ID F3YC03_MELPT Unreviewed; 556 AA.
AC F3YC03;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Pyruvate decarboxylase, alpha-keto-acid decarboxylase {ECO:0000313|EMBL:BAK22031.1};
DE EC=4.1.1.- {ECO:0000313|EMBL:BAK22031.1};
DE EC=4.1.1.1 {ECO:0000313|EMBL:BAK22031.1};
GN OrderedLocusNames=MPTP_1603 {ECO:0000313|EMBL:BAK22031.1};
OS Melissococcus plutonius (strain ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB
OS 702443).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Melissococcus.
OX NCBI_TaxID=940190 {ECO:0000313|EMBL:BAK22031.1, ECO:0000313|Proteomes:UP000008456};
RN [1] {ECO:0000313|EMBL:BAK22031.1, ECO:0000313|Proteomes:UP000008456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35311 / CIP 104052 / LMG 20360 / NCIMB 702443
RC {ECO:0000313|Proteomes:UP000008456};
RX PubMed=21622755; DOI=10.1128/JB.05151-11;
RA Okumura K., Arai R., Okura M., Kirikae T., Takamatsu D., Osaki M.,
RA Miyoshi-Akiyama T.;
RT "Complete genome sequence of Melissococcus plutonius ATCC 35311.";
RL J. Bacteriol. 193:4029-4030(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 35311;
RA Okumura K., Arai R., Osaki M., Okura M., Kirikae T., Takamatsu D.,
RA Akiyama T.;
RT "Whole genome sequence of Melissococcus plutonius ATCC 35311.";
RL Submitted (APR-2011) 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; AP012200; BAK22031.1; -; Genomic_DNA.
DR RefSeq; WP_013774467.1; NC_015516.1.
DR AlphaFoldDB; F3YC03; -.
DR STRING; 940190.MPTP_1603; -.
DR KEGG; mps:MPTP_1603; -.
DR HOGENOM; CLU_013748_0_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000008456; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:BAK22031.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR036565-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2}; Pyruvate {ECO:0000313|EMBL:BAK22031.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008456};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..106
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 198..312
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 399..530
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR036565-2"
SQ SEQUENCE 556 AA; 61785 MW; AA6A8CC16980831D CRC64;
MYTVADYLLD IVKALGADEV FGVPGDYNLN FLDHITSRKD LRWLGNANEL NAAYMADGYA
RKKGFAAFVT TFGVGELSAL NGFAGSKAEH VPVLEIVGTP LTPVQKASAP IHHTFGDGNF
KKFEAAHQAL GFHTAHLTHE NAVEEINKLI KTMIETRQPA YLTIPMDVAE IQINQEIKNE
IPALIKEPME KTNSMLIELI MEQLNKAKSP IIFIGHELAR FKLENFVEKF IVNNNLPFTN
NGFSKGVVSE SLPQFIGTYN GAFSKHMTKE IIDQADLILL LGVQLTDLVT GNFTQSFNDT
KTIALNADHM RFFGKTENAQ QPYHFASTIQ ALSEETISTS IKTGTAFSKM INQPNGTDNK
LTQDFYDTAV AAFIQPEEVL FAEQGTSFLG LTMNELPNKA RYNAQPLWGS IGYTFPAMLG
SQVADPTSRN ILSIGEGSLQ MTIQEFGFAF RENLHPIILL IENSGYTIER FIHGMDESYN
DVAQLDYGKI PQLFGAKKSD YLLRYVTTEN ELLEAFSQAR ENTDKLILIR IELAEKDAPK
PLRDMVKAAE AAAKVN
//
