ID   PPAT_BACCR              Reviewed;         396 AA.
AC   Q81I05;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase;
DE            EC=2.3.1.-;
GN   OrderedLocusNames=BC_0621;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AE016877; AAP07638.1; -; Genomic_DNA.
DR   RefSeq; NP_830437.1; NC_004722.1.
DR   RefSeq; WP_000095905.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q81I05; -.
DR   SMR; Q81I05; -.
DR   STRING; 226900.BC_0621; -.
DR   EnsemblBacteria; AAP07638; AAP07638; BC_0621.
DR   GeneID; 67505314; -.
DR   KEGG; bce:BC0621; -.
DR   PATRIC; fig|226900.8.peg.580; -.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   Proteomes; UP000001417; Chromosome.
DR   GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IBA:GO_Central.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR010962; AONS_Archaea/Firmicutes.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01825; gly_Cac_T_rel; 1.
DR   PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..396
FT                   /note="Putative pyridoxal phosphate-dependent
FT                   acyltransferase"
FT                   /id="PRO_0000163834"
FT   BINDING         111..112
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         211..214
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         241..244
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         244
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   396 AA;  43063 MW;  41EDE8BB40A3EAC2 CRC64;
     MSSKTLAKFL EENLEDLKSK GLYNVIDPLE SSNGPIITIG GKEYINLSSN NYLGLATDSR
     LQEAAIGAIH KYGVGAGAVR TINGTLDLHI KLEETIAKFK HTEAAIAYQS GFNCNMAAIS
     AVMDKNDAIL SDELNHASII DGSRLSKAKI IVYKHSDMED LRQKAIAAKE SGLYNKLMVI
     TDGVFSMDGD VAKLPEIVEI AEELDLMTYV DDAHGSGVLG KGAGTVKHFG LSDKVDFQIG
     TLSKAIGVIG GYVAGKQNLI DWLKVRSRPF LFSTALTPAD AAACMRSIEI LMESTELHDR
     LWENGRYLKQ GLKELGFNIG ESETPITPCI IGDEVLTQEF SKRLNEEGVY AKSIVFPTVA
     KGTGRVRNMP TAAHTKEMLD EAILKYEKVG KEMGII