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Database: UniProt
Entry: A0R4G6_MYCS2
LinkDB: A0R4G6_MYCS2
Original site: A0R4G6_MYCS2 
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
//
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