ID A0A069K2F0_9ACTN Unreviewed; 580 AA.
AC A0A069K2F0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KDQ70410.1};
GN ORFNames=DT87_25395 {ECO:0000313|EMBL:KDQ70410.1};
OS Streptomyces sp. NTK 937.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ70410.1, ECO:0000313|Proteomes:UP000027475};
RN [1] {ECO:0000313|EMBL:KDQ70410.1, ECO:0000313|Proteomes:UP000027475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ70410.1,
RC ECO:0000313|Proteomes:UP000027475};
RA Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT producer of the benzoxazol antibiotic caboxamycin.";
RL Submitted (APR-2014) 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}.
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:KDQ70410.1}.
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DR EMBL; JJOB01000001; KDQ70410.1; -; Genomic_DNA.
DR RefSeq; WP_037880559.1; NZ_JJOB01000001.1.
DR AlphaFoldDB; A0A069K2F0; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000027475; 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:KDQ70410.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..114
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 192..320
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; 62870 MW; 9D9FC7CE2BB7CE62 CRC64;
MAKQNVSEQF VDILARAGVK RMYGVVGDSL NPVVDAVRRN PAMEWIQVRH EETAAFAAGA
EAQITGNLAV CAGSCGPGNL HLINGLYDAH RSMAPVLALA SHIPSSEIGL AYFQATHPEL
LFQECSHYNE MISNPQQMPR LLQTAIQHAI GQGGVSVVAM PGDIASQPAP EKSVEHALVT
SRPSVRPGDE EIDKLRRMVD EAERVTLFCG SGTAGAHAEV MEFAERVKAP VGHALRGKEW
IQYDNPFDVG MSGLLGYGAA YEATNECDLL ILLGTDFPYN AFLPTDVKIV QVDVRPEHLG
RRSKLDLAVW GDVRETLRCL TPQVRIKENR KFLDRMLKKH ADALEGVVKA YTRKVEKHVP
IHPEYVASML DELADDDAVF TVDTGMCNVW AARYLTPNGK RRVIGSFSHG SMANALPQAI
GAQFVDPNRQ VVSMSGDGGF SMLMGDFLTL VQYDLPVKVV LFNNSSLGMV ELEMLVAGLP
SFGTTNKNPD FAAIARAAGA YGVRVEKPKQ LEGALKDAFK HKGPALVDVV TDPNALSIPP
KISADMVTGF ALSASKIVLD GGVGRMLQMA RSNLRNVPRP
//