PPAT_BACAN
ID PPAT_BACAN Reviewed; 396 AA.
AC Q81V80; Q6I3G7; Q6KX80;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Putative pyridoxal phosphate-dependent acyltransferase;
DE EC=2.3.1.-;
GN OrderedLocusNames=BA_0620, GBAA_0620, BAS0586;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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; AE016879; AAP24637.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29722.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52914.1; -; Genomic_DNA.
DR RefSeq; NP_843151.1; NC_003997.3.
DR RefSeq; WP_000095911.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_026863.1; NC_005945.1.
DR AlphaFoldDB; Q81V80; -.
DR SMR; Q81V80; -.
DR STRING; 261594.GBAA_0620; -.
DR DNASU; 1087998; -.
DR EnsemblBacteria; AAP24637; AAP24637; BA_0620.
DR EnsemblBacteria; AAT29722; AAT29722; GBAA_0620.
DR GeneID; 45020681; -.
DR KEGG; ban:BA_0620; -.
DR KEGG; bar:GBAA_0620; -.
DR KEGG; bat:BAS0586; -.
DR PATRIC; fig|198094.11.peg.618; -.
DR eggNOG; COG0156; Bacteria.
DR HOGENOM; CLU_015846_11_0_9; -.
DR OMA; MDTHGFG; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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_0000163833"
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; 43092 MW; 4E0DF2BB5945F0C2 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 LFSTAVTPAD AAACMRSIEI LMESTELHDR
LWENGRYLKQ GLKELGFNIG ESETPITPCI IGDEVLTQEF SKRLNEEGVY AKSIVFPTVA
KGTGRVRNMP TAAHTKEMLD EAIRKYEKVG KEMGII
