TRPDC_RUMGV
ID TRPDC_RUMGV Reviewed; 490 AA.
AC A7B1V0;
DT 13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 25-MAY-2022, entry version 63.
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=RUMGNA_01526 {ECO:0000312|EMBL:EDN78222.1};
OS Ruminococcus gnavus (strain ATCC 29149 / VPI C7-9).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=411470;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29149 / VPI C7-9;
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29149 / VPI C7-9;
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus gnavus (ATCC 29149).";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:4OBU, ECO:0007744|PDB:4OBV}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEXES WITH PYRIDOXAL
RP PHOSPHATE AND INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 29149 / VPI C7-9;
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 Ruminococcus gnavus
CC (strain ATCC 29149 / VPI C7-9) may influence host brain and behavior.
CC Has weak activity with tyrosine and phenylalanine.
CC {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:0000269|PubMed:25263219};
CC -!- ACTIVITY REGULATION: Inhibited by (S)-alpha-fluoromethyltryptophan.
CC {ECO:0000269|PubMed:25263219}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 mM for tryptophan {ECO:0000269|PubMed:25263219};
CC KM=70 mM for phenylalanine {ECO:0000269|PubMed:25263219};
CC Note=kcat is 4400 min(-1) with tryptophan as substrate. kcat is 230
CC min(-1) with phenylalanine as substrate.
CC {ECO:0000269|PubMed:25263219};
CC -!- SUBUNIT: Homodimer. {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; AAYG02000011; EDN78222.1; -; Genomic_DNA.
DR PDB; 4OBU; X-ray; 2.80 A; A/B/C/E/F/G/H/U=1-490.
DR PDB; 4OBV; X-ray; 2.84 A; A/B/C/D=1-490.
DR PDBsum; 4OBU; -.
DR PDBsum; 4OBV; -.
DR AlphaFoldDB; A7B1V0; -.
DR SMR; A7B1V0; -.
DR STRING; 411470.RUMGNA_01526; -.
DR PRIDE; A7B1V0; -.
DR EnsemblBacteria; EDN78222; EDN78222; RUMGNA_01526.
DR eggNOG; COG0076; Bacteria.
DR Proteomes; UP000004410; 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:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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 Pfam; PF00282; Pyridoxal_deC; 1.
DR PRINTS; PR00800; YHDCRBOXLASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00392; DDC_GAD_HDC_YDC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Decarboxylase; Lyase; Pyridoxal phosphate.
FT CHAIN 1..490
FT /note="Tryptophan decarboxylase"
FT /id="PRO_0000446224"
FT MOD_RES 306
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:25263219"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:4OBU"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 105..117
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:4OBU"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 193..201
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 238..247
FT /evidence="ECO:0007829|PDB:4OBU"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:4OBU"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 297..303
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:4OBV"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 361..371
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 373..394
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 400..407
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 410..415
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:4OBU"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:4OBU"
FT HELIX 466..485
FT /evidence="ECO:0007829|PDB:4OBU"
SQ SEQUENCE 490 AA; 54956 MW; 8E229384AC0CD998 CRC64;
MSQVIKKKRN TFMIGTEYIL NSTQLEEAIK SFVHDFCAEK HEIHDQPVVV EAKEHQEDKI
KQIKIPEKGR PVNEVVSEMM NEVYRYRGDA NHPRFFSFVP GPASSVSWLG DIMTSAYNIH
AGGSKLAPMV NCIEQEVLKW LAKQVGFTEN PGGVFVSGGS MANITALTAA RDNKLTDINL
HLGTAYISDQ THSSVAKGLR IIGITDSRIR RIPTNSHFQM DTTKLEEAIE TDKKSGYIPF
VVIGTAGTTN TGSIDPLTEI SALCKKHDMW FHIDGAYGAS VLLSPKYKSL LTGTGLADSI
SWDAHKWLFQ TYGCAMVLVK DIRNLFHSFH VNPEYLKDLE NDIDNVNTWD IGMELTRPAR
GLKLWLTLQV LGSDLIGSAI EHGFQLAVWA EEALNPKKDW EIVSPAQMAM INFRYAPKDL
TKEEQDILNE KISHRILESG YAAIFTTVLN GKTVLRICAI HPEATQEDMQ HTIDLLDQYG
REIYTEMKKA
