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Database: UniProt
Entry: W2EJI8_9ACTN
LinkDB: W2EJI8_9ACTN
Original site: W2EJI8_9ACTN 
ID   W2EJI8_9ACTN            Unreviewed;       580 AA.
AC   W2EJI8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:ETK31868.1};
GN   ORFNames=MPTA5024_32990 {ECO:0000313|EMBL:ETK31868.1};
OS   Microbispora sp. ATCC PTA-5024.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Microbispora.
OX   NCBI_TaxID=316330 {ECO:0000313|EMBL:ETK31868.1, ECO:0000313|Proteomes:UP000018869};
RN   [1] {ECO:0000313|EMBL:ETK31868.1, ECO:0000313|Proteomes:UP000018869}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC PTA-5024 {ECO:0000313|EMBL:ETK31868.1,
RC   ECO:0000313|Proteomes:UP000018869};
RX   PubMed=24459268;
RA   Sosio M., Gallo G., Pozzi R., Serina S., Monciardini P., Bera A.,
RA   Stegmann E., Weber T.;
RT   "Draft Genome Sequence of the Microbispora sp. Strain ATCC-PTA-5024,
RT   Producing the Lantibiotic NAI-107.";
RL   Genome Announc. 2:e01198-13(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETK31868.1}.
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DR   EMBL; AWEV01000266; ETK31868.1; -; Genomic_DNA.
DR   RefSeq; WP_036331303.1; NZ_KI866526.1.
DR   AlphaFoldDB; W2EJI8; -.
DR   STRING; 316330.MPTA5024_32990; -.
DR   PATRIC; fig|316330.3.peg.6348; -.
DR   HOGENOM; CLU_013748_3_0_11; -.
DR   OrthoDB; 4959782at2; -.
DR   Proteomes; UP000018869; Unassembled WGS sequence.
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:ETK31868.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018869};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          5..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          192..319
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          383..529
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   580 AA;  62539 MW;  523DEE3AE3A66E57 CRC64;
     MARQTIADQF VDILAQAGVR RIYGIVGDSL NPITDAVRRS PDVTWVQVRH EETAAFAAGA
     EAQITGRLAA CAGSCGPGNV HLVNGLYDAH RSMAPVLALA AHIPSSEIGT GYFQETHPDR
     LFAECSHYSE LISHPSQMPR VLQTAIQHAV GRSGVSVVSL PGDVAGREAP ERAAELALVT
     RRPAIRPGED EIAALARMVD AAQRVTLFCG SGTAGAHDEV MELAGRIKSP VGHALRGKEW
     IQYDNPFDVG MSGLLGYGAA YDAMHEADLL ILLGTDFPYR PFLPDDVRTV QVDVRPEHLG
     RRSKLDLAVW GDVRETLRAI IPRVREKTDR RFLDRMLKRH ADALEGVVAA YTRDVERHVP
     IHPEYVASVL DEEAADDAVF TVDTGMCNVW AARYLTPNGR RRVIGSFSHG SMANALPQAL
     GVQLAQPGRQ VVSVSGDGGF SMLMGDFLSL VQHRLPVKVV VFDNSSLGMV DLEMMVAGLP
     PYGTSYPHTD YAAIARAAGA FGVRVENPKE VADGLREAFR HDGPALVDVV TDPNALSIPP
     HITGEQLTGF ALSASKIIVS GGVGRMVQLA RANLRNIPRP
//
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