UP000196581; Unassembled WGS sequence.
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; 3.90.1150.10; 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; IPR012773; Ectoine_EctB.
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 NCBIfam; TIGR02407; ectoine_ectB; 1.
DR PANTHER; PTHR43552; DIAMINOBUTYRATE--2-OXOGLUTARATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR43552:SF2; DIAMINOBUTYRATE--2-OXOGLUTARATE TRANSAMINASE; 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:0000256|RuleBase:RU365034,
KW ECO:0000313|EMBL:SLM98708.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Pyruvate {ECO:0000313|EMBL:SLM98708.1};
KW Transferase {ECO:0000256|RuleBase:RU365034, ECO:0000313|EMBL:SLM98708.1}.
SQ SEQUENCE 428 AA; 46285 MW; D0367143129FE820 CRC64;
MTDIFYSLES EVRSYSRSWP VEFVQASGAT QTDASGTEYL DFFSGAGALN YGHNNPVVME
PLIEYLQSGA VLHSMDMMTP AKREFLQTFK DVILEPRELP YKVMFPGPTG TNTVEAALKL
ARKYTGRQHI LSFTNAFHGM TLGSLSVTGN SMKRQGAGIP LTNSSKIPYD DYFDGETADF
LWLERVLEDS GSGVDKPAAI IVETVQGEGG LRAARFDWLR RLSDLCAEHE ILLIVDDVQA
GCGRTGTFFS FEDAGIVPDI VCLSKSIAGS GLPMALTLFR PELDIWSPGE HNGTFRGNNA
AFVTATAALK EYWADPSFQK ELATTIDAMH ARLESIAVTT SGAGVRGRGL LSGLFFEDPE
AAGKIAAEAF RNGMLLETSG PKDEVVKIMP PLTVTADELE RGLDIIEAAV RTVTGPAVER
PSAEATSA
//
