ID   D5DBF5_PRIM3            Unreviewed;       438 AA.
AC   D5DBF5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:ADF37937.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:ADF37937.1};
GN   OrderedLocusNames=BMD_1076 {ECO:0000313|EMBL:ADF37937.1};
OS   Priestia megaterium (strain DSM 319 / IMG 1521) (Bacillus megaterium).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Priestia.
OX   NCBI_TaxID=592022 {ECO:0000313|EMBL:ADF37937.1, ECO:0000313|Proteomes:UP000002365};
RN   [1] {ECO:0000313|EMBL:ADF37937.1, ECO:0000313|Proteomes:UP000002365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 319 / IMG 1521 {ECO:0000313|Proteomes:UP000002365};
RX   PubMed=21705586; DOI=10.1128/JB.00449-11;
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Koenig S.S., Huot Creasy H., Rosovitz M.J., Riley D.R., Daugherty S.,
RA   Martin M., Elbourne L.D., Paulsen I., Biedendieck R., Braun C.,
RA   Grayburn S., Dhingra S., Lukyanchuk V., Ball B., Ul-Qamar R., Seibel J.,
RA   Bremer E., Jahn D., Ravel J., Vary P.S.;
RT   "Genome sequences of the biotechnologically important Bacillus megaterium
RT   strains QM B1551 and DSM319.";
RL   J. Bacteriol. 193:4199-4213(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001982; ADF37937.1; -; Genomic_DNA.
DR   RefSeq; WP_013082073.1; NZ_CP120609.1.
DR   AlphaFoldDB; D5DBF5; -.
DR   KEGG; bmd:BMD_1076; -.
DR   PATRIC; fig|592022.4.peg.994; -.
DR   HOGENOM; CLU_016922_10_0_9; -.
DR   Proteomes; UP000002365; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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; PTHR11986; AMINOTRANSFERASE CLASS III; 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:ADF37937.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ADF37937.1}.
SQ   SEQUENCE   438 AA;  47856 MW;  09B0D089DFE00534 CRC64;
     MTQASLTQLM NSLPDLLAPS MAKDHPNLPV VKAEGCYYYG ADGKTYLDFT SGIATANTGH
     RHPKVVQAIK ESVDHLMHGP SGVIMYESIL QLAEELKTVL PRGLDCFFFA NSGTEAIEGA
     LKLAKYVTQR PYTVSFTGCF HGRSLGALSV TTSKSKYRKF LQPSGLTYQV PYADVIQCPK
     GEDPEIYCVE KLEKDFDTLF KHQVTPEEVA CMIVEPVLGE GGYVIPPKAW LQKIREVCDR
     HGILLIFDEV QTGFGRTGEW FAAQTFNVTP DIMAIAKGIA SGLPLSATVA SKQLMEKWPI
     GTHGTTFGGN PIACSAALAT LDVLKEEKLI ENSKEMGKYA ADQLQHLKAK HEVIGSIRSV
     GLLIGIEIIN PKTKQGDGNL LLEILDKCLE KGVLFYLCGN SGEVIRMIPP LTITKEEIDA
     GLRVLDEALT EITSLHVI
//