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
//