ID A0A0X3S5S0_9ACTN Unreviewed; 580 AA.
AC A0A0X3S5S0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KUJ39004.1};
GN ORFNames=ADL25_22515 {ECO:0000313|EMBL:KUJ39004.1};
OS Streptomyces sp. NRRL F-5122.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609098 {ECO:0000313|EMBL:KUJ39004.1, ECO:0000313|Proteomes:UP000054048};
RN [1] {ECO:0000313|Proteomes:UP000054048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL F-5122 {ECO:0000313|Proteomes:UP000054048};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUJ39004.1}.
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DR EMBL; LMWH01000228; KUJ39004.1; -; Genomic_DNA.
DR RefSeq; WP_059129561.1; NZ_LMWH01000228.1.
DR AlphaFoldDB; A0A0X3S5S0; -.
DR OrthoDB; 4959782at2; -.
DR Proteomes; UP000054048; 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; 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.
PE 3: Inferred from homology;
KW Pyruvate {ECO:0000313|EMBL:KUJ39004.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000054048};
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..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; 62656 MW; 482E05144812D5F4 CRC64;
MAKQNVADQF VDILARAGVK RLYGVVGDSL NPIVDAVRRN AALDWVHVRH EETAAFAAGA
EAQITGRLAA CAGSCGPGNL HLVNGLYDAH RSMAPVLALA SHIPSSEIGL GYFQETHPDR
LFQECSHYCE LISNPKQMPR LLQTAIQNAI GRSGVSVVAL PGDIADQPAP DKPVQTALVT
ARPTVRPSDA EIDKLVAMID EAERVTLFCG SGTAGAHAEV MELAGKIKSP VGHALRGKEW
IQYDNPFDVG MSGLLGYGAA YEATHECDLL ILLGTDFPYN AFLPDDVTIA QVDVRPENLG
RRSKLDLAVW GDVKETLRCL TPRLRPKQNR RFLDKMLKKH ADALEGVVKA YTRKVDKHVP
IHPEYVASVL DELAHPEAVF TVDTGMCNVW AARYISPNGR RRIIGSFSHG SMANALPMAI
GAQFTDRNRQ VVSISGDGGF SMLMGDFLTL VQLDLPVKVV LFNNSSLGMV ELEMMVAGLP
SYGTANQNPD FAAVARACGA YGIRVEKPKQ LPGALKDAFR HKGPALVDIV TDPNALSIPP
RISREMVTGF ALSASKVVLD GGVGRMVQMA RSNLRNVPRP
//