ID   PPAT_OCEIH              Reviewed;         396 AA.
AC   Q8EM07;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase;
DE            EC=2.3.1.-;
GN   OrderedLocusNames=OB3054;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC15010.1; -; Genomic_DNA.
DR   RefSeq; WP_011067450.1; NC_004193.1.
DR   AlphaFoldDB; Q8EM07; -.
DR   SMR; Q8EM07; -.
DR   STRING; 221109.22778742; -.
DR   EnsemblBacteria; BAC15010; BAC15010; BAC15010.
DR   KEGG; oih:OB3054; -.
DR   eggNOG; COG0156; Bacteria.
DR   HOGENOM; CLU_015846_11_0_9; -.
DR   OMA; MDTHGFG; -.
DR   OrthoDB; 479874at2; -.
DR   PhylomeDB; Q8EM07; -.
DR   Proteomes; UP000000822; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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_0000163836"
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;  43236 MW;  688975A7D1A88B82 CRC64;
     MTSSKLDQFL QENISDLKDR GLYNEIDTVQ GANGPEITIE GKKLINLSSN NYLGLATNNE
     MKEIAKKAID SHGVGAGAVR TINGTLDLHI ELEKKIAQFK GTEAAIAYQS GFNCNMAAIS
     AVMDKNDAIL SDSLNHASII DGCRLSKAKI IRFEHSDMND LRQKAKEAVE SGQYNKIMVI
     TDGVFSMDGD IAKLPEIVDI AEEFDLITYV DDAHGSGVTG DGAGTVKHFG LQDKVDMQMG
     TLSKAIGVIG GYVAGKQSLI DWLKVRSRPF LFSTAVSPAD AVASKRAIEM LMESTELNEK
     LWENGDYLKQ GLKELGFDIG ESETPITPCI IGDEKKAQEF SKRLYEEGVY AKSIVFPTVP
     RGTGRVRNMP TAAHTKEMLD DAIAIYKKIG QEMKLI