ID Q4LAE7_STAHJ Unreviewed; 472 AA.
AC Q4LAE7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 123.
DE RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=SH0069 {ECO:0000313|EMBL:BAE03378.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE03378.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE03378.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE03378.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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DR EMBL; AP006716; BAE03378.1; -; Genomic_DNA.
DR RefSeq; WP_002498810.1; NC_007168.1.
DR AlphaFoldDB; Q4LAE7; -.
DR KEGG; sha:SH0069; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_011856_0_4_9; -.
DR Proteomes; UP000000543; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR CDD; cd06450; DOPA_deC_like; 1.
DR Gene3D; 3.90.1150.170; -; 1.
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; IPR010977; Aromatic_deC.
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; 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 PRINTS; PR00800; YHDCRBOXLASE.
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 290
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 472 AA; 53129 MW; BDFA2C07604B83AC CRC64;
MEFNENNIDL ETIIRDEVNK YLSRDIGDLP ATQQAPLELR EKYEKMEVPN KGRDIYEVLK
DLNNEVLNYL YRPNHPRSFS FIPGPASRLS WLGDILTTAN NIHASNFANA TLPINIERNL
INYLVGKIGY EIKPAGGVFV SGGSMANLTA IVAARDAQVE MEDIKKATVY LTSQTHHSVG
KALHVAGFLK NNIRRIEYND DFTMNTDSLK AAIDKDIEEG YKPAMVIATA GTTNTGSVDD
FTTLGDICDH YNLWLHVDGA YGLSHILSDK AQHLFKGIER SDSASWDAHK LLFQTYSCAM
VIVKEKNHLL QSFGEDAEYL DDIASDDDVI DPEMLGIELT RPARALKLWI TLQVIGEDEI
IERIKYGEGL AEYAEEYVSS LDNWRIISHA NLSIVNFRYE NSDLTEAQNN QLNSMAAQKI
ADSGYAIAYT TVLNNQRVIR LCTTNPLTTH DDIRETINRL DQYIGDYDMK DA
//
