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Database: UniProt
Entry: A0A1I7M633_9BRAD
LinkDB: A0A1I7M633_9BRAD
Original site: A0A1I7M633_9BRAD 
ID   A0A1I7M633_9BRAD        Unreviewed;       466 AA.
AC   A0A1I7M633;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=L-2,4-diaminobutyrate transaminase {ECO:0000313|EMBL:SFV17394.1};
GN   ORFNames=SAMN05192541_12853 {ECO:0000313|EMBL:SFV17394.1};
OS   Bradyrhizobium arachidis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=858423 {ECO:0000313|EMBL:SFV17394.1, ECO:0000313|Proteomes:UP000199591};
RN   [1] {ECO:0000313|EMBL:SFV17394.1, ECO:0000313|Proteomes:UP000199591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 26795 {ECO:0000313|EMBL:SFV17394.1,
RC   ECO:0000313|Proteomes:UP000199591};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; FPBQ01000028; SFV17394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7M633; -.
DR   OrthoDB; 9801834at2; -.
DR   Proteomes; UP000199591; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}.
SQ   SEQUENCE   466 AA;  51201 MW;  3F9E15156C1A3D7F CRC64;
     MTDIKTVAER DRSSVLHPFT QLKDFATGKI GDPTIVTDGR GVSIKDAEGR SYIDGFAGLY
     CVNVGYGRTE VAEAIARQAY KLAYYHTYAA HTTEELATLS DRLVRMAPGA PSKVFYGLSG
     SDANETQAKL VWYYNNLRGQ PRRKKIISRE RGYHGCSVIS GSMTGMSFYH DHMDLPFPGI
     LHTGSPHHYW GAEPGETEDS FSRRRAAELE QLILREGPET IGAFIAEPVL GTGGITPPPT
     GYWREIQTVL RRYDVLLIAD EVICGFGRTG ADFGSILYGM EPDLVTVAKG LTSGYMPLSA
     AIVGQRVYNV MEEAADRVGA FSHGYTYSGH PIAAAAANAV LDIFEKEELT NRAKTVGSHF
     QKRLKERFAQ LEIVGEVRGV GLLGAIEFVA DRQTKRRFDP QIKVGARISK AARDRGLIAR
     AMPHGDILGF APPLIVSEPE IDEMIDLAYR ATKQVMDELA KESQTT
//
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