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Database: UniProt
Entry: W1ISD5_9GAMM
LinkDB: W1ISD5_9GAMM
Original site: W1ISD5_9GAMM 
ID   W1ISD5_9GAMM            Unreviewed;       649 AA.
AC   W1ISD5;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Putative Tyrosine decarboxylase {ECO:0000313|EMBL:CDL80526.1};
DE            EC=4.1.1.25 {ECO:0000313|EMBL:CDL80526.1};
GN   ORFNames=XSR1_10012 {ECO:0000313|EMBL:CDL80526.1};
OS   Xenorhabdus szentirmaii DSM 16338.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL80526.1, ECO:0000313|Proteomes:UP000019202};
RN   [1] {ECO:0000313|EMBL:CDL80526.1, ECO:0000313|Proteomes:UP000019202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL80526.1,
RC   ECO:0000313|Proteomes:UP000019202};
RA   Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT   "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT   Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT   16338.";
RL   Submitted (NOV-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:CDL80526.1}.
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DR   EMBL; CBXF010000001; CDL80526.1; -; Genomic_DNA.
DR   RefSeq; WP_038233462.1; NZ_NIBV01000002.1.
DR   AlphaFoldDB; W1ISD5; -.
DR   STRING; 1427518.XSR1_10012; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000019202; Unassembled WGS sequence.
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; IPR021115; Pyridoxal-P_BS.
DR   InterPro; IPR049373; TyrDC_C.
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, ECO:0000313|EMBL:CDL80526.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019202}.
FT   DOMAIN          487..626
FT                   /note="L-tyrosine decarboxylase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21391"
FT   MOD_RES         397
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   649 AA;  73585 MW;  67746C7D6AB54EC5 CRC64;
     MTKSLRPNLN IDALFLGPKS ENAVFFREMM DYAISEHIHW RSGFHPSDAT FITSLDRHEH
     DYRETLYQTE GILNQLSAKL KNTSVPFFSP RYLGHINSDT LMVSNLAYVM AMIYNQNNCT
     YEVSPTTTEL ELESGLDLCR MFGYDPEKSW GHITSGGTVA NYEGLWVARN LKTLPFAIYQ
     HPKTKALLSH KSPQQLKNMP TAEILDLITE IQKIGVFEEI RDMTCRGIGV KPEILGKLLV
     PQSKHYSWTK AADIFGIGQE NIISLPVNEH YQTDVAKMRE ITFQLIEQGE PILAMIAVVG
     TTEVGAIDRI DEVVALRQEC EKRYGESFYI HVDAAYAGYA CSMLLNEQGE FLEYDTLHSH
     HRSIGIMPEE ISWPKPEVYE SFKALKHVDS ITVDPHKVGF IQYSAGAICM KDKRILGLIS
     SKAAYVFAQD ENQKEATGIN RGILGSAIME GSKAGATAAA LWAAHRLLPL NISGYGKVIA
     AGIVTAHKLL SKLSTLPPIV VGKHRFEVHT MLSPDFHMIN FTFKEIGNES LNNHNALNKR
     LYELCSYSTG RAYTNDFLTS STALDYKEYG DTPWHYAEKC GFSREEWEKV HRIYVLRAAI
     MTYCLRNEEH FQEFWQQLNA IFIKKLNQLV DEEEKKSRLI SGLYTPFIS
//
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