ID A0A1E5GUG8_9ENTE Unreviewed; 548 AA.
AC A0A1E5GUG8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Indole-3-pyruvate decarboxylase {ECO:0000313|EMBL:OEG16312.1};
GN ORFNames=BCR23_05330 {ECO:0000313|EMBL:OEG16312.1};
OS Enterococcus quebecensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=903983 {ECO:0000313|EMBL:OEG16312.1, ECO:0000313|Proteomes:UP000094764};
RN [1] {ECO:0000313|EMBL:OEG16312.1, ECO:0000313|Proteomes:UP000094764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26306 {ECO:0000313|EMBL:OEG16312.1,
RC ECO:0000313|Proteomes:UP000094764};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OEG16312.1}.
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DR EMBL; MIKB01000013; OEG16312.1; -; Genomic_DNA.
DR RefSeq; WP_069634766.1; NZ_MIKB01000013.1.
DR AlphaFoldDB; A0A1E5GUG8; -.
DR STRING; 903983.BCR23_05330; -.
DR PATRIC; fig|903983.4.peg.2556; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000094764; Unassembled WGS sequence.
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:OEG16312.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..112
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 200..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..517
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 430
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 459
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 548 AA; 60450 MW; 0250A3E623419B52 CRC64;
MYTVADYLLD RLKEVGIDDI FGVPGDYNLK FLDHITARND LNWIGNANEL NAAYMADGYA
RTKGVSAFVT TFGVGELSAI NGLAGSYAEN VPVIEIVGSP TTTVQEGKKL VHHTLGDGDF
SHFEKMHEKV TAAIAHLTVE NALTEIDRVL TIAMTQKRPV YLNLPIDVAE IKVSKPNTPL
LTEQKELTNT ESELLDIVEK ALTNSVNPVI IAGHEILSYH LEKHLDNFIQ KYNLPVTTLP
FGKGAFNEED PHYLGTYSGS PTTEPLKSRV DEADLVLLLG AKLTDSATSG FSFGFTDKQI
LSIGSTEISI HGEKQAGIQL DRFIPALKTI NYSGFIGEIN PLKRLSNGEN TTEKLTQKHF
WEMVETFLIQ GDTVVGEQGT SFFGLTNVPL KKAMHFIGQP LWGSIGYTFP SALGSQMANK
ASRHLLFIGD GSLQLTVQEL GTALREGLTP IVFVINNNGY TVEREIHGAT EPYNDIPMWD
YQHLPLVFGG TKDSVATYKV TTEIELDNAM KAARKDTQRL QWIEVVMDQE DAPDLLKKLA
KNFAKQNS
//
