ID A0R4G6_MYCS2 Unreviewed; 768 AA.
AC A0R4G6;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE SubName: Full=Pyruvate decarboxylase {ECO:0000313|EMBL:ABK73595.1};
GN OrderedLocusNames=MSMEG_5826 {ECO:0000313|EMBL:ABK73595.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK73595.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK73595.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000480; ABK73595.1; -; Genomic_DNA.
DR RefSeq; YP_890054.1; NC_008596.1.
DR AlphaFoldDB; A0R4G6; -.
DR STRING; 246196.MSMEG_5826; -.
DR PaxDb; 246196-MSMEI_5668; -.
DR KEGG; msm:MSMEG_5826; -.
DR PATRIC; fig|246196.19.peg.5669; -.
DR eggNOG; COG0028; Bacteria.
DR OMA; ANWYARH; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000000757; 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:ABK73595.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 176..293
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 372..502
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 562..717
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 768 AA; 82590 MW; 68E7E47FF0A61BBC CRC64;
MSSPRTRSGI RVSRSSAELG AKSIGTTMHA TASSTAHGSP GSNHSPSSTD SASPTGIAMN
SIRNAALGWA PRKPPRTSVA STNSSTARMS SAICSALSVF SVTPRWSFIV KLMAMPVSTS
TIGAVSRRRC ISRDSRDHTA STTEIAISDS NTRKSLQPSH RFPRWRRGYH RQMSQTVAEY
VLQRLREWNV EQVFGYPGDG INGLIAAFGK DESAGPRFVQ TRHEEMAALA ATGYAKFSGN
VGVCIATSGP GAIHLLNGLY DAKLDHTPVV AIVGQTARSA MGGSYQQEVD LQALFSDVAS
DYLVEVNVAG QLPNALDRAF RTARARRAPT AVVIPSDLQE QPYEPPGHAF KQVPSSAPHD
AEPVLSPDPA ALQDAADVLN AGSKVAILIG QGARGAADEV TQVTDLLGAG VAKALLGKDV
LPDDLPFVTG SIGLLGTRPS YELMRDCDTL LIVGTNFPYS QFLPDYGQAR AVQIDIDGAN
IGMRYPTEVN IVAVAKTALA QLVPLLERKD DRSWQQSLEK GVAQWWETVE RQSMLKADPV
NPMRVVWELS SRLPEYAMVA GDSGSSTNWY ARCLKFTSTT RGSLSGTLAT MGSAVPYAIG
AKFAQPDRPV IALVGDGAMQ MNGLAELLTI RRYAHLWADP RMVICVFHNN DLAHVTWELR
AMGGAPKFEG SQSLPEVSYA DVARVMGLRC ITVDDPEQIG AAWDDALSAD EPVLLDVHTD
PEVPPIPPHV TYEQMKATAQ AFVKDPNGWH LFAEIAKNKA AELLPNRR
//