ID Q81DD4_BACCR Unreviewed; 558 AA.
AC Q81DD4;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=Indole-3-pyruvate decarboxylase {ECO:0000313|EMBL:AAP09396.1};
DE EC=4.1.1.74 {ECO:0000313|EMBL:AAP09396.1};
GN OrderedLocusNames=BC_2433 {ECO:0000313|EMBL:AAP09396.1};
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900 {ECO:0000313|EMBL:AAP09396.1, ECO:0000313|Proteomes:UP000001417};
RN [1] {ECO:0000313|EMBL:AAP09396.1, ECO:0000313|Proteomes:UP000001417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB
RC 9373 / NCTC 2599 / NRRL B-3711 {ECO:0000313|Proteomes:UP000001417};
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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}.
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DR EMBL; AE016877; AAP09396.1; -; Genomic_DNA.
DR RefSeq; NP_832195.1; NC_004722.1.
DR AlphaFoldDB; Q81DD4; -.
DR KEGG; bce:BC2433; -.
DR PATRIC; fig|226900.8.peg.2462; -.
DR HOGENOM; CLU_013748_0_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000001417; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IBA:GO_Central.
DR CDD; cd02005; TPP_PDC_IPDC; 1.
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; 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; IPR047214; TPP_PDC_IPDC.
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; 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:AAP09396.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001417};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 6..109
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..314
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 402..535
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 441
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 558 AA; 62564 MW; D83BEBF9FC01873C CRC64;
MKKQYTVSTY LLDRLHELGI EHIFGVPGDY NLAFLDDVVA HENLKWIGNC NELNAAYAAD
GYARIKGIAA LITTFGVGEL SAINGIAGSY AENVPVIKIT GTPPTKVMEN GAIVHHTLGD
GKFDHFSNMY REITVAQTNV TPEHAAEEID RVLRACWNEK RPVHINLPID VYNKPINKPT
EPIINKPILS NKEALNKMLL HAISKINSAK KPVILADFEV DRFHAKENLH QFVEKTGFPI
ATLSMGKGIF PEKHPQFIGI YTGDVSSPYL RKRIDESDCI ISIGVKLTDT ITGGFTQGFT
KEQVIEIHPY TVKIIDKKYG PVVMQDVLQH LSDSIEHRNK DTLDVKPFIL ESSPFTEEFI
PKAQMVTQKR FWQQMYHFLQ ENDVLIVEQG TPFFGSSAIP LPNNTAYVGQ PLWGSIGYTL
PALLGTQLAN LSRRNILIIG DGSFQVTAQE LSTILRQNLK PIIFLINNNG YTVERAIHGQ
NQLYNDIQMW DYNKLSMVFG AEEKSLTFKV ENEAELAAVL TNITFNKNQL IFIEVIMSQS
DQPELLAKLG KRSGQQNS
//
