ID A0A3R7HE81_9STRA Unreviewed; 515 AA.
AC A0A3R7HE81;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Tyrosine decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BBI17_008747 {ECO:0000313|EMBL:RLN10151.1}, BBO99_00008220
GN {ECO:0000313|EMBL:RLN75591.1}, JM16_007963
GN {ECO:0000313|EMBL:KAG2513473.1}, JM18_007733
GN {ECO:0000313|EMBL:KAG2518277.1};
OS Phytophthora kernoviae.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=325452 {ECO:0000313|EMBL:RLN75591.1, ECO:0000313|Proteomes:UP000285624};
RN [1] {ECO:0000313|EMBL:KAG2513473.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2513473.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2518277.1};
RX PubMed=26981359;
RA Studholme D.J., McDougal R.L., Sambles C., Hansen E., Hardy G., Grant M.,
RA Ganley R.J., Williams N.M.;
RT "Genome sequences of six Phytophthora species associated with forests in
RT New Zealand.";
RL Genom Data 7:54-56(2015).
RN [2] {ECO:0000313|Proteomes:UP000285624, ECO:0000313|Proteomes:UP000285883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Chile2 {ECO:0000313|EMBL:RLN10151.1}, and Chile4
RC {ECO:0000313|EMBL:RLN75591.1};
RA Studholme D.J., Sanfuentes E., Panda P., Hill R., Sambles C., Grant M.,
RA Williams N.M., Mcdougal R.L.;
RT "Genome sequencing of oomycete isolates from Chile give support for New
RT Zealand origin for Phytophthora kernoviae and make available the first
RT Nothophytophthora sp. genome.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2513473.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NZFS 2646 {ECO:0000313|EMBL:KAG2513473.1}, and NZFS 3630
RC {ECO:0000313|EMBL:KAG2518277.1};
RA Studholme D.J.;
RL Submitted (JUN-2020) 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|ARBA:ARBA00009533, 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:RLN75591.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JPWV03000388; KAG2513473.1; -; Genomic_DNA.
DR EMBL; JPWU03000372; KAG2518277.1; -; Genomic_DNA.
DR EMBL; MAYM02001877; RLN10151.1; -; Genomic_DNA.
DR EMBL; MBDN02000403; RLN75591.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7HE81; -.
DR STRING; 325452.A0A3R7HE81; -.
DR Proteomes; UP000285624; Unassembled WGS sequence.
DR Proteomes; UP000285883; Unassembled WGS sequence.
DR Proteomes; UP000785171; Unassembled WGS sequence.
DR Proteomes; UP000792063; Unassembled WGS sequence.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 1.20.1340.10; dopa decarboxylase, N-terminal domain; 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 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 PRINTS; PR00800; YHDCRBOXLASE.
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:UP000285624}.
FT MOD_RES 331
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 515 AA; 56296 MW; 008F7A31B413AD75 CRC64;
MHDSVTTAAT FCSGLISGAA LLAVVQHLAR HRALESTSPL DARDPEAIRH PAAALTELLP
GSLVAQLPTE CPEDPQSYAD IFRDVEQLIF PALSHWASPS FHAYFKICGS DPSVLADYLC
SSLDVVGFSW ISAPAATELE QVVCDWLAKL LALPECFLTS SPGGGVIQGS ASESALCALI
AARNSALEGL EGATRQEKAA KLVVYVSDQT HAIAEKGCMV LDIPHLRVVS TVRGKVDKDN
YGLAPEDVAH AMAEDRAKGL VPFCLMPTVG TTSTTAIDPL QDLIAVARAQ PEHVWVHLDG
AYGGAACVCP EYQHWLDGAE GCDSICVNTH KWLLVSFDAS LLWVKDRRPL IRALAHNPEY
LKNDFMQSAP NYKDWQVPLG RRFRALKLWF TFRRFGASGL RAHIRQSVAL AKQAEELLAK
DARFEFFVRA RMGLVCFYVA FGGRELNEAL LRRVNESGKA FLIHSVVDGV HFLRLAIGGL
EVDTWHIENV VHVLSTTLSE VIAENPKWQK LQALS
//
