ID B7JPK0_BACC0 Unreviewed; 558 AA.
AC B7JPK0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Putative indolepyruvate decarboxylase {ECO:0000313|EMBL:ACK90871.1};
GN OrderedLocusNames=BCAH820_2507 {ECO:0000313|EMBL:ACK90871.1};
OS Bacillus cereus (strain AH820).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405535 {ECO:0000313|EMBL:ACK90871.1, ECO:0000313|Proteomes:UP000001363};
RN [1] {ECO:0000313|EMBL:ACK90871.1, ECO:0000313|Proteomes:UP000001363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH820 {ECO:0000313|EMBL:ACK90871.1,
RC ECO:0000313|Proteomes:UP000001363};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH820.";
RL Submitted (OCT-2008) 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}.
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DR EMBL; CP001283; ACK90871.1; -; Genomic_DNA.
DR AlphaFoldDB; B7JPK0; -.
DR KEGG; bcu:BCAH820_2507; -.
DR HOGENOM; CLU_013748_0_2_9; -.
DR Proteomes; UP000001363; Chromosome.
DR GO; GO:0016831; F:carboxy-lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:ACK90871.1};
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..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 401..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; 62804 MW; 0A21A9F2DD858A16 CRC64;
MKTQYTVSTY LLDRLSELGI EHIFGVPGDY NLAFLDYVLA HKNLEWIGNC NELNAAYAAD
GYARIKGIAA LITTFGVGEL SAINGIAGSY AENVPVIKIT GTPTTTVMEN GELVHHTLGD
GKFNHFSNMY REITVAQTNL TPEHAVEEID RVLRACWNEK RPVHINLPID VYNKPINKPA
GPILHKPILS NKETLDKMLL HAISKINSAK KPIILADFEV DRFHAKEYLY QFVEKTGFPI
ATLSMGKGIF PEKHPQFIGI YTGDVSSPYL RKRIDESDCI ISIGVKLTDT ITGGFTQGFT
KEQVIEIHPY TVKITDKKYG PVVMKDVLQQ LSDVIEHRNE ETLDIKPFIS ESLSMTEEFN
PKAQMVTQKR FWQQIYHFLQ ENDVLLAEQG TPFFGSAAIP LPNDTTYVAQ PLWGSIGYTL
PALLGTQLAN LSRRNILIIG DGSFQLTVQE LSTMLRQNLK PIIFLINNNG YTVERAIHGQ
IEPYNDIQMW EYTKLANVFG TEEKSQTFKV ENETELQEVL TKISIDKDQL TFVEVVMSQG
DQPELLAKLG KRFGQQNS
//
