ID F8JK20_STREN Unreviewed; 382 AA.
AC F8JK20; G8XHK7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Histidine decarboxylase {ECO:0000313|EMBL:AEW99844.1};
GN OrderedLocusNames=SCATT_p16510 {ECO:0000313|EMBL:AEW99844.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OG Plasmid pSCATT {ECO:0000313|EMBL:AEW99844.1,
OG ECO:0000313|Proteomes:UP000007842}.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW99844.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RC PLASMID=Plasmid pSCATT {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC 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; CP003229; AEW99844.1; -; Genomic_DNA.
DR RefSeq; WP_014150550.1; NC_017585.1.
DR AlphaFoldDB; F8JK20; -.
DR KEGG; scy:SCATT_p16510; -.
DR PATRIC; fig|1003195.11.peg.86; -.
DR HOGENOM; CLU_028929_0_2_11; -.
DR OrthoDB; 3335676at2; -.
DR Proteomes; UP000007842; Plasmid pSCATT.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProt.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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 PANTHER; PTHR46101; -; 1.
DR PANTHER; PTHR46101:SF2; SERINE DECARBOXYLASE; 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 Plasmid {ECO:0000313|EMBL:AEW99844.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000007842}.
FT MOD_RES 245
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 382 AA; 40403 MW; 24271D448C7D9A08 CRC64;
MNSPLRIEED GVAAEQVWSV VTAMVGELRQ RVPRMLGFPA NLAWDASAAH SLLSMLINNA
GDPSEHDDSG NDVKSFERAV LSWFTGIAGG DRDTYGYVTA SGSEGILFGL FVARHRFPRA
PVYLSADAHY SVRKAATILR METVTVPCRD DGTMDPSALA RLCRRHRDAR GGRPGDGAVV
VATIGTVMRG AVDDLPALRE AALAAGGVHL HADAALGGLV AAFCHPEPAW NLAHGADSVS
VSGHKLLGCP VPCGVVLTPR RYLPPAPTGQ YLGAPDHTLG CSRSGLAAAL LWCRLREAGT
RGVRETVHRC RRTAAYATEA LAAAGAHPER FPGALTVTFD RPGPRTCATW HLATQGDRAH
LVAMPHVTPQ AVDALCADLR GS
//
