ID A0A0A7FS35_9CLOT Unreviewed; 617 AA.
AC A0A0A7FS35;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Tyrosine decarboxylase {ECO:0000313|EMBL:AIY82348.1};
DE EC=4.1.1.25 {ECO:0000313|EMBL:AIY82348.1};
GN Name=tdc {ECO:0000313|EMBL:AIY82348.1};
GN ORFNames=U729_1871 {ECO:0000313|EMBL:AIY82348.1};
OS Clostridium baratii str. Sullivan.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1415775 {ECO:0000313|EMBL:AIY82348.1, ECO:0000313|Proteomes:UP000030635};
RN [1] {ECO:0000313|EMBL:AIY82348.1, ECO:0000313|Proteomes:UP000030635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sullivan {ECO:0000313|EMBL:AIY82348.1};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
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DR EMBL; CP006905; AIY82348.1; -; Genomic_DNA.
DR RefSeq; WP_039314057.1; NZ_CP006905.1.
DR AlphaFoldDB; A0A0A7FS35; -.
DR STRING; 1561.NPD11_1144; -.
DR GeneID; 60852369; -.
DR KEGG; cbv:U729_1871; -.
DR eggNOG; COG0076; Bacteria.
DR HOGENOM; CLU_005446_0_1_9; -.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000030635; 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:0004837; F:tyrosine decarboxylase activity; IEA:UniProtKB-EC.
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 InterPro; IPR049373; TyrDC_C.
DR InterPro; IPR022397; Tyrosine_deCO2ase_bac.
DR NCBIfam; TIGR03811; tyr_de_CO2_Ent; 1.
DR PANTHER; PTHR42735; -; 1.
DR PANTHER; PTHR42735:SF4; -; 1.
DR Pfam; PF00282; Pyridoxal_deC; 2.
DR Pfam; PF21391; tyr_de_CO2_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AIY82348.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000030635}.
FT DOMAIN 470..610
FT /note="L-tyrosine decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21391"
FT MOD_RES 389
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 617 AA; 69450 MW; E71038C9C11F3935 CRC64;
MSGQDLNLKA LFLGPKSENK ETFSKHLNTL LQDHSEWRKN YHPEDKNIIK TSDFHAEDFQ
MTADKMNDVL VELSRKLRSK SLPWHSPRFL GHMNSETLMP ALLGYFAGML YNGNNVAYES
SPGTSEMEEE VGADFAKLMG YEDGIGWGHI CADGSIANLE AIWYARNIKS LPLAMKEVAP
ELVEGKSEWE LLNMSTKEIL DLVDRVPEQL DDLKAKSARS GKNLGKLGKW FVPQTKHYSW
LKSADIIGIG LDQVEAVEVN EQYRMNTEVL EKRIRELAAQ GIPTLGVVGV VGSTEEGAVD
DIHKIIAVRD KLAKEGINFY VHVDAAYGGY ARSIFLDENY DFIPKEELKA KYLEHGVFLN
EETEWPSDDT YEAFKAISEC DTVTIDPHKM GYIPYSAGGI VVKDKRMRES ISYFATYVFE
KGMDIPALLG AFMLEGSKAG ATAASVWAAH RTLPLNITGY GKLIGAGIEG SFNLYNHFNG
KEFIVGGKKI ILNTLIRPDF NMVDFAFNEE GNTDLVKMNQ LNHDFYEEAS YARGGLYEND
FITSHTDFAV PDYGNSPYPF VKSLGFSRES WDEVQKVTVL RACVLSPFIN DKETFAEYME
KVDTAIQRKL ENIYDVR
//