ID   F5LHV5_9BACL            Unreviewed;       490 AA.
AC   F5LHV5;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Pyridoxal-dependent decarboxylase domain protein {ECO:0000313|EMBL:EGL18054.1};
GN   ORFNames=HMPREF9413_4124 {ECO:0000313|EMBL:EGL18054.1};
OS   Paenibacillus sp. HGF7.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=944559 {ECO:0000313|EMBL:EGL18054.1, ECO:0000313|Proteomes:UP000003445};
RN   [1] {ECO:0000313|EMBL:EGL18054.1, ECO:0000313|Proteomes:UP000003445}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HGF7 {ECO:0000313|EMBL:EGL18054.1,
RC   ECO:0000313|Proteomes:UP000003445};
RA   Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA   Nelson K.E.;
RL   Submitted (FEB-2011) 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.
CC       {ECO:0000256|RuleBase:RU000382}.
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:EGL18054.1}.
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DR   EMBL; AFDH01000056; EGL18054.1; -; Genomic_DNA.
DR   RefSeq; WP_009673905.1; NZ_AFDH01000056.1.
DR   AlphaFoldDB; F5LHV5; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000003445; Unassembled WGS sequence.
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; 3.90.1150.170; -; 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; IPR021115; Pyridoxal-P_BS.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00392; DDC_GAD_HDC_YDC; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003445}.
FT   MOD_RES         304
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   490 AA;  54740 MW;  C7028193D8AFAA34 CRC64;
     MMKHNSIFNL DTDERMDIGT YLLEQINDYM TNIRGVRVSP ELSVDAIAEH SRKLSFEHPV
     SAREAINHIL EGLRQFQVHT PHPRYFGLYN PRPNFMGIMA DTITAAFNPQ LAAWSHAPVA
     VEMENYVLKE IASRFGYSAD AADGTFTTGG AEANLTAVLT ALVHYFPSYA KEGLRSLPSH
     PVMYASAESH HSLVKAARSC GLGTDSLRII TTGSEMHIDV HALHHQIQVD RAAGYTPFLI
     IATGGTTGAG AIDPINEMAN LAEREQLWLH VDAAYGGASV FAPELRDLLR GIDRADSITF
     DAHKWMSVPM GAGIYITRHK DILHRTFSIT ADYMPKEGAD LDVIDPFTHS IQWSRRFIGL
     KVYLSLVTAG WEGYRSMVQH QTEMGNRLRR ELTFSNWKVV NDTVLPVVCF TDSNIQSKSQ
     SNFASFICQE ILHSGQAWIS VYETNKAPVL RACITNYDTT EEDIMVLMQL LNGARAKYLE
     ETSERSELNL
//