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Database: UniProt
Entry: Q6GWG3_AZOBR
LinkDB: Q6GWG3_AZOBR
Original site: Q6GWG3_AZOBR 
ID   Q6GWG3_AZOBR            Unreviewed;       208 AA.
AC   Q6GWG3;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   SubName: Full=Indole-3-pyruvate decarboxylase {ECO:0000313|EMBL:AAT46130.1};
DE   Flags: Fragment;
GN   Name=ipdC {ECO:0000313|EMBL:AAT46130.1};
OS   Azospirillum brasilense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192 {ECO:0000313|EMBL:AAT46130.1};
RN   [1] {ECO:0000313|EMBL:AAT46130.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sp245 {ECO:0000313|EMBL:AAT46130.1};
RX   PubMed=16232298; DOI=10.1111/j.1462-2920.2005.00848.x;
RA   Rothballer M., Schmid M., Fekete A., Hartmann A.;
RT   "Comparative in situ analysis of ipdC-gfpmut3 promoter fusions of
RT   Azospirillum brasilense strains Sp7 and Sp245.";
RL   Environ. Microbiol. 7:1839-1846(2005).
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}.
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DR   EMBL; AY628754; AAT46130.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6GWG3; -.
DR   GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Pyruvate {ECO:0000313|EMBL:AAT46130.1}.
FT   DOMAIN          1..105
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   NON_TER         208
FT                   /evidence="ECO:0000313|EMBL:AAT46130.1"
SQ   SEQUENCE   208 AA;  21395 MW;  C27851C65B29B5B4 CRC64;
     MKLAEALLRA LKDRGAQAMF GIPGDSACPS LGGGGNADPA APHAEHEPPV GFAADAAARY
     SSTLGVAAVT YGSGAFNMVN AVAGAYAEKS PVVVISGAPG TTEGNPGLLL HHQDRTLDTQ
     FQVFKEITVA QARLDDPAKA PAEIARVLGA ARALSRPVYL EIPRNMVNAE VEPVGDDPAW
     PVDRDALAAC ADEVLAAMRS ATSPVQMV
//
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