ID Q4L9J0_STAHJ Unreviewed; 546 AA.
AC Q4L9J0;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 02-AUG-2005, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=SH0376 {ECO:0000313|EMBL:BAE03685.1};
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808 {ECO:0000313|EMBL:BAE03685.1, ECO:0000313|Proteomes:UP000000543};
RN [1] {ECO:0000313|EMBL:BAE03685.1, ECO:0000313|Proteomes:UP000000543}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435 {ECO:0000313|EMBL:BAE03685.1,
RC ECO:0000313|Proteomes:UP000000543};
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE03685.1; -; Genomic_DNA.
DR RefSeq; WP_011274702.1; NC_007168.1.
DR AlphaFoldDB; Q4L9J0; -.
DR KEGG; sha:SH0376; -.
DR eggNOG; COG3961; Bacteria.
DR HOGENOM; CLU_013748_0_2_9; -.
DR OrthoDB; 4494979at2; -.
DR Proteomes; UP000000543; 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 GO; GO:0009234; P:menaquinone biosynthetic process; IEA:UniProtKB-KW.
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 Menaquinone biosynthesis {ECO:0000256|ARBA:ARBA00022428};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR036565-2};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 4..107
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 194..318
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 390..510
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 546 AA; 60513 MW; 5F509D5938425A4E CRC64;
MKQRVGQYLM DAVHRAGVDK IFGVPGDFNL AFLDDIVRHN GVEWVGTTNE LNGSYAADGY
ARINGLGVLV TTFGVGELSA VNGIAGSYAE RVPVIAITGA PTQAVEQAGK YVHHSLGEGR
FDSYQKMFEH ITTAQAYITA ENATTEIPRV INAAIHERRP VHIHLPIDVA MTEIEVDSEY
DVAPTADVNV ERYIDMVADK LRSASQPVII TGHEINSFHL HKALEQFVNQ THIPVAQLSL
GKGAFNEENP YYIGIYDGKI AEDQIKDYVD NSDAILNIGA KLTDSATAGF SYEFDIDDVV
MLNHHNFKLN ETIAEDVTLP SLIDGLNTID YRYEGSFPTF EKGSSKEVAL SDDILTQSTY
FDMMQHFIKD DDVLLAEQGT SFFGAYDLAL PKDMTFIGQP LWGSIGYTLP ATLGTQMANS
NRRNILLIGD GSLQLTVQEL STMIRQDIKP IIFVINNDGY TVERLIHGME ETYNDIRMWD
YKALPKVFGG DNVVVHDVKT SNDLQNVFDA INAAPEQLHF TEVTMKWDDA PAKLRDISKA
FAAQNK
//
