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Database: UniProt
Entry: J9BU02_BACCE
LinkDB: J9BU02_BACCE
Original site: J9BU02_BACCE 
ID   J9BU02_BACCE            Unreviewed;       381 AA.
AC   J9BU02;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=IG3_03200 {ECO:0000313|EMBL:EJV82551.1};
OS   Bacillus cereus HuA2-1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1053201 {ECO:0000313|EMBL:EJV82551.1, ECO:0000313|Proteomes:UP000004136};
RN   [1] {ECO:0000313|EMBL:EJV82551.1, ECO:0000313|Proteomes:UP000004136}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HuA2-1 {ECO:0000313|EMBL:EJV82551.1,
RC   ECO:0000313|Proteomes:UP000004136};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA   Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA   Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA   Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Bacillus cereus HuA2-1.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family.
CC       {ECO:0000256|RuleBase:RU004508}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJV82551.1}.
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DR   EMBL; AHDV01000023; EJV82551.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9BU02; -.
DR   PATRIC; fig|1053201.3.peg.3275; -.
DR   HOGENOM; CLU_033332_2_1_9; -.
DR   Proteomes; UP000004136; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   CDD; cd00616; AHBA_syn; 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; IPR000653; DegT/StrS_aminotransferase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR30244:SF34; DTDP-4-AMINO-4,6-DIDEOXYGALACTOSE TRANSAMINASE; 1.
DR   PANTHER; PTHR30244; TRANSAMINASE; 1.
DR   Pfam; PF01041; DegT_DnrJ_EryC1; 1.
DR   PIRSF; PIRSF000390; PLP_StrS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR000390-2,
KW   ECO:0000256|RuleBase:RU004508}.
FT   ACT_SITE        193
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-1"
FT   MOD_RES         193
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000390-2"
SQ   SEQUENCE   381 AA;  42471 MW;  7F350220430D9794 CRC64;
     MIKSKEKIYL SAPHMSGNEQ KYIQNAFDSN WIAPLGPNVD EFERELASFV GVKGGAAVSS
     GTAAIHLALR LLDVQKGDTV FCSSFTFVAS ANPIVYLGAE PVFIDSELET WNMSPQALAL
     ALYDANKAGK LPKAVILVHL YGQSAKLDEI LSLCNQYDVP IIEDAAESLG STYKGKASGT
     FGRFGVYSFN GNKIITTSGG GMLISDDAEA LVKAKFLATQ AKDPAPHYEH SEIGYNYRMS
     NILAGVGRGQ LEVLEDRVRA RRRIFNRYYE ELSHIPGFYF MPELENTRSN RWLTTMMIDE
     KESGISIEKL LTTLAEENIE ARPTWKPLHM QPLFKDSKYY SHQKDNDVSK RLFEQGVCLP
     SGSNMMDEDQ RRVIQAIINI I
//
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