ID H6RCD5_NOCCG Unreviewed; 597 AA.
AC H6RCD5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Putative pyruvate decarboxylase {ECO:0000313|EMBL:CCF63875.1};
GN OrderedLocusNames=NOCYR_3109 {ECO:0000313|EMBL:CCF63875.1};
OS Nocardia cyriacigeorgica (strain GUH-2).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1127134 {ECO:0000313|EMBL:CCF63875.1, ECO:0000313|Proteomes:UP000008190};
RN [1] {ECO:0000313|EMBL:CCF63875.1, ECO:0000313|Proteomes:UP000008190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GUH-2 {ECO:0000313|EMBL:CCF63875.1,
RC ECO:0000313|Proteomes:UP000008190};
RX PubMed=22461543; DOI=10.1128/JB.00161-12;
RA Zoropogui A., Pujic P., Normand P., Barbe V., Beaman B., Beaman L.,
RA Boiron P., Colinon C., Deredjian A., Graindorge A., Mangenot S.,
RA Nazaret S., Neto M., Petit S., Roche D., Vallenet D., Rodriguez-Nava V.,
RA Richard Y., Cournoyer B., Blaha D.;
RT "Genome sequence of the human- and animal-pathogenic strain Nocardia
RT cyriacigeorgica GUH-2.";
RL J. Bacteriol. 194:2098-2099(2012).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; FO082843; CCF63875.1; -; Genomic_DNA.
DR RefSeq; WP_014351331.1; NC_016887.1.
DR AlphaFoldDB; H6RCD5; -.
DR STRING; 1127134.NOCYR_3109; -.
DR KEGG; ncy:NOCYR_3109; -.
DR eggNOG; COG0028; Bacteria.
DR HOGENOM; CLU_013748_3_0_11; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000008190; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02014; TPP_POX; 1.
DR CDD; cd07039; TPP_PYR_POX; 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; IPR047211; POXB-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; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR047212; TPP_POXB-like.
DR InterPro; IPR047210; TPP_PYR_POXB-like.
DR PANTHER; PTHR42981; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR PANTHER; PTHR42981:SF2; PYRUVATE DEHYDROGENASE [UBIQUINONE]; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:CCF63875.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008190};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 199..328
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 388..543
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 64365 MW; 3D974DEE2925991F CRC64;
MAEQVGDVLL RRLGEWGVRQ VFGYPGDGIN GLLAAWAEGV GHPQFVQARH EEMAAFEAVG
FAKFSGSVGV CAATGGPGAI HLLNGLYDAK LDHVPVVAIV GQTERSALGG SHQQEIDLPA
AFKDVCSAYS QLCVVPQQLP NVLDRAFRVA IAERAPTAVI VPADVFSLDY TAPAHEMKNV
PSSLGLSEGV VSPDAEALHR AAEILDAGER VAILVGQGAR GCAEELTRLA DLLGAGVAKA
LLGKDVLPDT EPWVTGSLGL LGTTASHFLM SEADTLLTIG SNFPYSEYLP EFGQVRGIQI
DRSGAWIGMR YPYEVSIVAD AKAALRELIP LVRRKRDRSW RKRVEQEVTQ WWRVADEVAM
LDADPINPMR IFSELSPQLP DNALVTADSG TSADWYARHL RFHGAMRGSL SGTLASMGCA
VPYAIGAKWA YPDRPAIALV GDGAMQMNGL AELITIARYW RQWQDPRLIV AVLHNNDLNQ
VTWELRGMHG APKFPDSQTL PDVDYAAFAR SLGLGARSID DPAELAGAWS SALASSRPVV
LDIVCDPNVA PIPPNTTFEQ FSSLARALLH GDEDAGPVLA HSVKQKTRRF FARHRNG
//
