ID Q135I6_RHOPS Unreviewed; 543 AA.
AC Q135I6;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Phenylpyruvate decarboxylase {ECO:0000313|EMBL:ABE40253.1};
DE EC=4.1.1.43 {ECO:0000313|EMBL:ABE40253.1};
GN OrderedLocusNames=RPD_3027 {ECO:0000313|EMBL:ABE40253.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE40253.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE40253.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE40253.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR036565-2};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000256|PIRSR:PIRSR036565-2};
CC -!- COFACTOR:
CC Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC Evidence={ECO:0000256|ARBA:ARBA00001920};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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; CP000283; ABE40253.1; -; Genomic_DNA.
DR AlphaFoldDB; Q135I6; -.
DR STRING; 316057.RPD_3027; -.
DR KEGG; rpd:RPD_3027; -.
DR eggNOG; COG3961; Bacteria.
DR HOGENOM; CLU_013748_0_2_5; -.
DR BioCyc; RPAL316057:RPD_RS15200-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050177; F:phenylpyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:InterPro.
DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR017765; IPDC.
DR InterPro; IPR012110; PDC/IPDC-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR NCBIfam; TIGR03394; indol_phenyl_DC; 1.
DR PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:ABE40253.1};
KW Magnesium {ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR036565-2};
KW Pyruvate {ECO:0000313|EMBL:ABE40253.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..110
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 382..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 428
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 455
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 543 AA; 57924 MW; 0B899F1846DE8D68 CRC64;
MPTLATALLD ALKDHGAKEI FGIPGDFVLP FFKVIEESGT LPYFTVSHEP AVGFAADAAS
RYRGGIGVAV VTYGAGAFNL VNSIAGAYAE RSPVVVIAGA PGARERTSGY LLHHQVRTVD
TQLAVFKEVT CAQAVLDDPL TAPAEIARVL RCALELSLPV YIEFPRDMVD AKVDPVVKLP
QREADPGALA ECSEEILARI AKAKSPVVVV DVEIRRYGVE KQVAALARKL GLPVVTTFMG
RGLLEGDDDV VAGTYLGAAG DSGLSALVEE SDLVLMFGVI LSDTNFALST NMTDPRRTVL
ATGREVQIGH HVYRDLPLAD LIAGLDAHAT QHPPRPRNAG QGMVYPRNLV ADASAIAPSD
IATAINDLFD RHGKMPMTAD IGDCLFTAME IDNTALAAPG YYAGMGFGVP AGFGVAATGL
RPLILVGDGA FQMTGWELGN CKRYGLDPIV VLFNNCSWEM LRVFQPESKF NDLDDWHFAD
IAPSIGGHGV RVTTRAELAA ALDAAVKRRG QFSLIEVMLP RGATSHTLAR FVAGFKAARE
RMK
//
