ID   TRPDC_CLOS1             Reviewed;         417 AA.
AC   J7SZ64;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Tryptophan decarboxylase {ECO:0000303|PubMed:25263219};
DE            Short=Trp decarboxylase {ECO:0000303|PubMed:25263219};
DE            EC=4.1.1.105 {ECO:0000269|PubMed:25263219};
GN   ORFNames=CLOSPO_02083 {ECO:0000312|EMBL:EDU35915.1};
OS   Clostridium sporogenes (strain ATCC 15579).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=471871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15579;
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J., Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R.,
RA   Wilson R.K.;
RT   "Draft genome sequence of Clostridium sporogenes ATCC 15579.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBCELLULAR LOCATION.
RC   STRAIN=ATCC 15579;
RX   PubMed=25263219; DOI=10.1016/j.chom.2014.09.001;
RA   Williams B.B., Van Benschoten A.H., Cimermancic P., Donia M.S.,
RA   Zimmermann M., Taketani M., Ishihara A., Kashyap P.C., Fraser J.S.,
RA   Fischbach M.A.;
RT   "Discovery and characterization of gut microbiota decarboxylases that can
RT   produce the neurotransmitter tryptamine.";
RL   Cell Host Microbe 16:495-503(2014).
CC   -!- FUNCTION: Catalyzes the decarboxylation of tryptophan to tryptamine.
CC       Tryptamine is a neurotransmitter that induces the release of serotonin,
CC       which is suggested to modulate gastrointestinal motility. Therefore,
CC       the tryptophan decarboxylase from the gut bacteria Clostridium
CC       sporogenes (strain ATCC 15579) may influence host brain and behavior.
CC       Has weak activity with tyrosine. Activity against phenylalanine is
CC       undetectable. {ECO:0000269|PubMed:25263219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-tryptophan = CO2 + tryptamine; Xref=Rhea:RHEA:30339,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57887,
CC         ChEBI:CHEBI:57912; EC=4.1.1.105;
CC         Evidence={ECO:0000269|PubMed:25263219};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:A7B1V0};
CC   -!- ACTIVITY REGULATION: Inhibited by (S)-alpha-fluoromethyltryptophan.
CC       {ECO:0000269|PubMed:25263219}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 mM for tryptophan {ECO:0000269|PubMed:25263219};
CC         Note=kcat is 1200 min(-1) with tryptophan as substrate.
CC         {ECO:0000269|PubMed:25263219};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Note=In vitro,
CC       tryptamine is excreted into the extracellular fluid, suggesting that
CC       the bacterium has the potential to excrete tryptamine in the host gut
CC       lumen. {ECO:0000269|PubMed:25263219}.
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000305}.
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DR   EMBL; ABKW02000004; EDU35915.1; -; Genomic_DNA.
DR   RefSeq; WP_003484002.1; NZ_DS981517.1.
DR   AlphaFoldDB; J7SZ64; -.
DR   SMR; J7SZ64; -.
DR   EnsemblBacteria; EDU35915; EDU35915; CLOSPO_02083.
DR   HOGENOM; CLU_028929_2_1_9; -.
DR   Proteomes; UP000006610; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0036469; F:L-tryptophan decarboxylase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Decarboxylase; Lyase; Pyridoxal phosphate.
FT   CHAIN           1..417
FT                   /note="Tryptophan decarboxylase"
FT                   /id="PRO_0000446223"
FT   MOD_RES         263
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:A7B1V0"
SQ   SEQUENCE   417 AA;  48413 MW;  4BCA9ABD6E85194C CRC64;
     MKFWRKYTQQ EMDEKITESL EKTLNYDNTK TIGIPGTKLD DTVFYDDHSF VKHSPYLRTF
     IQNPNHIGCH TYDKADILFG GTFDIERELI QLLAIDVLNG NDEEFDGYVT QGGTEANIQA
     MWVYRNYFKK ERKAKHEEIA IITSADTHYS AYKGSDLLNI DIIKVPVDFY SRKIQENTLD
     SIVKEAKEIG KKYFIVISNM GTTMFGSVDD PDLYANIFDK YNLEYKIHVD GAFGGFIYPI
     DNKECKTDFS NKNVSSITLD GHKMLQAPYG TGIFVSRKNL IHNTLTKEAT YIENLDVTLS
     GSRSGSNAVA IWMVLASYGP YGWMEKINKL RNRTKWLCKQ LNDMRIKYYK EDSMNIVTIE
     EQYVNKEIAE KYFLVPEVHN PTNNWYKIVV MEHVELDILN SLVYDLRKFN KEHLKAM