ID A7GHE9_CLOBL Unreviewed; 417 AA.
AC A7GHE9;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Decarboxylase family protein {ECO:0000313|EMBL:ABS41991.1};
GN OrderedLocusNames=CLI_2984 {ECO:0000313|EMBL:ABS41991.1};
OS Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS41991.1, ECO:0000313|Proteomes:UP000002410};
RN [1] {ECO:0000313|Proteomes:UP000002410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Langeland / NCTC 10281 / Type F
RC {ECO:0000313|Proteomes:UP000002410};
RA Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR EMBL; CP000728; ABS41991.1; -; Genomic_DNA.
DR RefSeq; WP_012100712.1; NC_009699.1.
DR AlphaFoldDB; A7GHE9; -.
DR KEGG; cbf:CLI_2984; -.
DR HOGENOM; CLU_028929_2_1_9; -.
DR Proteomes; UP000002410; Chromosome.
DR GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382}.
FT MOD_RES 263
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 417 AA; 48286 MW; B66A3FBF65B38BEA CRC64;
MKFWRKYTQQ EMDEKITKSL EKTLNYDNTK TIGIPGTKLD DTVFYDGHSF VKHSPYLRTF
IQNPNHIGCH TYDKADILFG GTFDIERELI QLLAIDVLNG NDEEFDGYVT QGGTEANIQA
MWVYRNYFKK ERKAKHDEIA IITSADTHYS AYKGADLLNI DIIKVPVDFH SRKIEEKTLD
NIVKEAKEIG KKYFIVISNM GTTMFGSVDD PDLYANIFDR YNLEYKIHVD GAFGGFIYPI
NNKECKTDFS NKNVSSITLD GHKMLQAPYG TGIFVCRKNL IHNTLTKEAT YIENLDVTLS
GSRSGSNAVS IWMVLASYGP YGWMEKINKL RNRTKWLCKQ LNDMGIKYYK EDSMNIVTIE
EQYVNKEIAE KYFLVPEVHN PTNKWYKIVV MEHVELDILN SLVYDLKKFN KEHLKAM
//
