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Database: UniProt
Entry: A0A069K2F0_9ACTN
LinkDB: A0A069K2F0_9ACTN
Original site: A0A069K2F0_9ACTN 
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
//
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