ID R2SW83_9ENTE Unreviewed; 618 AA.
AC R2SW83;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Tyrosine decarboxylase {ECO:0000313|EMBL:EOH99465.1};
GN ORFNames=UAW_00617 {ECO:0000313|EMBL:EOH99465.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH99465.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH99465.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH99465.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) 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};
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:EOH99465.1}.
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DR EMBL; AJAR01000010; EOH99465.1; -; Genomic_DNA.
DR RefSeq; WP_010760827.1; NZ_KE136479.1.
DR AlphaFoldDB; R2SW83; -.
DR STRING; 155618.RV06_GL001038; -.
DR PATRIC; fig|1158608.3.peg.595; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 9803665at2; -.
DR Proteomes; UP000013858; 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; 3.40.640.10; 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 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; TYROSINE DECARBOXYLASE; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR Pfam; PF21391; tyr_de_CO2_C; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50}.
FT DOMAIN 471..611
FT /note="L-tyrosine decarboxylase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21391"
FT MOD_RES 390
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 618 AA; 69739 MW; 3BF5C2812D3496DE CRC64;
MKNFNTDDTN LKALFLGDKG ENVDLFKELL NKMIDEHVGW RQNYMPQDLP VISPQDRSSK
SFQETADNMR SVFNVLSSRL RTESLPWHSA GRFWGHMNAE TLMPSIIAYT TAMLWNGNNV
AYESSPATSQ MEEEVGLEFA TLMGYEDGWG HIAADGSIAN LEGLWYARNM KSLPWAIQAV
APEMVAGKSD WELLNMPTSE VLDILDQLQD KFDEIKANSA RSGKNLDKLG KWIVPQTKHY
SWLKAADIIG IGLDQVIAGE VNSEYRMDID KLEAQIRDLA AQGIPTLGVV GVVGSTEEGQ
VDRIDQIIAL RDKLAKEGIY FYVHVDAAYG GYGRSIFLDE NDQFIEWDKI EEVYAKHNIF
QEKNDWLTRE VYESFKAIEQ AESVTIDPHK MGYIPYSAGG VVIKDIRMRD VISYFATYVF
EKGADIPALL GAYILEGSKA GATAAAVWTA HKVLPLNVTG YGKLMGASIE GAYHFYHFID
GLEFKVGNKI IEIHALTKPD FNMVDYVFNE KGNTDLVKMN KLNHDFYDYA SYTKGGLYNN
EFITSHTDFA IEEYGHSPFE FVNSLGFSRA EWERADKVTI LRAAGMSPYM NDKEVFDDYA
EKIKVAIQEK LEAIYAEQ
//