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
//